Extracellular matrix assemblies

Prockop, D.J., andHulmes, D.J. S. (1994). Assembly of collagen fibrils de now from soluble precursors. In Extracellular Matrix Assembly and Structure (P. D. Yurchenco, D. E. Birkand R. P. Mecham, Eds.), pp. 47-90. Academic Press, San Diego. 

Fibrillin microfibrils are widely distributed extracellular matrix assemblies that endow elastic and non elastic connective tissues with long-range elasticity. They direct tropoelastin deposition during elastic fibrillogenesis and form an outer mantle for mature elastic fibers. Microfibril arrays are also abundant in dynamic tissues that do not express elastin, such as the ciliary zonules of the eye. Mutations in fibrillin-1—the principal structural component of microfibrils—cause Marfan syndrome, a heritable disease with severe aortic, ocular, and skeletal defects. Isolated fibrillin-rich microfibrils have a complex 56 nm beads-on-a-string appearance the molecular basis of their assembly and... 

Netti, P.A., Berk, D.A., Swartz, M.A., Grodzinsky, A.J. and Jain, R.K. (2000) Role of extracellular matrix assembly in interstitial transport in solid tumors. Cancer Res., 60, 2497-2503. 

Veis A, George A. Fundamentals of Interstitial Collagen Self-Assembly. Extracellular Matrix Assembly. New York Academic Press 1994 15 15. 

McDonald, J. A. (1988). Extracellular matrix assembly. Ann. Rev. Cell Biol. 4,... 

Ruoslahti, E. Engvall, E. Integrins and vascular extracellular matrix assembly. J. Clin. Invest. 1997, 99 (6), 1149-1152. 

Paul A. Janmey received an AB degree from Oberlin College in 1976 and a PhD degree in physical chemistry from the University ofWisconsin in 1982 (for his work on fibrin polymerization, under the guidance of J. D. Ferry). A postdoctoral fellowship in the Hematology Unit of Massachusetts General Hospital motivated application of methods of polymer physics to the cytoskeleton. Since then his lab has studied the viscoelastic properties of biopolymer networks and the regulation of cytoskeletal and extracellular matrix assembly. 

Aguilera, A., Souza-Egipsy, V., Martin-Uriz, P. S. Amils, R. (2008). Extracellular matrix assembly in extreme acidic eukaryotic biofilms and their possible implications in heavy metal adsorption. Aquat Toxicol, 88, 257-266. 

Kielty, C.M., Hopkinson, 1., Grant, M.E. Collagen structure, assembly and organization in the extracellular matrix. In Connective Tissue and its Heritable Disorders Wiley-Liss, Chichester, pp. 103-147, 1993. 

Stress fibers are parallel bundles of actin filaments that develop in the cytoplasm of fibroblasts from the cortical actin network in response to mechanical tension. These often bind to the plasma membrane at focal contacts and, through transmembrane linker glycoproteins, to the extracellular matrix. Thus, actin filaments of stress fibers indirectly Join to the inner face of the plasma membrane through molecular assemblies of attachment proteins, which include an actin-capping protein, a-actinin, vinculin, and talin (Small, 1988). 

The first elastomeric protein is elastin, this structural protein is one of the main components of the extracellular matrix, which provides stmctural integrity to the tissues and organs of the body. This highly crosslinked and therefore insoluble protein is the essential element of elastic fibers, which induce elasticity to tissue of lung, skin, and arteries. In these fibers, elastin forms the internal core, which is interspersed with microfibrils [1,2]. Not only this biopolymer but also its precursor material, tropoelastin, have inspired materials scientists for many years. The most interesting characteristic of the precursor is its ability to self-assemble under physiological conditions, thereby demonstrating a lower critical solution temperature (LCST) behavior. This specific property has led to the development of a new class of synthetic polypeptides that mimic elastin in its composition and are therefore also known as elastin-like polypeptides (ELPs). 

S. Amott, in S. Amott and D. A. Rees (Eds.), Glycosaminoglycan Assemblies in the Extracellular Matrix, Humana Press, Clifton, 1984. 

Cappello R et al (2006) Notochordal cell produce and assemble extracellular matrix in a distinct manner, which may be responsible for the maintenance of healthy nucleus pulposus. Spine (Phila Pa 1976) 31(8) 873—882, discussion 883... 

Vardi A, Formiggini F, Casotti R, De Martino A, Ribalet F, Miralto A, Bowler C (2006) A stress surveillance system based on calcium and nitric oxide in marine diatoms. PLoS Biol 4 411 119 Vorwerk S, Somerville S, Somerville C (2004) The role of plant cell wall polysaccharide composition in disease resistance. Trends Plant Sci 9 203-209 Vreeland V, Laetsch WM (1990) A gelling carbohydrate in algal cell wall formation. In Adair WS, Mecham RP (eds) Organization and assembly of plant and animal extracellular matrix. Academic, San Diego, CA, ppl 37—171... 

Putnam AJ, Schultz K, Mooney DJ. Control of microtubule assembly by extracellular matrix and externally applied strain. Am J Physiol Cell Physiol 2001 280(3) C556-C564. 

Nature often uses cystine knots of variable complexity to assemble polypeptide chains in the correct order and to stabilize the structure of the resulting proteins. Classical examples are proteins of the extracellular matrix with collagens and gelatines as the main components. This simple cystine-knot approach has been applied to synthetic constructs to ligate in a desired order helix bundles. [166 170 194-1%] It has also been used to mimic natural multiple-chain containing proteins like collagen.[83 1691971... 

Kielty, C. M., and Grant, M. E. (2002). The Collagen Family Structure Assembly and Organization in the Extracellular Matrix. In Connective Tissue and its Heritable Disorders, (P. M. Royce andB. Steinmann, Eds.), pp. 159-222. Wiley-Liss, New York. 

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