Linked Life Data

8163496

Source:http://linkedlifedata.com/resource/pubmed/id/8163496

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1994-5-26
pubmed:databankReference
pubmed:abstractText
Ascites sublines of the highly metastatic 13762 rat mammary adenocarcinoma contain abundant amounts of a heterodimeric cell surface glycoprotein complex composed of a mucin subunit ASGP-1 (ascites sialoglycoprotein-1) and a transmembrane subunit (ASGP-2). Previous studies showed that the complex is synthesized from a single polypeptide encoded by a 9 kb transcript. The sequence of the transmembrane subunit was obtained from a 5-kilobase (kb) cDNA isolated from a plasmid library (Sheng, Z., Wu, K., Carraway, K. L., and Fregien, N. (1992) J. Biol. Chem. 267, 16341-16346). Completion of the sequence of this cDNA revealed the C-terminal domain of ASGP-1, which is rich in serine and threonine but contains no typical mucin-type repeats. The remainder of the sequence of ASGP-1 and the 9-kb transcript was obtained by two 5'-RACE (rapid amplification of cDNA ends) steps and primer extension analysis. These results revealed that the 5' half of the 9-kb transcript contains a short 5'-noncoding region and encodes a signal sequence, a short nonrepeat region, and a repeat domain containing 11 repeats. Nine of these repeats are found in tandem, but the two end repeats are separated from the others by short unique sequences. The repeats vary from 117-124 amino acids and are 70-90% identical to a consensus sequence. Overall, the sequence predicts that ASGP-1 contains 2172 amino acids (M(r) 224,190), 43% of which are serine and threonine. We propose that the complex of this mucin and its transmembrane subunit, which contains growth factor-modulating activity, may play an important role in tumor progression.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11950-5
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8163496-Adenocarcinoma, pubmed-meshheading:8163496-Amino Acid Sequence, pubmed-meshheading:8163496-Animals, pubmed-meshheading:8163496-Base Sequence, pubmed-meshheading:8163496-Cloning, Molecular, pubmed-meshheading:8163496-DNA Primers, pubmed-meshheading:8163496-Female, pubmed-meshheading:8163496-Mammary Neoplasms, Experimental, pubmed-meshheading:8163496-Membrane Glycoproteins, pubmed-meshheading:8163496-Molecular Sequence Data, pubmed-meshheading:8163496-Mucin-4, pubmed-meshheading:8163496-Neoplasm Proteins, pubmed-meshheading:8163496-Polymerase Chain Reaction, pubmed-meshheading:8163496-RNA, Neoplasm, pubmed-meshheading:8163496-Rats, pubmed-meshheading:8163496-Repetitive Sequences, Nucleic Acid, pubmed-meshheading:8163496-Sequence Homology, Amino Acid, pubmed-meshheading:8163496-Sialoglycoproteins
pubmed:year
1994
pubmed:articleTitle
Molecular cloning and sequencing of the mucin subunit of a heterodimeric, bifunctional cell surface glycoprotein complex of ascites rat mammary adenocarcinoma cells.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Florida 33101.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.