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391 results on '"Fransen, J.A.M."'

51. Detection of specific messenger RNA by electron microscopy in situ hybridization: implications for nucleocytoplasmic transport

Author

Macville, M.V.E., Wiesmeijer, K.C., Fransen, J.A.M., Dirks, R.W., and Raap, A.K.

Subjects
Intracellulair transport van glycoprotëinen in gepolariseerde epitheelcellen epitheelcellen, Intracellular transport of glycoproteins in polarized epithelial cells, GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries)
Abstract

Contains fulltext : 21773___.PDF (Publisher’s version ) (Open Access)

Published
1995

53. Rapid sequestration of DPPIV/CD26 and other cell surface in an autophagic-like compartment in Caco-2 cells treated with forsfokolin

Author

Baricault, L., Fransen, J.A.M., Garcia, M., Sapin, C., Codogno, P., Ginsel, L.A., and Trugnan, G.

Subjects
a molecular-cell biological [Expression of brush-border and lysosomal enzymes in polarized epithelial cells], een molecualir celbiologisch onderzoek [Expressie van brush-border en lysosomale enzymen in gepolariseerde epitheelcellen], GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries)
Abstract

Contains fulltext : 20994.PDF (Publisher’s version ) (Open Access)

Published
1995

54. Digital images lead the way

Author

Fransen, J.A.M., Ginsel, L.A., and Smith, G.

Abstract

Item does not contain fulltext

Published
1995

55. Golgi retention of mutant brush-border sucrase-isomaltase and mutant lysosomal a-glucosidase: quality control beyond the ER?

Author

Ouwendijk, J., Moolenaar, E.C., Wittpoth, M., Reuser, A.J.J., Ginsel, L.A., Naim, H.Y., and Fransen, J.A.M.

Subjects
a molecular-cell biological [Expression of brush-border and lysosomal enzymes in polarized epithelial cells], een molecualir celbiologisch onderzoek [Expressie van brush-border en lysosomale enzymen in gepolariseerde epitheelcellen]
Abstract

Item does not contain fulltext

Published
1995

56. Adenylate kinase 1 deficiency induces molecular and structural adaptations to support muscle energy metabolism.

Author

Janssen, E.E.W., Groof, A.J.C. de, Wijers-Rouw, M.J.P., Fransen, J.A.M., Dzeja, P.P., Terzic, A., Wieringa, B., Janssen, E.E.W., Groof, A.J.C. de, Wijers-Rouw, M.J.P., Fransen, J.A.M., Dzeja, P.P., Terzic, A., and Wieringa, B.

Abstract

Contains fulltext : 186091.pdf (Publisher’s version ) (Open Access), Genetic ablation of adenylate kinase 1 (AK1), a member of the AK family of phosphotransfer enzymes, disturbs muscle energetic economy and decreases tolerance to metabolic stress, despite rearrangements in alternative high energy phosphoryl transfer pathways. To define the mechanisms of this adaptive response, soleus and gastrocnemius muscles from AK1(-/-) mice were characterized by cDNA array profiling, Western blot and ultrastructural analysis. We demonstrate that AK1 deficiency induces fiber-type specific variation in groups of transcripts involved in glycolysis and mitochondrial metabolism and in gene products defining structural and myogenic events. This was associated with increased phosphotransfer capacities of the glycolytic enzymes pyruvate kinase and 3-phosphoglycerate kinase. Moreover, in AK1(-/-) mice, fast-twitch gastrocnemius, but not slow-twitch soleus, had an increase in adenine nucleotide translocator (ANT) and mitochondrial creatine kinase protein, along with a doubling of the intermyofibrillar mitochondrial volume. These results provide molecular evidence for wide-scale remodeling in AK1-deficient muscles aimed at preservation of efficient energetic communication between ATP producing and utilizing cellular sites.

Published
2003

57. Colocalisation of the protein tyrosine phosphatases PTP-SL and PTPBR7 with beta4-adaptin in neuronal cells.

Author

Dilaver, G., Schepens, J.T.G., Maagdenberg, A.M.J.M. van den, Wijers-Rouw, M.J.P., Pepers, B.A., Fransen, J.A.M., Hendriks, W.J.A.J., Dilaver, G., Schepens, J.T.G., Maagdenberg, A.M.J.M. van den, Wijers-Rouw, M.J.P., Pepers, B.A., Fransen, J.A.M., and Hendriks, W.J.A.J.

