Primary structure of matrilin‐3, a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin‐1) and von Willebrand factor

FEBS Letters

Wagener, Raimund¹  Paulsson, Mats¹  Kobbe, Birgit¹ 

[1] Institute for Biochemistry II, Medical Faculty, University of Cologne, Joseph-Stelzmann-Strasse 52, D-50931 Cologne, Germany

关键词: Cartilage matrix protein;    Matrilin;    Extracellular matrix;    Von Willebrand factor type A;    Epidermal growth factor;    Coiled-coil α-helix;    vWFA;    von Willebrand factor type A;    CMP;    cartilage matrix protein;    EGF;    epidermal growth factor;    EST;    expressed sequence tag;    GAPDH;    glyceraldehyde-3-phosphate dehydrogenase;   

DOI  :  10.1016/S0014-5793(97)00895-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A mouse cDNA encoding for matrilin-3, the third member of the novel matrilin family of extracellular matrix proteins, was cloned. The protein precursor of 481 amino acids consists of a putative signal peptide, a short positively charged sequence, a single vWFA-like domain followed by four epidermal growth factor-like modules and a potential coiled-coil α-helical oligomerization domain at the C-terminus. It is the smallest member of the matrilin family with a predicted M _r of the mature protein of 48 902. The primary structure of a C-terminal portion of 310 amino acids of the human matrilin-3 was determined and showed a sequence identity to the mouse matrilin-3 of 84.8%. Northern blot hybridization of mouse matrilin-3 mRNA showed a 2.9 kb mRNA expressed in sternum, femur and trachea and indicates a cartilage-specific expression.

【 授权许可】

Unknown