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276 results on '"Jyrki Heino"'

101. Integrin α2β1 Mediates Isoform-Specific Activation of p38 and Upregulation of Collagen Gene Transcription by a Mechanism Involving the α2 Cytoplasmic Tail

Author

Johanna Ivaska, Veli-Matti Kähäri, Jyrki Heino, Hilkka Reunanen, Leeni Koivisto, and Jukka Westermarck

Subjects
collagen, Integrins, Receptors, Collagen, Transcription, Genetic, integrin, Integrin, cytoplasmic domain, CDC42, Biology, p38 MAPK, Transfection, CD49c, p38 Mitogen-Activated Protein Kinases, Collagen receptor, Tumor Cells, Cultured, Humans, Protein Isoforms, Cell Biology, Molecular biology, Cell biology, Up-Regulation, Enzyme Activation, Integrin alpha M, biology.protein, Integrin, beta 6, Original Article, Signal transduction, Mitogen-Activated Protein Kinases, ITGA6, Signal Transduction
Abstract

Two collagen receptors, integrins alpha1beta1 and alpha2beta1, can regulate distinct functions in cells. Ligation of alpha1beta1, unlike alpha2beta1, has been shown to result in recruitment of Shc and activation of the Ras/ERK pathway. To identify the downstream signaling molecules activated by alpha2beta1 integrin, we have overexpressed wild-type alpha2, or chimeric alpha2 subunit with alpha1 integrin cytoplasmic domain in human osteosarcoma cells (Saos-2) lacking endogenous alpha2beta1. The chimeric alpha2/alpha1 chain formed a functional heterodimer with beta1. In contrast to alpha2/alpha1 chimera, forced expression of alpha2 integrin resulted in upregulation of alpha1 (I) collagen gene transcription in response to three-dimensional collagen, indicating that the cytoplasmic domain of alpha2 integrin was required for signaling. Furthermore, signals mediated by alpha2beta1 integrin specifically activated the p38alpha isoform, and selective p38 inhibitors blocked upregulation of collagen gene transcription. Dominant negative mutants of Cdc42, MKK3, and MKK4 prevented alpha2beta1 integrin-mediated activation of p38alpha. RhoA had also some inhibitory effect, whereas dominant negative Rac was not effective. Our findings show the isoform-specific activation of p38 by alpha2beta1 integrin ligation and identify Cdc42, MKK3, and MKK4 as possible downstream effectors. These observations reveal a novel signaling mechanism of alpha2beta1 integrin that is distinct from ones previously described for other integrins.

Published
1999

102. Echovirus 1 Infection Induces both Stress- and Growth-Activated Mitogen-Activated Protein Kinase Pathways and Regulates the Transcription of Cellular Immediate-Early Genes

Author

Jyrki Heino, Pasi Huttunen, Timo Hyypiä, Pia Vihinen, and Liisa Nissinen

Subjects
Gene Expression Regulation, Viral, MAPK/ERK pathway, Transcription, Genetic, JUNB, p38 mitogen-activated protein kinases, Biology, Kidney, Antiviral Agents, 03 medical and health sciences, Virology, Proto-Oncogenes, Gene expression, Cell Adhesion, Tumor Cells, Cultured, Animals, Humans, RNA, Messenger, Enzyme Inhibitors, Phosphorylation, Protein kinase A, Genes, Immediate-Early, 030304 developmental biology, Regulation of gene expression, 0303 health sciences, 030302 biochemistry & molecular biology, Haplorhini, Isoxazoles, Semliki forest virus, Molecular biology, Enterovirus B, Human, 3. Good health, Cell biology, Transcription Factor AP-1, Poliovirus, Protein Biosynthesis, Mitogen-activated protein kinase, Calcium-Calmodulin-Dependent Protein Kinases, biology.protein, Receptors, Virus, Collagen, Sarcoma, Experimental
Abstract

