Abstract:
:Cartilage oligomeric matrix protein (COMP) is an abundant component in the extracellular matrix (ECM) of load-bearing tissues such as tendons and cartilage. It provides adaptor functions by bridging different ECM structures. We have previously shown that COMP is also a constitutive component of healthy human skin and is strongly induced in fibrosis. It binds directly and with high affinity to collagen I and to collagen XII that decorates the surface of collagen I fibrils. We demonstrate here that lack of COMP-collagen interaction in the extracellular space leads to changes in collagen fibril morphology and density, resulting in altered skin biomechanical properties. Surprisingly, COMP also fulfills an important intracellular function in assisting efficient secretion of collagens, which were retained in the endoplasmic reticulum of COMP-null fibroblasts. Accordingly, COMP-null mice showed severely attenuated fibrotic responses in skin. Collagen secretion was fully restored by introducing wild-type COMP. Hence, our work unravels a new, non-structural and intracellular function of the ECM protein COMP in controlling collagen secretion.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Schulz JN,Nüchel J,Niehoff A,Bloch W,Schönborn K,Hayashi S,Kamper M,Brinckmann J,Plomann M,Paulsson M,Krieg T,Zaucke F,Eckes Bdoi
10.1242/jcs.180216subject
Has Abstractpub_date
2016-02-15 00:00:00pages
706-16issue
4eissn
0021-9533issn
1477-9137pii
jcs.180216journal_volume
129pub_type
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