Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization

Biochemical Journal

Volumn 423, Issue 1, 2009, Pages 53-59

  Kalamajski, Sebastian ^a,c   Aspberg, Anders ^b   Lindblom, Karin ^a   Heinegård, Dick ^a   Oldberg, Åke ^a  

^a LUND UNIVERSITY   (Sweden)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c BOSTON CHILDREN S HOSPITAL   (United States)

Author keywords

Asporin; Biomineralization; Calcium; Collagen binding; Decorin; Small leucine rich repeat proteoglycan protein (SLRP)

Indexed keywords

ASPORIN; COLLAGEN BINDING; DECORIN; ECM (EXTRACELLULAR MATRIX); IN-VITRO; LEUCINE-RICH REPEATS; OSTEOBLASTIC ACTIVITY; OSTERIX; POLYASPARTATES; SMALL LEUCINE-RICH REPEAT PROTEOGLYCAN/PROTEIN (SLRP);

AMINO ACIDS; BIOMINERALIZATION; CALCIUM; CALCIUM ALLOYS; ELECTRIC DISCHARGE MACHINING; ESCHERICHIA COLI; HYDROXYAPATITE; MINERALOGY; OCEAN HABITATS;

COLLAGEN;

ASPORIN; BIGLYCAN; CALCIUM; COLLAGEN TYPE 1; DECORIN; HYDROXYAPATITE; MESSENGER RNA; POLYASPARTIC ACID; PROTEOGLYCAN; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR OSTERIX; TRANSCRIPTION FACTOR RUNX2; UNCLASSIFIED DRUG; ASPN PROTEIN, HUMAN; COLLAGEN; CYSTEINE; DISULFIDE; FIBRILLAR COLLAGEN; SCLEROPROTEIN;

ARTICLE; BINDING AFFINITY; BINDING SITE; BONE MINERALIZATION; CALCIUM BINDING; COLLAGEN METABOLISM; COMPETITIVE INHIBITION; CONTROLLED STUDY; ESCHERICHIA COLI; EXPRESSION VECTOR; HUMAN; HUMAN CELL; IN VITRO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; OSTEOBLAST; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; AMINO ACID SEQUENCE; BINDING COMPETITION; CELL CULTURE; CHEMISTRY; METABOLISM; PHYSIOLOGY; PROTEIN BINDING;

ESCHERICHIA COLI;

AMINO ACID SEQUENCE; BINDING, COMPETITIVE; CALCIFICATION, PHYSIOLOGIC; CALCIUM; CELLS, CULTURED; COLLAGEN; CYSTEINE; DISULFIDES; EXTRACELLULAR MATRIX PROTEINS; FIBRILLAR COLLAGENS; HUMANS; OSTEOBLASTS; PROTEIN BINDING; PROTEOGLYCANS;

EID: 70349772632     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090542     Document Type: Article

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