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rdf:type |
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lifeskim:mentions |
umls-concept:C0009015,
umls-concept:C0017963,
umls-concept:C0017968,
umls-concept:C0021701,
umls-concept:C0033453,
umls-concept:C0034793,
umls-concept:C0042971,
umls-concept:C0080103,
umls-concept:C0086418,
umls-concept:C0205225,
umls-concept:C0332307,
umls-concept:C0678594,
umls-concept:C1136310,
umls-concept:C1154393,
umls-concept:C1321758,
umls-concept:C1334146,
umls-concept:C1366562,
umls-concept:C1706439
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pubmed:issue |
25
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pubmed:dateCreated |
1988-9-28
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pubmed:databankReference |
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pubmed:abstractText |
Mac-1 (CD 11b/CD18) is a leukocyte adhesion heterodimeric glycoprotein which functions both as a receptor for iC3b (CR3) and in several cell-cell and cell-substrate adhesive interactions. We describe full-length cDNA clones for the alpha subunit of Mac-1. Mac-1 alpha subunit message was detected in blood monocytes and phorbol-12-myristate acetate-induced myeloid cell lines, but not in cells of the T or B lineages, correlating with Mac-1 protein surface expression. The alpha subunit of Mac-1 is a transmembrane protein of 1137 residues with a long extracellular domain (1092 residues) and a 19-amino acid cytoplasmic tail. The extracellular domain contains three putative divalent cation-binding sequences and 19 potential N-glycosylation sites. The amino acid sequence of Mac-1 alpha shows that it is a member of the integrin superfamily; Mac-1 alpha shows 63% identity to the alpha subunit of the leukocyte adhesion glycoprotein p150.95 and 25% to the alpha subunits of the extracellular matrix receptors platelet glycoprotein IIb/IIIa, the fibronectin receptor, and the vitronectin receptor. The Mac-1 alpha subunit putative divalent cation-binding sites and the flanking regions exhibit a high degree of identity both to the p150.95 alpha subunit (87% identity at the amino acid level) and to the rest of the integrin alpha subunits (38%). The alpha subunit of Mac-1, like the p150.95 alpha subunit, contains a domain of 187 amino acids in the extracellular region which is absent in other integrins. This leukocyte or "L" domain is homologous to the A domains of von Willebrand factor, which in turn are homologous to regions of the C3-binding proteins factor B and C2. These findings draw attention to this region of Mac-1 as a potential binding site for iC3b.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Factor B,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Recombinant,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Function-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Macrophage-1 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement 3b,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibronectin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Vitronectin,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/von Willebrand Factor
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12403-11
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2457584-Amino Acid Sequence,
pubmed-meshheading:2457584-Antigens, Differentiation,
pubmed-meshheading:2457584-Base Sequence,
pubmed-meshheading:2457584-Complement Factor B,
pubmed-meshheading:2457584-DNA,
pubmed-meshheading:2457584-DNA, Recombinant,
pubmed-meshheading:2457584-Enzyme Precursors,
pubmed-meshheading:2457584-Granulocytes,
pubmed-meshheading:2457584-Humans,
pubmed-meshheading:2457584-Integrins,
pubmed-meshheading:2457584-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:2457584-Macrophage-1 Antigen,
pubmed-meshheading:2457584-Membrane Glycoproteins,
pubmed-meshheading:2457584-Molecular Sequence Data,
pubmed-meshheading:2457584-Monocytes,
pubmed-meshheading:2457584-Nucleic Acid Hybridization,
pubmed-meshheading:2457584-Peptide Fragments,
pubmed-meshheading:2457584-Platelet Membrane Glycoproteins,
pubmed-meshheading:2457584-RNA, Messenger,
pubmed-meshheading:2457584-Receptors, Complement,
pubmed-meshheading:2457584-Receptors, Complement 3b,
pubmed-meshheading:2457584-Receptors, Fibronectin,
pubmed-meshheading:2457584-Receptors, Immunologic,
pubmed-meshheading:2457584-Receptors, Vitronectin,
pubmed-meshheading:2457584-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2457584-Trypsin,
pubmed-meshheading:2457584-von Willebrand Factor
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pubmed:year |
1988
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pubmed:articleTitle |
The human leukocyte adhesion glycoprotein Mac-1 (complement receptor type 3, CD11b) alpha subunit. Cloning, primary structure, and relation to the integrins, von Willebrand factor and factor B.
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pubmed:affiliation |
Laboratory of Membrane Immunochemistry, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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