Linked Life Data

1400330

Source:http://linkedlifedata.com/resource/pubmed/id/1400330

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1992-11-16
pubmed:abstractText
Fibulin is a recently described extracellular matrix (ECM) and plasma glycoprotein (Argraves, W. S., Tran, H., Burgess, W. H., and Dickerson, K. (1990) J. Cell Biol. 111, 3155-3164). In this report, ligand affinity chromatography and solid-phase binding analyses were performed to determine which ECM protein(s) interact with fibulin. Fibulin-Sepharose bound two polypeptides of 240 and 100 kDa from the culture medium of metabolically radiolabeled fibroblasts. These two proteins were identified as fibronectin (FN) and fibulin, respectively, based on their electrophoretic behavior and reactivity with monoclonal antibodies. Consistent with the findings of affinity chromatography, fibulin bound to surfaces coated with FN (either plasma or cellular form) or fibulin but not with other ECM proteins, such as laminin, merosin, and types I and IV collagen. The binding of fibulin to solid-phase FN was estimated to have a Kd of 139 nM, whereas the Kd for self-interaction was 322 nM. Evaluation of proteolytic fragments from all regions of FN allowed a fibulin-binding site to be localized within a 23-kDa heparin-binding fragment containing type III repeats 13-14. Heparin did not compete for the interaction between fibulin and FN, suggesting that the binding sites for fibulin and heparin are distinct.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20120-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin.
pubmed:affiliation
American Red Cross, Biochemistry Laboratory, Rockville, Maryland 20855.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't