Extracellular Matrix Biology Research Articles

Interaction of fibronectin with arginine—agarose

FEBS LettersVolume 150, Issue 1 p. 243-246 Full-length articleFree Access Interaction of fibronectin with arginine—agarose Mamoru Isemura, Mamoru Isemura Department of Biochemistry, Tohoku University School of Medicine, Sendai, 980 JapanSearch for more papers by this authorCheng-Chin Hsu, Cheng-Chin Hsu Department of Biochemistry, Tohoku University School of Medicine, Sendai, 980 JapanSearch for more papers by this authorZensaku Yosizawa, Zensaku Yosizawa Department of Biochemistry, Tohoku University School of Medicine, Sendai, 980 JapanSearch for more papers by this authorShoji Odani, Shoji Odani Department of Biochemistry, Niigata University School of Medicine, Niigata, 951, JapanSearch for more papers by this authorTeruo Ono, Teruo Ono Department of Biochemistry, Niigata University School of Medicine, Niigata, 951, JapanSearch for more papers by this author Mamoru Isemura, Mamoru Isemura Department of Biochemistry, Tohoku University School of Medicine, Sendai, 980 JapanSearch for more papers by this authorCheng-Chin Hsu, Cheng-Chin Hsu Department of Biochemistry, Tohoku University School of Medicine, Sendai, 980 JapanSearch for more papers by this authorZensaku Yosizawa, Zensaku Yosizawa Department of Biochemistry, Tohoku University School of Medicine, Sendai, 980 JapanSearch for more papers by this authorShoji Odani, Shoji Odani Department of Biochemistry, Niigata University School of Medicine, Niigata, 951, JapanSearch for more papers by this authorTeruo Ono, Teruo Ono Department of Biochemistry, Niigata University School of Medicine, Niigata, 951, JapanSearch for more papers by this author First published: December 13, 1982 https://doi.org/10.1016/0014-5793(82)81343-4Citations: 4AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL References 1 K.M. Yamada, K. Olden, Nature, 275, (1978), 179– 184. 2 E. Ruoslahti, E. Engvall, E.G. Hayman, Coll. Res., 1, (1981), 95– 128. 3 K.M. Yamada, E.D. Hay Cell Biology of Extracellular Matrix (1981), Plenum New York 95– 114. 4 E. Engvall, E. Ruoslahti, Int. J. Cancer, 20, (1977), 1– 5. 5 M. Vuento, A. Vaheri, Biochem. J., 175, (1978), 333– 336. 6 M. Vuento, A. Vaheri, Biochem. J., 183, (1979), 331– 337. 7 M. Isemura, N. Sato, Z. Yosizawa, J. Biol. Chem., (1983), in press 8 M. Isemura, Z. Yosizawa, K. Takahashi, H. Kosaka, N. Kojima, T. Ono, J. Biochem., 90, (1981), 1– 9. 9 M. Vuento, E. Salonen, K. Österlund, U-H. Stanman, Biochem. J., 201, (1982), 1– 8. 10 M. Isemura, Z. Yosizawa, 12th Int. Congr. Biochem. Perth, (1982), 333– abstr. 11 G. Balian, E.M. Click, E. Crouch, M. Davidson, P. Bornstein, J. Biol. Chem., (1979), 1429– 1432. 12 T. Vartio, Eur. J. Biochem., 123, (1982), 223– 233. Citing Literature Volume150, Issue1December 13, 1982Pages 243-246 ReferencesRelatedInformation

Maintaining Binocular Vision

<h3>Abstract</h3> Tissue decellularization has demonstrated widespread applications across numerous organ systems for tissue engineering and regenerative medicine applications. Decellularized tissues are expected to retain structural and/or compositional features of the natural extracellular matrix (ECM), enabling investigation of biochemical factors and cell-ECM interactions that drive tissue homeostasis, healing, and disease. However, the dense collagenous tendon matrix has limited the efficacy of traditional decellularization strategies without the aid of harsh chemical detergents and/or physical agitation that disrupt tissue integrity and denature proteins involved in regulating cell behavior. Here, we adapted and established the advantages of a detergent-free decellularization method that relies on Latrunculin B actin destabilization, alternating hypertonic-hypotonic salt and water incubations, nuclease-assisted elimination of cellular material, and protease inhibitor supplementation under aseptic conditions. Compared with previous tendon decellularization studies, our method minimized collagen denaturation while adequately removing cells and preserving bulk tissue alignment and mechanical properties. Furthermore, we demonstrated that decellularized tendon ECM-derived coatings isolated from different mouse strains, injury states (i.e., naïve and acutely injured/’provisional’), and anatomical sites harness distinct biochemical cues and robustly maintain tendon cell viability <i>in vitro</i>. Together, our work provides a simple and scalable decellularization method to facilitate mechanistic studies that will expand our fundamental understanding of tendon ECM and cell biology. <h3>Impact Statement</h3> In this study, we present a decellularization method for tendon that does not rely on any detergents or physical processing techniques. We assessed the impact of detergent-free decellularization using tissue, cellular, and molecular level analyses and validated the preservation of tendon structural organization, collagen molecular integrity, and ECM-associated biological cues that are essential for studying physiological cell-ECM interactions. Lastly, we demonstrated the success of this method on healthy and injured tendon environments, across mouse strains, and for different types of tendons, illustrating the utility of this approach for isolating the contributions of biochemical cues within unique tendon ECM microenvironments.

DR. Eduardo Perroncito

Osteogenesis imperfecta, or brittle bone disease, is a congenital disease that primarily causes low bone mass and bone fractures but it can negatively affect other organs. It is usually inherited in an autosomal dominant fashion, although rarer recessive and X-chromosome-linked forms of the disease have been identified. In addition to type I collagen, mutations in a number of other genes, often involved in type I collagen synthesis or in the differentiation and function of osteoblasts, have been identified in the last several years. Seldom, the study of a rare disease has delivered such a wealth of new information that have helped our understanding of multiple processes involved in collagen synthesis and bone formation. In this short review I will describe the clinical features and the molecular genetics of the disease, but then focus on how OI dysregulates all aspects of extracellular matrix biology. I will conclude with a discussion about OI therapeutics.