Linked Life Data

8119487

Source:http://linkedlifedata.com/resource/pubmed/id/8119487

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-4-7
pubmed:databankReference
pubmed:abstractText
An extracellular matrix-associated glycoprotein expressed in a variety of tissues during embryogenesis and repair, SPARC contains modular domains that can function independently to bind cells and matrix components. Because SPARC can selectively disrupt cellular contacts with matrix and thereby effect changes in cell shape, it has been referred to as an antiadhesin. Inhibition of the expression of SPARC altered axial development in frogs, and deregulated expression in nematode worms resulted in a derangement of muscle attachment and embryonic lethality. SPARC also inhibits cell cycle progression in vitro, in part through a cationic, disulfide-bonded region that is homologous to a repeated domain in the cytokine inhibitor, follistatin. Moreover, SPARC binds specifically to the B chain of platelet-derived growth factor and alters the response of cells to several cytokines. Although information concerning the expression, biochemical properties, and cellular activities of SPARC has increased significantly over the last decade, the precise function of the protein has not been resolved. Goals of future studies include characterization of cell-surface receptors for SPARC and the interactions with morphogens and growth factors that regulate specific activities during animal development.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
163-73
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The biology of SPARC, a protein that modulates cell-matrix interactions.
pubmed:affiliation
Department of Genetics, Howard Hughes Medical Institute, Harvard University School of Medicine, Boston, Massachusetts 02115.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review