Linked Life Data

3530901

Source:http://linkedlifedata.com/resource/pubmed/id/3530901

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1986-11-10
pubmed:abstractText
Osteocalcin is an abundant Ca2+-binding protein indigenous to the organic matrix of bone, dentin, and possibly other mineralized tissues. This protein contains 47-50 amino acid residues (molecular weight 5,200-5,900) depending on the species. Osteocalcin is distinguished by its content of three gamma-carboxyglutamic (Gla) residues. The vitamin-K-dependent biosynthesis of osteocalcin occurs in bone, and the protein is not homologous to the Gla-containing regions of known vitamin-K-dependent blood coagulation proteins. The two major structural features of osteocalcin which appear to control its function include: the 'Gla helix', a compact Ca2+-dependent alpha-helical conformation, in which the three Gla residues are aligned to facilitate adsorption to hydroxyapatite, and the 'COOH-terminal beta-sheet' which exhibits chemoattractant activity toward mononuclear leukocytes, specifically monocytes, the putative precursors of osteoclasts. While the biological function of osteocalcin is unknown, it appears to be a highly specific osteoblastic marker produced during bone formation, and is rapidly becoming a clinically important diagnostic parameter of bone pathology. This article reviews recent advances in the understanding of osteocalcin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0301-0147
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
258-72
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Osteocalcin: the vitamin K-dependent Ca2+-binding protein of bone matrix.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't