scholarly journals Primary Structure and Expression of Matrilin-2, the Closest Relative of Cartilage Matrix Protein within the von Willebrand Factor Type A-like Module Superfamily

1997 ◽  
Vol 272 (14) ◽  
pp. 9268-9274 ◽  
Author(s):  
Ferenc Deák ◽  
Dorothea Piecha ◽  
Csanád Bachrati ◽  
Mats Paulsson ◽  
Ibolya Kiss
Keyword(s):  
Von Willebrand Factor ◽  
Primary Structure ◽  
Matrix Protein ◽  
Type A ◽  
Cartilage Matrix ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Modulation of TMEM16A channel activity by the von Willebrand factor type A (VWA) domain of the calcium-activated chloride channel regulator 1 (CLCA1)

2017 ◽  
Vol 292 (22) ◽  
pp. 9164-9174 ◽  
Author(s):  
Monica Sala-Rabanal ◽  
Zeynep Yurtsever ◽  
Kayla N. Berry ◽  
Colin G. Nichols ◽  
Tom J. Brett
Keyword(s):  
Von Willebrand Factor ◽  
Chloride Channel ◽  
Type A ◽  
Channel Activity ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Assembly of a Novel Cartilage Matrix Protein Filamentous Network: Molecular Basis of Differential Requirement of von Willebrand Factor A Domains

1999 ◽  
Vol 10 (7) ◽  
pp. 2149-2162 ◽  
Author(s):  
Qian Chen ◽  
Yue Zhang ◽  
David M. Johnson ◽  
Paul F. Goetinck
Keyword(s):  
Von Willebrand Factor ◽  
Metal Ion ◽  
Matrix Protein ◽  
Network Formation ◽  
Cartilage Matrix ◽  
Immunogold Electron Microscopy ◽  
A Domains ◽  
Von Willebrand ◽  
A2 Domain ◽  
Willebrand Factor

Cartilage matrix protein (CMP) is the prototype of the newly discovered matrilin family, all of which contain von Willebrand factor A domains. Although the function of matrilins remain unclear, we have shown that, in primary chondrocyte cultures, CMP (matrilin-1) forms a filamentous network, which is made up of two types of filaments, a collagen-dependent one and a collagen-independent one. In this study, we demonstrate that the collagen-independent CMP filaments are enriched in pericellular compartments, extending directly from chondrocyte membranes. Their morphology can be distinguished from that of collagen filaments by immunogold electron microscopy, and mimicked by that of self-assembled purified CMP. The assembly of CMP filaments can occur from transfection of a wild-type CMP transgene alone in skin fibroblasts, which do not produce endogenous CMP. Conversely, assembly of endogenous CMP filaments by chondrocytes can be inhibited specifically by dominant negative CMP transgenes. The two A domains within CMP serve essential but different functions during network formation. Deletion of the A2 domain converts the trimeric CMP into a mixture of monomers, dimers, and trimers, whereas deletion of the A1 domain does not affect the trimeric configuration. This suggests that the A2 domain modulates multimerization of CMP. Absence of either A domain from CMP abolishes its ability to form collagen-independent filaments. In particular, Asp22in A1 and Asp255in A2 are essential; double point mutation of these residues disrupts CMP network formation. These residues are part of the metal ion–dependent adhesion sites, thus a metal ion–dependent adhesion site–mediated adhesion mechanism may be applicable to matrilin assembly. Taken together, our data suggest that CMP is a bridging molecule that connects matrix components in cartilage to form an integrated matrix network.

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