Abstract

Item does not contain fulltext, The mouse gene Ptprr encodes the neuronal protein tyrosine phosphatases PTP-SL and PTPBR7. These proteins differ in their N-terminal domains, with PTP-SL being a cytosolic, membrane-associated phosphatase and PTPBR7 a type I transmembrane protein. In this study, we further explored the nature of the PTP-SL-associated vesicles in neuronal cells using a panel of organelle markers and noted a comparable subcellular distribution for PTP-SL and the beta4-adaptin subunit of the AP4 complex. PTP-SL, PTPBR7 and beta4-adaptin are localised at the Golgi apparatus and at vesicles throughout the cytoplasm. Immunohistochemical analysis demonstrated that PTP-SL, PTPBR7 and beta4-adaptin are all endogenously expressed in brain. Interestingly, coexpression of PTP-SL and beta4-adaptin leads to an altered subcellular localisation for PTP-SL. Instead of the Golgi and vesicle-type staining pattern, still observable for beta4-adaptin, PTP-SL is now distributed throughout the cytoplasm. Although beta4-adaptin was found to interact with the phosphatase domain of PTP-SL and PTPBR7 in the yeast two-hybrid system, it failed to do so in transfected neuronal cells. Our data suggest that the tyrosine phosphatases PTP-SL and PTPBR7 may be involved in the formation and transport of AP4-coated vesicles or in the dephosphorylation of their transmembrane cargo molecules at or near the Golgi apparatus.

Published
2003

58. Decision-support in rheumatoid arthritis.

Author

Riel, P.L.C.M. van, Stucki, G., Michel, B.A., Fransen, J.A.M., Riel, P.L.C.M. van, Stucki, G., Michel, B.A., and Fransen, J.A.M.

Abstract

KUN, 08 mei 2003, Promotores : Riel, P.L.C.M. van, Stucki, G., Michel, B.A., Item does not contain fulltext

Published
2003

59. The creatine kinase system is essential for optimal refill of the sarcoplasmic reticulum Ca2+ store in skeletal muscle.

Author

Groof, A.J.C. de, Fransen, J.A.M., Errington, R., Willems, P.H.G.M., Wieringa, B., Koopman, W.J.H., Groof, A.J.C. de, Fransen, J.A.M., Errington, R., Willems, P.H.G.M., Wieringa, B., and Koopman, W.J.H.

Abstract

Item does not contain fulltext, Muscle function depends on an adequate ATP supply to sustain the energy consumption associated with Ca(2+) cycling and actomyosin sliding during contraction. In this regulation of energy homeostasis, the creatine kinase (CK) circuit for high energy phosphoryl transfer between ATP and phosphocreatine plays an important role. We earlier established a functional connection between the activity of the CK system and Ca(2+) homeostasis during depolarization and contractile activity of muscle. Here, we show how CK activity is coupled to the kinetics of spontaneous and electrically induced Ca(2+) transients in the sarcoplasm of myotubes. Using the UV ratiometric Ca(2+) probe Indo-1 and video-rate confocal microscopy in CK-proficient and -deficient cultured cells, we found that spontaneous and electrically induced transients were dependent on ryanodine-sensitive Ca(2+) release channels, sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase pumps, extracellular calcium, and functional mitochondria in both cell types. However, at increasing sarcoplasmic Ca(2+) load (induced by electrical stimulation at 0.1, 1, and 10 Hz), the Ca(2+) removal rate and the amount of Ca(2+) released per transient were gradually reduced in CK-deficient (but not wild-type) myotubes. We conclude that the CK/phosphocreatine circuit is essential for efficient delivery of ATP to the sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase pumps and thereby directly influences sarcoplasmic reticulum refilling and the kinetics of the sarcoplasmic Ca(2+) signals.