We have previously shown that echovirus 1 (EV1) infection increases the mRNA levels of cellular immediate-early (IE) genes in host cells. Here we provide further evidence that the induction of junB, c-jun, and c-fos genes is due to active viral macromolecular synthesis rather than to the interaction of EV1 with its receptor, alpha2beta1 integrin. Nuclear run-on transcription assays indicated that differences in mRNA levels in infected and uninfected cells are brought about by regulation at the transcriptional level. EV1 infection induced the phosphorylation of both the stress-related p38 mitogen-activated protein kinase (MAPK) and the growth signal-related ERK1/2 MAPKs. Studies with selective MAPK inhibitors revealed that p38 was the main inducer of junB expression, whereas both MAPK pathways were involved in the induction of c-fos. Activation of AP-1 genes was also observed to occur during infections with other enteroviruses and with Semliki Forest A7(74) virus, suggesting that the phosphorylation of MAPKs and induction of AP-1 gene expression may be important regulators of host cell behavior during viral infections.

Published
1998

103. Transcription of α2 Integrin Gene in Osteosarcoma Cells Is Enhanced by Tumor Promoters

Author

Jukka Westermarck, Veli-Matti Kähäri, Liisa Nissinen, Leeni Koivisto, and Jyrki Heino

Subjects
Integrins, Time Factors, Transcription, Genetic, Integrin alpha3, Integrin, Integrin alpha2, CD18, Integrin alpha5, CD49c, CD49b, Collagen receptor, Antigens, CD, Okadaic Acid, Cell Adhesion, Tumor Cells, Cultured, Humans, Collagenases, RNA, Messenger, Osteosarcoma, biology, Activator (genetics), Integrin beta1, Cell Biology, Integrin alphaV, Blotting, Northern, Flow Cytometry, Molecular biology, Up-Regulation, Integrin alpha M, Carcinogens, biology.protein, Tetradecanoylphorbol Acetate, Integrin, beta 6, Collagen, Matrix Metalloproteinase 1
Abstract

Integrin alpha2beta1 is a heterodimeric transmembrane receptor for collagens. In osteogenic cells the expression of alpha2beta1 integrin is induced by both Kirsten sarcoma virus and chemical transformation. The association of alpha2 integrin with transformed cell phenotype was studied further by testing the effects of two tumor promoters, 12-O-tetradecanoylphorbol 13-acetate (TPA) and okadaic acid (OA), on human MG-63 osteosarcoma cells. TPA, an activator of protein kinase C, increased the cell surface expression of alpha2 integrin and the corresponding mRNA levels. Nuclear run-on assays indicated that TPA activated the transcription of alpha2 integrin gene. TPA also slightly increased the expression of alpha3 integrin but had no effect on the transcription of alpha5, alphav, or beta1 integrin subunits. OA, an inhibitor of serine/threonine phosphatases, increased alpha2 integrin gene transcription and mRNA levels, but in contrast to TPA, OA decreased alpha3 integrin expression. The increased expression of alpha2 integrin on TPA-treated MG-63 cells led to faster cell spreading on type I collagen. Our results link the enhanced transcription of alpha2 integrin gene to tumor progression and show the independent regulation of alpha2 integrin compared to other integrin genes.

Published
1998

104. Suprabasal expression of epidermal alpha2beta1 and alpha3beta1 integrins in skin treated with topical retinoic acid

Author

Lari Häkkinen, Nina Johansson, Jyrki Heino, Juha Peltonen, Veli-Matti Kähäri, Jukka Westermarck, and Heikki Aho

Subjects
Adult, Keratinocytes, Male, Integrins, Pathology, medicine.medical_specialty, Receptors, Collagen, Integrin, Cell Culture Techniques, Fluorescent Antibody Technique, Alpha (ethology), Tretinoin, Human skin, Dermatology, Administration, Cutaneous, Receptors, Laminin, Keratolytic Agents, medicine, Humans, Beta (finance), integumentary system, biology, Integrin alpha3beta1, Molecular biology, Fibronectin, HaCaT, medicine.anatomical_structure, biology.protein, Epidermis, Carrier Proteins, Keratinocyte
Abstract

