Linked Life Data

7964722

Source:http://linkedlifedata.com/resource/pubmed/id/7964722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-12-23
pubmed:abstractText
Plasminogen (PGn) that we identified in microglial-conditioned medium has a neurotrophic factor-like effect on cultured neurons. We have also shown that PGn binds specifically to a protein with a molecular mass of 45 kDa in the neuronal plasma membrane. As a candidate PGn receptor-like molecule on the neuronal surface, this 45-kDa protein was purified from the plasma membrane of embryonic rat brain. Amino acid sequence analysis of polypeptides derived from the cleavage of the protein with cyanogen bromide and V8 protease revealed that the 45-kDa protein is identical to rat alpha-enolase. In fact, PGn was found to bind to purified rat alpha-enolase and also to a synthetic peptide (30 residues) that corresponds to the carboxyl terminal region of rat alpha-enolase. Physical properties of the 45-kDa protein, such as molecular mass, isoelectric point, and the ability to form dimers, are quite similar to those of alpha-enolase. The 45-kDa PGn-binding protein in the plasma membrane was also recognized by anti-rat alpha-enolase antibody, and pretreatment with alpha-enolase antibody markedly diminished the PGn-binding to the plasma membrane. In addition, immunocytochemical staining of the cultured cells under the nonpermeable condition showed that alpha-enolase is present on the cell surface of a certain population of neurons. These results suggest that alpha-enolase may function as a PGn-binding molecule on the neuronal cell surface.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2048-57
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Plasminogen binds specifically to alpha-enolase on rat neuronal plasma membrane.
pubmed:affiliation
Department of Neurochemistry, National Institute of Neuroscience, Tokyo.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't