Published
2002

60. Accumulation of the amyloid-beta precursor protein in multivesicular body-like organelles.

Author

Verbeek, M.M., Otte-Holler, I., Fransen, J.A.M., Waal, R.M.W. de, Verbeek, M.M., Otte-Holler, I., Fransen, J.A.M., and Waal, R.M.W. de

Abstract

Item does not contain fulltext, It has been suggested that the successive proteolytic events leading to the production of the amyloid-beta protein from its precursor may take place at different intracellular locations. Using cultured human leptomeningeal smooth muscle cells and brain pericytes, we modulated the intracellular localization of the amyloid-beta precursor protein (APP) to study possible effects on its processing. By using immunofluorescence and immunoelectron microscopy we demonstrated that, under normal conditions, the APP is found in small intracellular vesicles, some of which were characterized as lysosomes. Both the cytokine interferon-gamma and the lysosomotropic drug chloroquine, but not the cytokines interleukin (IL)-1, IL-6, or tumor necrosis factor-alpha (TNF-alpha), induced an accumulation of APP in newly formed multivesicular body-like organelles. The secretion of the amyloid-beta precursor protein was slightly reduced by interferon-gamma or chloroquine. Double-labeling and tracer molecule uptake experiments showed that the multivesicular body-like organelles were part of the endocytic pathway. Our findings suggest that the multivesicular body-like organelles function as an intermediate organelle in the intracellular trafficking of the APP. Accumulation of the APP in this organelle is reflected by its reduced secretion from the cell.

Published
2002

61. The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen for presentation to T cells.

Author

Engering, A.J., Geijtenbeek, T.B., Vliet, S.J. van, Wijers-Rouw, M.J.P., Liempt, E. van, Demaurex, N., Lanzavecchia, A., Fransen, J.A.M., Figdor, C.G., Piguet, V., Kooyk, Y. van, Engering, A.J., Geijtenbeek, T.B., Vliet, S.J. van, Wijers-Rouw, M.J.P., Liempt, E. van, Demaurex, N., Lanzavecchia, A., Fransen, J.A.M., Figdor, C.G., Piguet, V., and Kooyk, Y. van

Abstract

Item does not contain fulltext, Dendritic cells (DCs) capture Ags or viruses in peripheral tissue to transport them to lymphoid organs to induce cellular T cell responses. Recently, a DC-specific C-type lectin was identified, DC-specific ICAM-grabbing non-integrin (DC-SIGN), that functions as cell adhesion receptor mediating both DC migration and T cell activation. DC-SIGN also functions as an HIV-1R that captures HIVgp120 and facilitates DC-induced HIV transmission of T cells. Internalization motifs in the cytoplasmic tail of DC-SIGN hint to a function of DC-SIGN as endocytic receptor. In this study we demonstrate that on DCs DC-SIGN is rapidly internalized upon binding of soluble ligand. Mutating a putative internalization motif in the cytoplasmic tail reduces ligand-induced internalization. Detailed analysis using ratio fluorescence imaging and electron microscopy showed that DC-SIGN-ligand complexes are targeted to late endosomes/lysosomes. Moreover, ligands internalized by DC-SIGN are efficiently processed and presented to CD4+ T cells. The distinct pattern of expression of C-type lectins on DCs in situ and their nonoverlapping Ag recognition profile hint to selective functions of these receptors to allow a DC to recognize a wide variety of Ags and to process these to induce T cell activation. These data point to a novel function of the adhesion receptor DC-SIGN as an efficient DC-specific Ag receptor that can be used as a target to induce viral and antitumor immunity.

Published
2002

68. A FERM domain governs apical confinement of PTP-BL in epithelial cells

Author

Cuppen, E.P.J.G., Wijers-Rouw, M.J.P., Schepens, J.T.G., Fransen, J.A.M., Wieringa, B., Hendriks, W.J.A.J., Cuppen, E.P.J.G., Wijers-Rouw, M.J.P., Schepens, J.T.G., Fransen, J.A.M., Wieringa, B., and Hendriks, W.J.A.J.

