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1,169 results on '"Iozzo, Renato V."'

10. A role for decorin in improving motor deficits after traumatic brain injury

Author

Oshima, Kaori, primary, Siddiqui, Noah, additional, Orfila, James E., additional, Carter, Danelle, additional, Laing, Justin, additional, Han, Xiaorui, additional, Zakharevich, Igor, additional, Iozzo, Renato V, additional, Ghasabayan, Arsen, additional, Moore, Hunter, additional, Zhang, Fuming, additional, Linhardt, Robert J, additional, Moore, Ernest E, additional, Quillinan, Nidia, additional, Schmidt, Eric P, additional, Herson, Paco S, additional, and Hippensteel, Joseph A, additional

Published
2023
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11. The injury response of aged tendons in the absence of biglycan and decorin

Author

Dunkman, Andrew A, Buckley, Mark R, Mienaltowski, Michael J, Adams, Sheila M, Thomas, Stephen J, Kumar, Akash, Beason, David P, Iozzo, Renato V, Birk, David E, and Soslowsky, Louis J

Subjects
Biological Sciences, Physical Injury - Accidents and Adverse Effects, Aging, 2.1 Biological and endogenous factors, Aetiology, Musculoskeletal, Animals, Biglycan, Biomechanical Phenomena, DNA Primers, Decorin, Female, Mice, Mice, Inbred C57BL, Mice, Transgenic, Microscopy, Electron, Transmission, Patellar Ligament, Reverse Transcriptase Polymerase Chain Reaction, Tendon Injuries, Wound Healing, Tendon, Injury, Proteoglycan, Biochemistry & Molecular Biology, Biological sciences
Abstract

Recent studies have demonstrated that the small leucine-rich proteoglycans (SLRPs) biglycan and decorin impact tendon development, aging and healing in mature mice. However, despite the increased risk of tendon injury in the elderly, the role of SLRPs in tendon repair has not been investigated in aged animals. Therefore, our objective was to elucidate the influences of bigylcan and decorin on tendon healing in aged mice to relate our findings to previous work in mature mice. Since the processes of aging and healing are known to interact, our hypothesis was that aging mediates the role of biglycan and decorin on tendon healing. Patellar tendons from wild-type, biglycan-null and decorin-null mice were injured at 270 days using an established model. At 3 and 6 weeks post-surgery, structural, mechanical and biochemical analyses were performed and compared to uninjured controls. Early stage healing was inferior in biglycan-null and decorin-null mice as compared to wild type. However, tendons of all genotypes failed to exhibit improved mechanical properties between 3 and 6 weeks post-injury. In contrast, in a previous investigation of tendon healing in mature (i.e., 120 day-old) mice, only biglycan-null mice were deficient in early stage healing while decorin-null mice were deficient in late-stage healing. These results confirm that the impact of SLRPs on tendon healing is mediated by age and could inform future age-specific therapies for enhancing tendon healing.

Published
2014

12. The Tendon Injury Response is Influenced by Decorin and Biglycan

Author

Dunkman, Andrew A, Buckley, Mark R, Mienaltowski, Michael J, Adams, Sheila M, Thomas, Stephen J, Satchell, Lauren, Kumar, Akash, Pathmanathan, Lydia, Beason, David P, Iozzo, Renato V, Birk, David E, and Soslowsky, Louis J

Subjects
Physical Injury - Accidents and Adverse Effects, Aetiology, 2.1 Biological and endogenous factors, Musculoskeletal, Animals, Biglycan, Collagen, Decorin, Disease Models, Animal, Female, Gene Expression Regulation, Mice, Mice, Knockout, Patellar Ligament, Tendon Injuries, Tendon, Injury, Proteoglycan, Extracellular matrix, SLRP, Healing
Abstract

