scholarly journals Structural features of cartilage matrix protein deduced from cDNA.

1987 ◽  
Vol 84 (2) ◽  
pp. 464-468 ◽  
Author(s):  
W. S. Argraves ◽  
F. Deak ◽  
K. J. Sparks ◽  
I. Kiss ◽  
P. F. Goetinck
Keyword(s):  
Matrix Protein ◽  
Structural Features ◽  
Cartilage Matrix

Crosslinking of cartilage matrix protein to aggrecan increases with maturation

1995 ◽  
Vol 66 (sup266) ◽  
pp. 71-72 ◽  
Author(s):  
Nik Hauser ◽  
Mats Paulsson ◽  
Dick Heinegård ◽  
Matthias Mörgelin
Keyword(s):  
Matrix Protein ◽  
Cartilage Matrix

scholarly journals The Structural Features of Henipavirus Matrix Protein Driving Intracellular Trafficking

2020 ◽  
Author(s):  
Camilla M. Donnelly ◽  
Justin A. Roby ◽  
Christopher J. Scott ◽  
Shane R. Raidal ◽  
Jade K. Forwood
Keyword(s):  
Intracellular Trafficking ◽  
Matrix Protein ◽  
Structural Features

scholarly journals Integrin α2β1 Is a Receptor for the Cartilage Matrix Protein Chondroadherin

1997 ◽  
Vol 138 (5) ◽  
pp. 1159-1167 ◽  
Author(s):  
Lisbet Camper ◽  
Dick Heinegård ◽  
Evy Lundgren-Åkerlund
Keyword(s):  
Cell Adhesion ◽  
Matrix Protein ◽  
Collagen Type ◽  
Human Fibroblasts ◽  
Cartilage Matrix ◽  
Affinity Column ◽  
Integrin Subunit ◽  
Β1 Integrin ◽  
Type Ii ◽  
Collagen Type Ii

Chondroadherin (the 36-kD protein) is a leucine-rich, cartilage matrix protein known to mediate adhesion of isolated chondrocytes. In the present study we investigated cell surface proteins involved in the interaction of cells with chondroadherin in cell adhesion and by affinity purification. Adhesion of bovine articular chondrocytes to chondroadherin-coated dishes was dependent on Mg2+ or Mn2+ but not Ca2+. Adhesion was partially inhibited by an antibody recognizing β1 integrin subunit. Chondroadherin-binding proteins from chondrocyte lysates were affinity purified on chondroadherin-Sepharose. The β1 integrin antibody immunoprecipitated two proteins with molecular mass ∼110 and 140 kD (nonreduced) from the EDTA-eluted material. These results indicate that a β1 integrin on chondrocytes interacts with chondroadherin. To identify the α integrin subunit(s) involved in interaction of cells with the protein, we affinity purified chondroadherin-binding membrane proteins from human fibroblasts. Immunoprecipitation of the EDTA-eluted material from the affinity column identified α2β1 as a chondroadherin-binding integrin. These results are in agreement with cell adhesion experiments where antibodies against the integrin subunit α2 partially inhibited adhesion of human fibroblast and human chondrocytes to chondroadherin. Since α2β1 also is a receptor for collagen type II, we tested the ability of different antibodies against the α2 subunit to inhibit adhesion of T47D cells to collagen type II and chondroadherin. The results suggested that adhesion to collagen type II and chondroadherin involves similar or nearby sites on the α2β1 integrin. Although α2β1 is a receptor for both collagen type II and chondroadherin, only adhesion of cells to collagen type II was found to mediate spreading.

scholarly journals 221 COLLAGEN TYPE IX AND CARTILAGE OLIGOMERIC MATRIX PROTEIN INFLUENCE CARTILAGE MATRIX ASSEMBLY

2008 ◽  
Vol 16 ◽  
pp. S104
Author(s):  
Y.M. Bastiaansen-Jenniskens ◽  
K. Blumbach ◽  
W. Koevoet ◽  
M. Paulsson ◽  
J. DeGroot ◽  
...  
Keyword(s):  
Cartilage Oligomeric Matrix Protein ◽  
Matrix Protein ◽  
Collagen Type ◽  
Cartilage Matrix ◽  
Matrix Assembly ◽  
And Cartilage

scholarly journals Purification and structural characterization of a cartilage matrix protein

1981 ◽  
Vol 197 (2) ◽  
pp. 367-375 ◽  
Author(s):  
M Paulsson ◽  
D Heinegård
Keyword(s):  
Molecular Weight ◽  
Matrix Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cartilage Matrix ◽  
Sedimentation Equilibrium ◽  
Intact Protein ◽  
Gel Chromatography ◽  
Guanidinium Chloride ◽  
Cscl Density Gradient

The cartilage matrix protein is a major non-collagenous protein in bovine cartilage. It was purified from a 5 M-guanidinium chloride extract of bovine tracheal cartilage by sequential CsCl-density-gradient centrifugation, gel chromatography in guanidinium chloride and differential precipitation. The molecular weight of the intact protein is 148 000, determined by sedimentation-equilibrium centrifugation. It was dissociated to three subunits of molecular weight 52 000 by reduction of disulphide bonds. The cartilage matrix protein was insoluble in low-salt solutions and behaved abnormally on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The content of cysteine was high, whereas the contents of aromatic amino acids were low. The carbohydrate content was 3.9% (w/w). Glycopeptides obtained after papain digestion were heterogenous on gel chromatography. Asparagine/aspartic acid was enriched in the purified glycopeptides, indicating the presence of N-glycosidic linkages to protein.

scholarly journals Cartilage matrix protein is a component of the collagen fibril of cartilage

1992 ◽  
Vol 193 (3) ◽  
pp. 266-276 ◽  
Author(s):  
Neil Winterbottom ◽  
M. Mehrdad Tondravi ◽  
Terrill L. Harrington ◽  
F. George Klier ◽  
Barbara M. Vertel ◽  
...  
Keyword(s):  
Collagen Fibril ◽  
Matrix Protein ◽  
Cartilage Matrix

scholarly journals Enhancement of Cell Adhesion and Spreading by a Cartilage-specific Noncollagenous Protein, Cartilage Matrix Protein (CMP/Matrilin-1), via Integrin α1β1

1999 ◽  
Vol 274 (16) ◽  
pp. 11417-11423 ◽  
Author(s):  
Seicho Makihira ◽  
Weiqun Yan ◽  
Shigeru Ohno ◽  
Takeshi Kawamoto ◽  
Katsumi Fujimoto ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Matrix Protein ◽  
Cartilage Matrix ◽  
Noncollagenous Protein
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