In normal adult human skin, expression of epidermal integrins is confined to keratinocytes in the basal layer. However, suprabasal expression of alpha 2, alpha 3 and beta 1 integrin subunits is noted in hyperproliferative epidermis in wound repair and psoriasis. In this study, we examined the effect of topical all-trans-retinoic acid (RA), known to induce epidermal hyperplasia, on expression of integrins in human epidermis. Immunostaining of vehicle-treated skin revealed expression of alpha 2, alpha 3 and beta 1, as well as alpha 6 and beta 4 integrin subunits entirely on basal keratinocytes. Topical application of RA (0.1%) for 2 weeks resulted in marked suprabasal expression of alpha 2, alpha 3 and beta 1 integrin subunits, whereas alpha 6 and beta 4 staining remained on basal keratinocytes. Staining for putative ligands of alpha 2 beta 1 and alpha 3 beta 1 integrins, i.e. type IV collagen, laminin-5 and fibronectin, was not detected in the epidermal layer in RA- or vehicle-treated skin. Treatment of HaCaT keratinocytes in culture with RA (1 mumol/L) enhanced alpha 2 and beta 1 mRNA abundance. Furthermore, RA slightly up-regulated the expression of alpha 2, alpha 3 and beta 1 integrin subunits on primary epidermal keratinocytes and HaCaT cells in culture with no effect on cell proliferation. These results provide evidence that RA-elicited epidermal hyperplasia is associated with aberrant suprabasal expression of alpha 2 beta 1 and alpha 3 beta 1 integrins, and that this also involves direct stimulation of keratinocyte integrin expression by RA.

Published
1998

105. Echovirus 1 replication, not only virus binding to its receptor, VLA-2, is required for the induction of cellular immediate-early genes

Author

Timo Hyypiä, Jyrki Heino, and Pasi Huttunen

Subjects
Integrins, Receptors, Collagen, Echovirus, viruses, Immunology, Integrin, Biology, Virus Replication, medicine.disease_cause, Microbiology, Virus, Virology, medicine, Humans, Receptor, Genes, Immediate-Early, Gene, Interleukin-6, Enterovirus B, Human, Transcription Factor AP-1, Gene Expression Regulation, Viral replication, Cell culture, Insect Science, biology.protein, Receptors, Virus, Signal transduction, Research Article
Abstract

Induction of immediate-early genes c-jun, junB, and c-fos was demonstrated during echovirus 1 infection in a human osteogenic sarcoma (HOS) cell line. Tenfold induction was seen at 10 h postinfection, corresponding approximately to the end of the first replication cycle of the virus. Echovirus 1 uses VLA-2 integrin as its cellular receptor, and ligand binding by integrin is known to trigger signal transduction pathways ultimately activating immediate-early genes. In the present study, however, VLA-2 binding alone was not sufficient to induce their expression; viral replication was needed. This conclusion was based on the observations that no stimulation of the immediate-early genes occurred in the MG-63 cell line where the virus attached only to VLA-2 but was not able to replicate and that induction of these genes was observed when the HOS cells were infected with echovirus type 7, known to use a different cellular receptor. Induction was not seen in the presence of the antiviral compound WIN 54954, which evidently inhibits the uncoating but not receptor binding of echovirus 1, suggesting that viral replication triggers the activation of the immediate-early genes. The induction of these genes may have a role in viral replication and in the pathogenesis of infection.

Published
1997

106. Biological Agents and Cell Therapies in Periodontal Regeneration

Author

Yi Yang, Jyrki Heino, Hannu Larjava, Lari Häkkinen, and Edward E. Putnins

Subjects
Clinical trial, medicine.medical_specialty, Pathology, Regeneration (biology), Critical factors, medicine, Biology, Intensive care medicine
Abstract

Regeneration of periodontal structures is a complex challenge for periodontal wound healing. As by Wikesjo et al. in this issue, wound space provision, primary stability, and healing by primary intention serve as critical factors for attempts to regenerate the periodontium. Barrier membranes for space maintenance can be cumbersome to use in a clinical setting and have proven to provide only partial success in regenerative therapies. Not surprisingly, investigators and clinicians have started to search for biological molecules and cell technologies that could help to either speed up or modify the healing process that depends on migration and differentiation of several different cell populations. In this chapter, we will briefly review the technologies that are currently in use or in clinical trials. Readers are welcome to review in-depth publications for further details on this complex and evolving area of research.