Defining the constituent regulatory molecules in tendon is critical to understanding the process of tendon repair and instructive to the development of novel treatment modalities. The purpose of this study is to define the structural, expressional, and mechanical changes in the tendon injury response, and elucidate the roles of two class I small leucine-rich proteoglycans (SLRPs). We utilized biglycan-null, decorin-null and wild type mice with an established patellar tendon injury model. Mechanical testing demonstrated functional changes associated with injury and the incomplete recapitulation of mechanical properties after 6 weeks. In addition, SLRP deficiency influenced the mechanical properties with a marked lack of improvement between 3 and 6 weeks in decorin-null tendons. Morphological analyses of the injury response and role of SLRPs demonstrated alterations in cell density and shape as well as collagen alignment and fibril structure resulting from injury. SLRP gene expression was studied using RT-qPCR with alterations in expression associated with the injured tendons. Our results show that in the absence of biglycan initial healing may be impaired while in the absence of decorin later healing is clearly diminished. This suggests that biglycan and decorin may have sequential roles in the tendon response to injury.

Published
2014

20. Supplementary Figure 1 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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21. Supplementary Figure 3 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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22. Supplemental Material from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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23. Supplementary Figure 6 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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24. Supplementary Figure 9 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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25. Supplementary Figure 4 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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26. Supplementary Figure 7 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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27. Supplementary Figure 2 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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28. Data from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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29. Supplementary Figure 8 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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30. Supplementary Figure 5 from αvβ6 Integrin Promotes Castrate-Resistant Prostate Cancer through JNK1-Mediated Activation of Androgen Receptor

Author

Lu, Huimin, primary, Wang, Tao, primary, Li, Jing, primary, Fedele, Carmine, primary, Liu, Qin, primary, Zhang, Jianzhong, primary, Jiang, Zhong, primary, Jain, Dhanpat, primary, Iozzo, Renato V., primary, Violette, Shelia M., primary, Weinreb, Paul H., primary, Davis, Roger J., primary, Gioeli, Daniel, primary, FitzGerald, Thomas J., primary, Altieri, Dario C., primary, and Languino, Lucia R., primary

Published
2023
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31. Progranulin Oncogenic Network in Solid Tumors

Author

Ventura, Elisa, primary, Ducci, Giacomo, additional, Benot Dominguez, Reyes, additional, Ruggiero, Valentina, additional, Belfiore, Antonino, additional, Sacco, Elena, additional, Vanoni, Marco, additional, Iozzo, Renato V., additional, Giordano, Antonio, additional, and Morrione, Andrea, additional

Published
2023
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47. Extracellular matrix guidance of autophagy: a mechanism regulating cancer growth

Author

Chen, Carolyn G. and Iozzo, Renato V.

Subjects
decorin, proteoglycan, Neovascularization, Pathologic, QH301-705.5, General Neuroscience, Immunology, Review, General Biochemistry, Genetics and Molecular Biology, Extracellular Matrix, perlecan, collagen VI, angiogenesis, Neoplasms, Autophagy, Humans, Proteoglycans, Biology (General), Review Articles
Abstract

The extracellular matrix (ECM) exists as a dynamic network of biophysical and biochemical factors that maintain tissue homeostasis. Given its sensitivity to changes in the intra- and extracellular space, the plasticity of the ECM can be pathological in driving disease through aberrant matrix remodelling. In particular, cancer uses the matrix for its proliferation, angiogenesis, cellular reprogramming and metastatic spread. An emerging field of matrix biology focuses on proteoglycans that regulate autophagy, an intracellular process that plays both critical and contextual roles in cancer. Here, we review the most prominent autophagic modulators from the matrix and the current understanding of the cellular pathways and signalling cascades that mechanistically drive their autophagic function. We then critically assess how their autophagic functions influence tumorigenesis, emphasizing the complexities and stage-dependent nature of this relationship in cancer. We highlight novel emerging data on immunoglobulin-containing and proline-rich receptor-1, heparanase and thrombospondin 1 in autophagy and cancer. Finally, we further discuss the pro- and anti-autophagic modulators originating from the ECM, as well as how these proteoglycans and other matrix constituents specifically influence cancer progression.

Published
2022

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