Linked Life Data

8662978

Source:http://linkedlifedata.com/resource/pubmed/id/8662978

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1996-8-13
pubmed:abstractText
Serum amyloid P (SAP), a member of the evolutionarily conserved pentraxin family, is a normal component of a number of basement membranes, including glomerular and alveolar. In vitro SAP binds to a variety of proteins including fibronectin, proteoglycans, and the collagen-like region of the complement component C1q. In these studies, binding of SAP to type IV collagen, a major component of basement membrane, was examined. Purified SAP binds to human and mouse type IV collagen but not type I, II, or III collagens. Binding of SAP to type IV collagen is dependent on the presence of Ca2+. This binding is saturable with a Kd approximately 1.2 x 10(-7) M based on solid phase binding and 4 x 10(-8) M based on the IC50 value from fluid phase binding data. Binding of SAP to type IV collagen was inhibited by both SAP and C-reactive protein (CRP). However, a 5-fold molar excess of CRP as compared with SAP was required to inhibit the SAP binding by 50%. Binding of SAP to type IV collagen was inhibited by both collagen IV and C1q but not by phosphatidylethanolamine or bovine serum albumin. The inhibition data indicate that SAP may bind to the triple helical region of type IV collagen via a site distinct from its galactan binding site. The most likely site of SAP involved in its interaction with type IV collagen may be the region spanning amino acid residues 108-120, which shows a great deal of sequence homology (60% strict identity) with the CRP region implicated in its binding to the collagen-like region of the C1q molecule.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14897-902
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Characterization of the binding of serum amyloid P to type IV collagen.
pubmed:affiliation
Division of Nephrology, Children's Hospital Research Foundation, University of Cincinnati College of Medicine, Cincinnati, Ohio 45229-3039, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't