Published
2013

107. Integrins in Wound Healing

Author

Hannu Larjava, Jyrki Heino, Leeni Koivisto, and Lari Häkkinen

Subjects
biology, business.industry, Integrin, Proteolytic enzymes, Granulation tissue, Cell migration, Critical Care and Intensive Care Medicine, medicine.disease, Cell biology, Extracellular matrix, medicine.anatomical_structure, Fibrosis, Comprehensive Invited Review, Immunology, Emergency Medicine, medicine, biology.protein, Wound healing, Receptor, business
Abstract

Significance: Regulation of cell adhesions during tissue repair is fundamentally important for cell migration, proliferation, and protein production. All cells interact with extracellular matrix proteins with cell surface integrin receptors that convey signals from the environment into the nucleus, regulating gene expression and cell behavior. Integrins also interact with a variety of other proteins, such as growth factors, their receptors, and proteolytic enzymes. Re-epithelialization and granulation tissue formation are crucially dependent on the temporospatial function of multiple integrins. This review explains how integrins function in wound repair. Recent Advances: Certain integrins can activate latent transforming growth factor beta-1 (TGF-β1) that modulates wound inflammation and granulation tissue formation. Dysregulation of TGF-β1 function is associated with scarring and fibrotic disorders. Therefore, these integrins represent targets for therapeutic intervention in fibrosis. Critical Issues: In...

Published
2013

108. Evolution of Cell Adhesion to Extracellular Matrix

Author

Bhanupratap Singh Chouhan, Tomi T. Airenne, Konstantin Denessiouk, Jyrki Heino, Mark S. Johnson, and Jarmo Käpylä

Subjects
Extracellular matrix, Fibronectin, Focal adhesion, Cell adhesion molecule, Adhesome, Integrin, biology.protein, Biology, Cell adhesion, Collagen receptor, Cell biology
Abstract

The extracellular matrix and cell adhesion receptors, especially the integrins, have played a major role in the emergence of multicellular animals. The members of the integrin family can be found in all present-day metazoans, and they actually predate the origin of the animal kingdom. Chordate integrins show structural and functional diversity, and they gather around themselves a large number of adaptor and signaling proteins, an adhesome. This chapter reviews the early evolution of integrin-type protein domains, the origin of integrin-dependent adhesion mechanisms, and the later developments in chordate-specific integrins.

Published
2013

109. Critical role for αvβ6 integrin in enamel biomineralization

Author

Lari Häkkinen, Kristiina Heikinheimo, Leeni Koivisto, Gethin Owen, Markus Haapasalo, Jyrki Heino, Charles E. Smith, Leena Kytömäki, Marc D. McKee, Guoqiao Jiang, Yanshuang Xie, Toshiyuki Yoshida, Colin Wiebe, Hannu Larjava, and Leila Mohazab

Subjects
Integrins, Amelogenesis Imperfecta, Integrin, Matrix (biology), 03 medical and health sciences, Mice, 0302 clinical medicine, stomatognathic system, Antigens, Neoplasm, medicine, Ameloblasts, Cell Adhesion, Animals, Dental Enamel, Tooth Demineralization, Reduced enamel epithelium, Cells, Cultured, 030304 developmental biology, Mice, Knockout, 0303 health sciences, Enamel paint, biology, Amelogenin, 030206 dentistry, Cell Biology, Amelogenesis, Anatomy, Tooth Attrition, Tooth enamel, Cell biology, Extracellular Matrix, stomatognathic diseases, medicine.anatomical_structure, visual_art, visual_art.visual_art_medium, biology.protein, Ameloblast, Tooth Calcification
Abstract

Tooth enamel has the highest degree of biomineralization of all vertebrate hard tissues. During the secretory stage of enamel formation, ameloblasts deposit an extracellular matrix that is in direct contact with ameloblast plasma membrane. Although it is known that integrins mediate cell-matrix adhesion and regulate cell signaling in most cell types, the receptors that regulate ameloblast adhesion and matrix production are not well characterized. Thus, we hypothesized that αvβ6 integrin is expressed in ameloblasts where it regulates biomineralization of enamel. Human and mouse ameloblasts were found to express both β6 integrin mRNA and protein. The maxillary incisors of Itgb6−/− mice lacked yellow pigment and their mandibular incisors appeared chalky and rounded. Molars of Itgb6−/− mice showed signs of reduced mineralization and severe attrition. The mineral-to-protein ratio in the incisors was significantly reduced in Itgb6−/− enamel, mimicking hypomineralized amelogenesis imperfecta. Interestingly, amelogenin-rich extracellular matrix abnormally accumulated between the ameloblast layer of Itgb6−/− mouse incisors and the forming enamel surface, and also between ameloblasts. This accumulation was related to increased synthesis of amelogenin, rather than to reduced removal of the matrix proteins. This was confirmed in cultured ameloblast-like cells, which did not use αvβ6 integrin as an endocytosis receptor for amelogenins, although it participated in cell adhesion on this matrix indirectly via endogenously produced matrix proteins. In summary, integrin αvβ6 is expressed by ameloblasts and it plays a crucial role in regulating amelogenin deposition/turnover and subsequent enamel biomineralization.

