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The matrilins – adaptor proteins in the extracellular matrix
Author(s) -
Wagener Raimund,
Ehlen Harald W.A.,
Ko Ya-Ping,
Kobbe Birgit,
Mann Henning H.,
Sengle Gerhard,
Paulsson Mats
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.018
Subject(s) - extracellular matrix , phenotype , signal transducing adaptor protein , aggrecan , microbiology and biotechnology , proteolysis , chemistry , loss function , cartilage oligomeric matrix protein , function (biology) , biology , genetics , gene , osteoarthritis , biochemistry , signal transduction , articular cartilage , medicine , alternative medicine , enzyme , pathology
The matrilins form a four‐member family of modular, multisubunit matrix proteins, which are expressed in cartilage but also in many other forms of extracellular matrix. They participate in the formation of fibrillar or filamentous structures and are often associated with collagens. It appears that they mediate interactions between collagen‐containing fibrils and other matrix constituents, such as aggrecan. This adaptor function may be modulated by physiological proteolysis that causes the loss of single subunits and thereby a decrease in binding avidity. Attempts to study matrilin function by gene inactivation in mouse have been frustrating and so far not yielded pronounced phenotypes, presumably because of the extensive redundancy within the family allowing compensation by one family member for another. However, mutations in matrilin‐3 in humans cause different forms of chondrodysplasias and perhaps also hand osteoarthritis. As loss of matrilin‐3 is not critical in mouse, these phenotypes are likely to be caused by dominant negative effects.