Document Detail

Osteoadherin, a cell-binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix.
MedLine Citation:
PMID:  9642227     Owner:  NLM     Status:  MEDLINE    
Osteoadherin is a recently described bone proteoglycan containing keratan sulfate. It promotes integrin (alphav beta3)-mediated cell binding (Wendel, M., Sommarin, Y., and Heinegârd, D. (1998) J. Cell Biol. 141, 839-847). The primary structure of bovine osteoadherin has now been determined by nucleotide sequencing of a cDNA clone from a primary bovine osteoblast expression library. The entire translated primary sequence corresponds to a 49,116-Da protein with a calculated isoelectric point for the mature protein of 5.2. The dominating feature is a central region consisting of 11 B-type, leucine-rich repeats ranging in length from 20 to 30 residues. The full, primary sequence contains four putative sites for tyrosine sulfation, three of which are at the N-terminal end of the molecule. There are six potential sites for N-linked glycosylation present. Osteoadherin shows highest sequence identity, 42%, to bovine keratocan and 37-38% identity to bovine fibromodulin, lumican, and human PRELP. Unique to osteoadherin is the presence of a large and very acidic C-terminal domain. The distribution of cysteine residues resembles that of other leucine-rich repeat proteins except for two centrally located cysteines. Northern blot analysis of RNA samples from various bovine tissues showed a 4.5-kilobase pair message for osteoadherin to be expressed in bone only. Osteoadherin mRNA was detected by in situ hybridization in mature osteoblasts located superficially on trabecular bone.
Y Sommarin; M Wendel; Z Shen; U Hellman; D Heinegârd
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  273     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1998 Jul 
Date Detail:
Created Date:  1998-08-06     Completed Date:  1998-08-06     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  16723-9     Citation Subset:  IM    
Department of Cellular and Molecular Biology, Section for Connective Tissue Biology, Lund University, S-221 00 Lund, Sweden.
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MeSH Terms
Amino Acid Sequence
Base Sequence
Blotting, Northern
Bone and Bones / metabolism*
Cloning, Molecular
DNA, Complementary
Extracellular Matrix / metabolism*
Extracellular Matrix Proteins / chemistry,  genetics*,  metabolism
In Situ Hybridization
Keratan Sulfate / chemistry,  genetics*,  metabolism
Leucine / analysis*
Molecular Sequence Data
Protein Binding
Proteochondroitin Sulfates / chemistry,  genetics*,  metabolism
Proteoglycans / chemistry,  genetics*,  metabolism
RNA, Messenger / genetics,  metabolism
Sequence Homology, Amino Acid
Reg. No./Substance:
0/DNA, Complementary; 0/Extracellular Matrix Proteins; 0/Proteochondroitin Sulfates; 0/Proteoglycans; 0/RNA, Messenger; 0/lumican; 0/osteoadherin; 61-90-5/Leucine; 9056-36-4/Keratan Sulfate

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