Published
2012

110. Novel α2β1 integrin inhibitors reveal that integrin binding to collagen under shear stress conditions does not require receptor preactivation

Author

Kalle Sipilä, Maria Salmela, Liisa Nissinen, Anne Marjamäki, Johanna Jokinen, Olli T. Pentikäinen, Jarkko T. Koivunen, Marjo Pihlavisto, Jonna Nieminen, Jarmo Käpylä, and Jyrki Heino

Subjects
Blood Platelets, Integrin, Platelet Membrane Glycoproteins, Biochemistry, CD49c, Collagen Type I, Collagen receptor, Cell Line, Mice, Cell Adhesion, Animals, Humans, Binding site, Receptor, Molecular Biology, Integrin binding, Sulfonamides, biology, Molecular Structure, Chemistry, ta1182, Cell Biology, Mice, Inbred C57BL, Integrin alpha M, biology.protein, Biophysics, Integrin, beta 6, Stress, Mechanical, Integrin alpha2beta1, Protein Binding
Abstract

The interaction between α2β1 integrin (GPIa/IIa, VLA-2) and vascular collagen is one of the initiating events in thrombus formation. Here, we describe two structurally similar sulfonamide derivatives, BTT-3033 and BTT-3034, and show that, under static conditions, they have an almost identical effect on α2-expressing CHO cell adhesion to collagen I, but only BTT-3033 blocks platelet attachment under flow (90 dynes/cm(2)). Differential scanning fluorimetry showed that both molecules bind to the α2I domain of the recombinant α2 subunit. To further study integrin binding mechanism(s) of the two sulfonamides, we created an α2 Y285F mutant containing a substitution near the metal ion-dependent adhesion site motif in the α2I domain. The action of BTT-3033, unlike that of BTT-3034, was dependent on Tyr-285. In static conditions BTT-3034, but not BTT-3033, inhibited collagen binding by an α2 variant carrying a conformationally activating E318W mutation. Conversely, in under flow conditions (90 dynes/cm(2)) BTT-3033, but not BTT-3034, inhibited collagen binding by an α2 variant expressing E336A loss-of-function mutation. Thus, the binding sites for BTT-3033 and BTT-3034 are differentially available in distinct integrin conformations. Therefore, these sulfonamides can be used to study the biological role of different functional stages of α2β1. Furthermore, only the inhibitor that recognized the non-activated conformation of α2β1 integrin under shear stress conditions effectively blocked platelet adhesion, suggesting that the initial interaction between integrin and collagen takes place prior to receptor activation.

Published
2012

111. Integrin α2β1 Is a Positive Regulator of Collagenase (MMP-1) and Collagen α1(I) Gene Expression

Author

Jukka Westermarck, Veli-Matti Kähäri, Jyrki Heino, Terhi Riikonen, Leeni Koivisto, and Arsi Broberg

Subjects
biology, Chemistry, Integrin, Cell Biology, Transfection, Biochemistry, Molecular biology, Collagen receptor, Collagen, type I, alpha 1, Integrin alpha M, Collagenase, medicine, biology.protein, Integrin, beta 6, Molecular Biology, Type I collagen, medicine.drug
Abstract

