Linked Life Data

3379044

Source:http://linkedlifedata.com/resource/pubmed/id/3379044

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1988-7-27
pubmed:databankReference
pubmed:abstractText
We have isolated and sequenced a cDNA clone encoding the mouse LAMP-1 (mLAMP-1) major lysosomal membrane glycoprotein. The deduced protein sequence, which included the NH2-terminal portion of the mLAMP-1 molecule, consisted of 382 amino acids (Mr 41,509). The predicted structure of this protein included an NH2-terminal intralumenal domain consisting of two homology units of approximately 160 residues each separated by a proline-rich hinge region. Each homology unit contained four cysteine residues with two intercysteine intervals of 36-38 residues and one of 68 or 76 residues. The molecule also contained 20 asparagine-linked glycosylation sites within residues 1-287, a membrane-spanning region from residues 347 to 370, and a carboxyl-terminal cytoplasmic domain of 12 residues. The biochemical properties and amino acid sequence of mLAMP-1 were highly similar to those of two other molecules that have been studied as cell surface onco-differentiation antigens: a highly sialylated polylactosaminoglycan-containing glycoprotein isolated from human chronic myelogenous leukemia cells (Viitala, J., Carlsson, S. R., Siebert, P. D., and Fukuda, M. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, in press) and the mouse gp130 (P2B) glycoprotein, in which an increase in beta 1-6 branching of asparagine-linked oligosaccharides has been correlated with metastatic potential in certain tumor cells (Dennis, J.W., Laferte, S., Waghorne, C., Breitman, M.L., and Kerbel, R.S. (1987) Science 236, 582-585).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8754-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:3379044-Amino Acid Sequence, pubmed-meshheading:3379044-Animals, pubmed-meshheading:3379044-Antigens, CD, pubmed-meshheading:3379044-Antigens, Differentiation, pubmed-meshheading:3379044-Base Sequence, pubmed-meshheading:3379044-Cell Line, pubmed-meshheading:3379044-Cells, Cultured, pubmed-meshheading:3379044-DNA, pubmed-meshheading:3379044-Genes, pubmed-meshheading:3379044-Humans, pubmed-meshheading:3379044-Leukemia, pubmed-meshheading:3379044-Lysosomal-Associated Membrane Protein 1, pubmed-meshheading:3379044-Lysosome-Associated Membrane Glycoproteins, pubmed-meshheading:3379044-Lysosomes, pubmed-meshheading:3379044-Membrane Glycoproteins, pubmed-meshheading:3379044-Mice, pubmed-meshheading:3379044-Molecular Sequence Data, pubmed-meshheading:3379044-Oncogenes, pubmed-meshheading:3379044-Sequence Homology, Nucleic Acid
pubmed:year
1988
pubmed:articleTitle
Isolation and sequencing of a cDNA clone encoding lysosomal membrane glycoprotein mouse LAMP-1. Sequence similarity to proteins bearing onco-differentiation antigens.
pubmed:affiliation
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't