Extracellular matrix matrices

Hocking, A. M., Shinomura, T. and McQuillan, D. J. (1998). Leucine-rich repeat glycoproteins of the extracellular matrix. Matrix Biol. 17, 1-19. 

Expression and secretion of proteases by the tumor microenvironment is critical both for support of tumor progression and metastasis, activation of growth factors and promotion of angiogenesis and invasion by digestion of the extracellular matrix (matrix metalloproteinases, MMPs, are collagenases) [114], The dominant cancer proteases are cathepsins and MMPs with both extracellular secreted MMPs and membrane type MMPs (MT-MMPs). This has promoted the use of cathepsin and MMP substrate peptides for tumor imaging and/or therapy [ 115,116]. 

Oberhauser et al., 1998] Oberhauser, A. F., Marszalek, P. E., Erickson, H., and Fernandez, J. The molecular elasticity of tenascin, an extracellular matrix protein. Nature. In Press. 

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. 

Extracellular matrix The surfaces of animal cells are covered with a flexible and sticky layer of complex carbohydrates, proteins, and lipids. This complex coating is cell-specific, serves in cell-cell recognition and communication, creates cell adhesion, and provides a protective outer layer. 

Proteoglycans may be soluble and located in the extracellular matrix, as is the case for serglycin, versican, and the cartilage matrix proteoglycan, or they may be integral transmembrane proteins, such as syndecan. Both types of proteoglycan... 

Secreted or extracellular matrix proteoglyeans Large aggregating cartilage proteoglycans CS/KS 220,952 2124... 

Cathepsins are intracellular proteinases that reside within lysosomes or specific intracellular granules. Cathepsins are used to degrade proteins or pqffides that are internalised from the extracellular space. Some cathepsins such as cathepsin-G or cathepsin-K may be released from the cell to degrade specific extracellular matrix proteins. All cathepsins except cathepsin-G (serine) and cathepsin-D (aspartyl) are cysteine proteinases. 

Integrins, selectins, cadherins, claudins and other cell adhesion molecules are involved in the interaction of cells with other cells or with extracellular matrix components. Some of them also serve as receptors by inducing outside-in or additional inside-out signaling. 

In biology, extracellular matrix (ECM) is the extracellular part of animal tissue that usually provides structural support to the cells in addition to performing various other important functions. ECM is the defining feature of connective tissue in animals. ECM includes the interstitial matrix and the basement membrane. 

Heparin sulfate proteoglycans (HSPGs) are heavily glycosylated proteins that are part of the extracellular matrix. Interaction with HSPGs help to stabilize and localize extracellular Wnts. 

Integrins constitute a large family of a (3 heterodimeric cell surface, transmembrane proteins that interact with a large number of extracellular matrix components through a metal ion-dependent interaction. The term integrin reflects their function in integrating cell adhesion and migration with the cystoskeleton. 

Reelin is an extracellular matrix protein, which is secreted by neuronal cells and binds to two lipoprotein receptors (VLDLR and ApoER2) that relay the Reelin signal inside target neurons by docking the tyrosine kinase adapter disabled-1 (Dabl). This allows neurons to complete migration and adopt their ultimate positions in laminar structures in the central nervous system. In... 

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