Linked Life Data

2483119

Source:http://linkedlifedata.com/resource/pubmed/id/2483119

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-4-6
pubmed:abstractText
Evidence is presented to support our hypothesis that an alpha-macroglobulin (alpha M) produced by lung macrophages serves as a specific binding protein for platelet-derived growth factor (PDGF) from these same macrophages. Culture medium "conditioned" by alveolar macrophages was fractionated by gel filtration according to molecular weight. Proteins larger than 200 kD were bound to greater than 50% of the macrophage-derived PDGF (MD-PDGF) that was extractable by 1 M acetic acid. Another approximately 25% was bound to fractions at approximately 150 kD, and approximately 20% remained unbound. The two high molecular weight fractions inhibited approximately 40% of specific [125I]PDGF binding to rat lung fibroblasts, whereas other fractions did not block PDGF binding to its receptor. Only the greater than 200 kD fractions inhibited the binding of PDGF antisera to purified human PDGF by 20% of control and exhibited specific complex formation and coelution on a gel filtration column with [125I]PDGF. The macrophage-derived alpha M (MD-alpha M) was separated from other macrophage-derived proteins by nickel-affinity chromatography and exhibited clear characteristics of alpha Ms, i.e., cross-reactivity with antibodies to human alpha 2-macroglobulin (alpha 2M) on immunoblots as well as gel migration corresponding to the electrophoretic mobility of the protease-bound "fast" and protease-unbound "slow" forms of human alpha 2M. Nickel-bound protein identified as an alpha M was bound to greater than 50% of the acid-extractable MD-PDGF in macrophage-conditioned medium, supporting the view that the greater than 200 kD protein separated by gel filtration is an alpha M.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1044-1549
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-9
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Alpha-macroglobulin secreted by alveolar macrophages serves as a binding protein for a macrophage-derived homologue of platelet-derived growth factor.
pubmed:affiliation
Laboratory of Pulmonary Pathobiology, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.
pubmed:publicationType
Journal Article