Linked Life Data

7592757

Source:http://linkedlifedata.com/resource/pubmed/id/7592757

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
43
pubmed:dateCreated
1995-12-14
pubmed:abstractText
The receptor for advanced glycation end products (RAGE), a newly-identified member of the immunoglobulin superfamily, mediates interactions of advanced glycation end product (AGE)-modified proteins with endothelium and other cell types. Survey of normal tissues demonstrated RAGE expression in situations in which accumulation of AGEs would be unexpected, leading to the hypothesis that under physiologic circumstances, RAGE might mediate interaction with ligands distinct from AGEs. Sequential chromatography of bovine lung extract identified polypeptides with M(r) values of approximately 12,000 (p12) and approximately 23,000 (p23) which bound RAGE. NH2-terminal and internal protein sequence data for p23 matched that reported previously for amphoterin. Amphoterin purified from rat brain or recombinant rat amphoterin bound to purified sRAGE in a saturable and dose-dependent manner, blocked by anti-RAGE IgG or a soluble form of RAGE (sRAGE). Cultured embryonic rat neurons, which express RAGE, displayed dose-dependent binding of 125I-amphoterin which was prevented by blockade of RAGE using antibody to the receptor or excess soluble receptor (sRAGE). A functional correlate of RAGE-amphoterin interaction was inhibition by anti-RAGE F(ab')2 and sRAGE of neurite formation by cortical neurons specifically on amphoterin-coated substrates. Consistent with a potential role for RAGE-amphoterin interaction in development, amphoterin and RAGE mRNA/antigen were co-localized in developing rat brain. These data indicate that RAGE has physiologically relevant ligands distinct from AGEs which are likely, via their interaction with the receptor, to participate in physiologic processes outside of the context of diabetes and accumulation of AGEs.
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
27
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
25752-61
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7592757-Animals, pubmed-meshheading:7592757-Base Sequence, pubmed-meshheading:7592757-Carrier Proteins, pubmed-meshheading:7592757-Cattle, pubmed-meshheading:7592757-Cells, Cultured, pubmed-meshheading:7592757-Cerebral Cortex, pubmed-meshheading:7592757-Chromatography, Affinity, pubmed-meshheading:7592757-HMGB1 Protein, pubmed-meshheading:7592757-High Mobility Group Proteins, pubmed-meshheading:7592757-Immunohistochemistry, pubmed-meshheading:7592757-In Situ Hybridization, pubmed-meshheading:7592757-Ligands, pubmed-meshheading:7592757-Lung, pubmed-meshheading:7592757-Molecular Sequence Data, pubmed-meshheading:7592757-Nerve Tissue Proteins, pubmed-meshheading:7592757-Neurites, pubmed-meshheading:7592757-Neurons, pubmed-meshheading:7592757-Protein Binding, pubmed-meshheading:7592757-RNA, Messenger, pubmed-meshheading:7592757-Rats, pubmed-meshheading:7592757-Rats, Wistar, pubmed-meshheading:7592757-Receptors, Immunologic
pubmed:year
1995
pubmed:articleTitle
The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system.
pubmed:affiliation
Department of Physiology, Columbia University, College of Physicians and Surgeons, New York, New York 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't