A classical model for studying the effects of extracellular matrix is to culture cells inside a three-dimensional collagen gel. When surrounded by fibrillar collagen, many cell types decrease the production of type I collagen, and the expression of interstitial collagenase (matrix metalloproteinase-1; MMP-1) is simultaneously induced. To study the role of the collagen-binding integrins α1β1 and α2β1 in this process, we used three different osteogenic cell lines with distinct patterns of putative collagen receptors: HOS cells, which express only α1β1 integrin, MG-63 cells, which express only α2β1 integrin, and KHOS-240 cells, which express both. Inside collagen gels, α1(I) collagen mRNA levels were decreased in HOS and KHOS-240 cells but not in MG-63 cells. In contrast, MMP-1 expression was induced in KHOS-240 and MG-63 cells but not in HOS cells. Transfection of MG-63 cells with α2 integrin cDNA produced cell clones overexpressing α2β1 integrin. Transfection of MG-63 cells with α2 integrin cDNA in an antisense orientation reduced the expression level of α2 integrin. These cell clones showed induction and reduction of mRNA levels for MMP-1, respectively. HOS cells normally lacking α2β1 integrin were forced to express it, and this prevented the down-regulation in the levels of α1(I) collagen mRNA when cells were grown inside collagen gels. The data indicate that the level of MMP-1 expression is regulated by the collagen receptor α2β1 integrin. The down-regulation of collagen α1(I) is mediated by another receptor. Integrin α2β1 may compete with it and thus be a positive regulator of collagen synthesis.

Published
1995

112. Insulin-like Growth Factor Receptor Type I (IGF1R) Signaling and Inflammation

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

113. Icmt (Isoprenylcysteine Carboxyl Methyltransferase)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

114. Integrin Alpha 4

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

115. IP3 Receptor–Associated cGMP Kinase Substrate A

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

116. Intersectin

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

117. Inositol Polyphosphate-5-Phosphatase, 145 kDa

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

118. Interleukin-1 Signal Transducer

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

119. IFN-Gamma

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

120. Integrin Alpha 11

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

121. Ionotropic Glutamate Receptors (AMPA, Kainate and NMDA Receptors)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

122. int-2

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

123. Interferon Regulatory Factor 5, IRF5

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

124. Interferon-Inducible eIF2α Kinase

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

125. Inositol Trisphosphate 5/6-Kinase

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

126. Inositol 1,4,5-trisphosphate-associated cGMP kinase substrate

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

127. Inositol 3,4,5,6-Tetrakisphosphate 1-Kinase

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

128. Integrin-Associated Protein

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

129. ITPK1 (Inositol 1,3,4-Triphosphate 5/6 Kinase)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

130. IkB-zeta

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

131. Integrin Alpha 4 (Itga 4)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

132. IFN-γ

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

133. Isl 1

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

134. Inhibitor of DNA Binding 4 (ID4)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

135. IL-1 Inducible Nuclear Ankyrin-Repeat Protein (INAP)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

136. Immunity-Related GTPases (IRG)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

137. Inhibitor of Apoptosis (IAP) Proteins

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

138. Melanoma-Associated Cancer-Testis Antigen 16 (CT16) Regulates the Expression of Apoptotic and Antiapoptotic Genes and Promotes Cell Survival

Author

Hannu Larjava, Camilla Nylund, Laura L. Elo, Pia Vihinen, Laura Laato, Aleksi Heino, Pekka Rappu, Jyrki Heino, Markku Kallajoki, Eveliina Pakula, Seppo Pyrhönen, and Gethin Owen

Subjects
Melanomas, Small interfering RNA, Skin Neoplasms, lcsh:Medicine, Apoptosis, Biochemistry, Malignant transformation, Metastasis, Gene expression, Molecular Cell Biology, Basic Cancer Research, Promoter Regions, Genetic, lcsh:Science, Melanoma, Skin Tumors, Regulation of gene expression, Multidisciplinary, Cell Death, Systems Biology, Malignant Melanoma, Immunohistochemistry, Oncology, DNA methylation, Cytochemistry, Cancer/testis antigens, Medicine, Melanoma-Specific Antigens, Immunocytochemistry, Research Article, Cell Survival, Blotting, Western, Malignant Skin Neoplasms, Dermatology, Biology, In Vitro Techniques, Real-Time Polymerase Chain Reaction, ta3111, Cell Line, Tumor, medicine, Gene silencing, Humans, Cell Proliferation, lcsh:R, ta1182, Proteins, Cancers and Neoplasms, medicine.disease, ta3122, Molecular biology, Cancer research, lcsh:Q, Tumor Suppressor Protein p53
Abstract