Abstract

Item does not contain fulltext

Published
1999

71. Anabolic steroids in part reverse glucocorticoid-induced alterations in rat diaphragm

Author

Balkom, R.H.H. van, Dekhuijzen, P.N.R., Folgering, H.T.M., Veerkamp, J.H., Moerkerk, H.T.B. van, Fransen, J.A.M., Herwaarden, C.L.A. van, Balkom, R.H.H. van, Dekhuijzen, P.N.R., Folgering, H.T.M., Veerkamp, J.H., Moerkerk, H.T.B. van, Fransen, J.A.M., and Herwaarden, C.L.A. van

Abstract

Item does not contain fulltext

Published
1998

73. Impaired Mammary Gland Development and Function in Mice Lacking LAR Receptor-like Tyrosine Phosphatase Activity

Author

Schaapveld, R.Q.J., Schepens, J.T.G., Robinson, G.W., Attema, J., Oerlemans, F.T.J.J., Fransen, J.A.M., Streuli, M., Wieringa, B., Hennighausen, L., Hendriks, W.J.A.J., Schaapveld, R.Q.J., Schepens, J.T.G., Robinson, G.W., Attema, J., Oerlemans, F.T.J.J., Fransen, J.A.M., Streuli, M., Wieringa, B., Hennighausen, L., and Hendriks, W.J.A.J.

Abstract

Contains fulltext : 26047___.PDF (publisher's version ) (Open Access)

Published
1997

81. Effects of different treatment regimens of methylprednisolone on rat diaphragm contractility, immunohistochemistry and biochemistry

Author

Balkom, R.H.H. van, Heijden, H.F.M. van der, Moerkerk, H.T.B. van, Veerkamp, J.H., Fransen, J.A.M., Ginsel, L.A., Folgering, H.T.M., Herwaarden, C.L.A. van, Dekhuijzen, P.N.R., Balkom, R.H.H. van, Heijden, H.F.M. van der, Moerkerk, H.T.B. van, Veerkamp, J.H., Fransen, J.A.M., Ginsel, L.A., Folgering, H.T.M., Herwaarden, C.L.A. van, and Dekhuijzen, P.N.R.

Abstract

Contains fulltext : 28408.pdf (publisher's version ) (Open Access)

Published
1996

83. Constitutive and inducible expression of SKALP/Elafin provides anti-elastase defense in human epithelia

Author

Pfundt, R., Ruissen, F. van, Vlijmen-Willems, I.M.J.J. van, Alkemade, J.A.C., Zeeuwen, P.L.J.M., Jap, P.H.K., Fransen, J.A.M., Croes, H.J.E., Dijkman, H.B.P.M., Erp, P.E.J. van, Schalkwijk, J., Pfundt, R., Ruissen, F. van, Vlijmen-Willems, I.M.J.J. van, Alkemade, J.A.C., Zeeuwen, P.L.J.M., Jap, P.H.K., Fransen, J.A.M., Croes, H.J.E., Dijkman, H.B.P.M., Erp, P.E.J. van, and Schalkwijk, J.

Abstract

Item does not contain fulltext

Published
1996

86. In vivo ANA is a fixation artifact : nucleosome-complexed antinucleosome autoantibodies bind to the cell surface and are internalized

Author

Kramers, K., Bruggen, M.C.J. van, Rijke-Schilder, G.P.M., Dijkman, H.B.P.M., Hylkema, M.N., Croes, H.J.E., Fransen, J.A.M., Assmann, K.J.M., Tax, W.J.M., Smeenk, R.J.T., Berden, J.H.M., Kramers, K., Bruggen, M.C.J. van, Rijke-Schilder, G.P.M., Dijkman, H.B.P.M., Hylkema, M.N., Croes, H.J.E., Fransen, J.A.M., Assmann, K.J.M., Tax, W.J.M., Smeenk, R.J.T., and Berden, J.H.M.

Abstract

Contains fulltext : 24092___.PDF (publisher's version ) (Open Access)

Published
1996

87. Congenital Sucrase-isomaltase deficiency

Author

Ouwendijk, J., Moolenaar, E.C., Peters, W.J.M, Hollenberg, C.P., Ginsel, L.A., Fransen, J.A.M., Ouwendijk, J., Moolenaar, E.C., Peters, W.J.M, Hollenberg, C.P., Ginsel, L.A., and Fransen, J.A.M.

Abstract

Item does not contain fulltext

Published
1996

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