Linked Life Data

8486654

Source:http://linkedlifedata.com/resource/pubmed/id/8486654

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1993-6-4
pubmed:databankReference
pubmed:abstractText
Macrosialin is a heavily glycosylated transmembrane protein of 87-115 kDa, highly and specifically expressed by mouse tissue macrophages, and to a lesser extent by dendritic cells. We have isolated cDNA clones encoding macrosialin from a thioglycollate-elicited peritoneal macrophage cDNA library by transient expression in COS cells and panning with the anti-macrosialin monoclonal antibody FA/11. A single 1.3-kilobase macrosialin transcript was detected in both untreated and phorbol 12-myristate 13-acetate-stimulated RAW cells. The cDNA sequence predicts a type I integral membrane protein of 326 residues with a heavily glycosylated extracellular domain of 306 residues containing nine potential N-linked glycosylation sites and numerous potential O-linked glycosylation sites. The extracellular domain consists of two distinct regions, separated by an extended 12 residue proline-rich hinge; a membrane-distal mucin-like domain of 89 residues containing short peptide repeats and consisting of 44% serine and threonine residues; and a membrane proximal domain of 170 residues, which has significant sequence homology to a family of lysosomal associated glycoproteins known as the lamp-1 group. Macrosialin is the murine homologue of the human macrophage glycoprotein CD68 (72% identity, 80% similarity). Both proteins are preferentially expressed by macrophages and share the same bipartite structure having a mucin-like domain and a domain common to the lamp family. Macrosialin and CD68 are the first examples of a lamp family protein with a restricted cell-type-specific expression. They may have evolved from the lamps to carry out specialized functions in dedicated phagocytic cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9661-6
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed-meshheading:8486654-Amino Acid Sequence, pubmed-meshheading:8486654-Animals, pubmed-meshheading:8486654-Antigens, CD, pubmed-meshheading:8486654-Antigens, Differentiation, Myelomonocytic, pubmed-meshheading:8486654-Base Sequence, pubmed-meshheading:8486654-Blotting, Northern, pubmed-meshheading:8486654-Cell Line, pubmed-meshheading:8486654-Cells, Cultured, pubmed-meshheading:8486654-Cloning, Molecular, pubmed-meshheading:8486654-DNA, pubmed-meshheading:8486654-Gene Library, pubmed-meshheading:8486654-Humans, pubmed-meshheading:8486654-Lysosome-Associated Membrane Glycoproteins, pubmed-meshheading:8486654-Macrophages, pubmed-meshheading:8486654-Membrane Glycoproteins, pubmed-meshheading:8486654-Mice, pubmed-meshheading:8486654-Mice, Inbred BALB C, pubmed-meshheading:8486654-Molecular Sequence Data, pubmed-meshheading:8486654-Oligodeoxyribonucleotides, pubmed-meshheading:8486654-Plasmids, pubmed-meshheading:8486654-Polymerase Chain Reaction, pubmed-meshheading:8486654-Protein Conformation, pubmed-meshheading:8486654-RNA, Messenger, pubmed-meshheading:8486654-Rats, pubmed-meshheading:8486654-Sequence Homology, Amino Acid, pubmed-meshheading:8486654-Tetradecanoylphorbol Acetate, pubmed-meshheading:8486654-Transfection
pubmed:year
1993
pubmed:articleTitle
Macrosialin, a mouse macrophage-restricted glycoprotein, is a member of the lamp/lgp family.
pubmed:affiliation
Cell Adhesion Laboratory, Imperial Cancer Research Fund, John Radcliffe Hospital, Headington, Oxford, United Kingdom.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't