Cancer-testis (CT) antigens are predominantly expressed in testis or placenta, but absent in most adult tissues. During malignant transformation CT genes are often activated. CT antigen 16 (CT16, PAGE5) is frequently expressed in advanced melanoma but its biological function has been unknown. To examine the role of CT16 in cell survival we knocked it down in A2058 melanoma cells using specific siRNAs and exposed the cells to cancer drug cisplatin known to induce apoptosis. As a result, cell survival was markedly decreased. To study the effects of CT16 on cell survival in more detail, the cellular gene expression profiles were investigated after CT16 silencing in CT16 positive A2058 melanoma cells, as well as after CT16 overexpression in CT16 negative WM-266-4 melanoma cells. Among the 11 genes both upregulated by CT16 silencing and downregulated by CT16 overexpression or vice versa, 4 genes were potentially apoptotic or antiapoptotic genes. CT16 was recognized as a positive regulator of antiapoptotic metallothionein 2A and interleukin 8 genes, whereas it inhibited the expression of apoptosis inducing dickkopf 1 (DKK1) gene. In addition CT16 enhanced the expression of fatty acid binding protein 7, a known promoter of melanoma progression. The effect of CT16 on DKK1 expression was p53 independent. Furthermore, CT16 did not regulate apoptotic genes via DNA methylation. In twenty melanoma metastasis tissue samples average DKK1 mRNA level was shown to be significantly (p

Published
2012

139. Interleukin-7

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

140. IFN-β2

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

141. Insulin-Like Growth Factor Receptor Type I (IGF1R)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

142. Integrin-Associated Signal Transducer

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

143. Integrin Alpha V (ITGAV)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

144. Integrin α2 (ITGA2)

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

145. Immune IFN

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

146. IP3 Receptors

Author

Kathryn M. Appleton, Ian Cushman, Yuri K. Peterson, Balachandran Manavalan, Shaherin Basith, Sangdun Choi, Akihiro Kimura, Tetsuji Naka, Tadamitsu Kishimoto, Benedict Seddon, Maria Traver, Gregory A. Taylor, Mads Gyrd-Hansen, Giovanni Blandino, Giulia Fontemaggi, Michael A. Grillo, Peter Koulen, Alexander Annenkov, Cédric Zeltz, Donald Gullberg, Maria Mittelbrunn, Francisco Sánchez-Madrid, Bethany A. Kerr, Tatiana V. Byzova, Jyrki Heino, Fan-ching Lin, Howard A. Young, Colin W. Taylor, Betsy J. Barnes, Yixing Zhou, Tobias M. H. Schenk, Stephen B. Shears, Ameet S. Sengar, Michael W. Salter, and Sean E. Egan

Published
2012

147. Cooperation between integrins and growth factor receptors in signaling and endocytosis

Author

Johanna Ivaska and Jyrki Heino

Subjects
Models, Molecular, Cell signaling, Integrins, Protein Conformation, Integrin, Biology, Endocytosis, Extracellular matrix, 03 medical and health sciences, 0302 clinical medicine, Growth factor receptor, Animals, Humans, Receptors, Growth Factor, Angiogenic Proteins, Receptor, 030304 developmental biology, 0303 health sciences, Multicellular animals, Cell Membrane, Cell Biology, Cell biology, Extracellular Matrix, Intracellular signal transduction, Protein Subunits, 030220 oncology & carcinogenesis, biology.protein, Intercellular Signaling Peptides and Proteins, Developmental Biology, Signal Transduction
Abstract

All multicellular animals express receptors for growth factors (GFs) and extracellular matrix (ECM) molecules. Integrin-type ECM receptors anchor cells to their surroundings and concomitantly activate intracellular signal transduction pathways. The same signaling mechanisms are regulated by GF receptors (GFRs). Recently, intensive research efforts have revealed novel mechanisms describing how the two receptor systems collaborate at many different levels. Integrins can directly bind to GFs and promote their activation. Adhesion receptors also organize signaling platforms and assist GFRs or even activate them via ligand-independent mechanisms. Furthermore, integrins can orchestrate endocytosis and recycling of GFRs. Here, we review the present knowledge about the interplay between integrins and GFRs and discuss recent ideas of how this collaboration may explain some previous controversies in integrin research.

Published
2011
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148. Collagen XXIII, novel ligand for integrin alpha2beta1 in the epidermis

Author

Johannes A. Eble, Guido Veit, Stephan Niland, Jarmo Käpylä, Manon C. Zweers, Akemi Ishada-Yamamoto, Jyrki Heino, Beate Eckes, Manuel Koch, Daniela Zwolanek, and Thomas Krieg

Subjects
Keratinocytes, Integrin, Glycobiology and Extracellular Matrices, Ligands, Biochemistry, Laminin 111, Collagen receptor, Cell Line, Focal adhesion, Extracellular matrix, medicine, Cell Adhesion, Humans, Cell adhesion, Molecular Biology, Basement membrane, Focal Adhesions, biology, Chemistry, Cell Biology, Surface Plasmon Resonance, Immunohistochemistry, Cell biology, medicine.anatomical_structure, Integrin alpha M, biology.protein, Collagen, Epidermis, Integrin alpha2beta1
Abstract

Cellular receptors for collagens belong to the family of β(1) integrins. In the epidermis, integrin α(2)β(1) is the only collagen-binding integrin present. Its expression is restricted to basal keratinocytes with uniform distribution on the cell surface of those cells. Although α(2)β(1) receptors localized at the basal surface interact with basement membrane proteins collagen IV and laminin 111 and 332, no interaction partners have been reported for these integrin molecules at the lateral and apical membranes of basal keratinocytes. Solid phase binding and surface plasmon resonance spectroscopy demonstrate that collagen XXIII, a member of the transmembrane collagens, directly interacts with integrin α(2)β(1) in an ion- and conformation-dependent manner. The two proteins co-localize on the surface of basal keratinocytes. Furthermore, collagen XXIII is sufficient to induce adhesion and spreading of keratinocytes, a process that is significantly reduced in the absence of functional integrin α(2)β(1).

Published
2011

149. Exploring scarless healing of oral soft tissues

Author

Hannu, Larjava, Colin, Wiebe, Corrie, Gallant-Behm, David A, Hart, Jyrki, Heino, and Lari, Häkkinen

Subjects
Cicatrix, Disease Models, Animal, Wound Healing, Swine, Mouth Mucosa, Animals, Humans, Regeneration
Abstract

Our research group is comparing clinical, histological and molecular healing profiles of oral and skin wounds using human and pig models. The goal is to determine the molecular cues that lead to scarless healing in the oral mucosa and use that information to develop scar prevention therapies for skin and prevent aberrant wound healing in the oral cavity. Wound healing in human and pig palatal mucosa is almost identical, and scar formation is reduced in oral wounds compared with skin. The striking difference between these tissues is transient and rapidly resolving inflammation in oral wounds compared with long-lasting inflammation in the skin wounds. Currently, we are looking at wound transcriptomes (genes differentially regulated) and proteomes (a set of proteins) to investigate how these wound healing responses in skin and oral mucosa are regulated at the molecular level.

Published
2011

150. Integrin-type Extracellular Matrix Receptors in Cancer and Inflammation

Author

Jyrki Heino

Subjects
Inflammation, Integrins, biology, Cell adhesion molecule, Integrin, General Medicine, Intercellular adhesion molecule, Extracellular Matrix, Cell biology, Arthritis, Rheumatoid, Fibronectin, Focal adhesion, Neoplasms, Chronic Disease, Cell Adhesion, biology.protein, Extracellular, Humans, Signal transduction, Cell adhesion
Abstract

The integrins are a large family of cell adhesion receptors, involved in cell-cell and cell-matrix interactions. At present, 20 different integrin heterodimers are known. Integrins participate in a complex apparatus anchoring cells to their surroundings and transducting signals into the cells. These signals regulate many important aspects of cell behaviour, including growth, differentiation, and phenotype. This is an overview of the molecular and cellular biology of the integrin-type extracellular matrix receptors. Integrins may play a central role in the healing process of tissue injuries, and in many diseases, especially in human cancer.

Published
1993

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