pubmed-article:1379596 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:1379596 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:1379596 | pubmed:dateCreated | 1992-9-10 | lld:pubmed |
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pubmed-article:1379596 | pubmed:abstractText | Ascites sublines of the 13762 rat mammary adenocarcinoma have a cell surface sialomucin complex composed of the sialomucin ascites sialoglycoprotein-1 (ASGP-1) and the membrane-associated glycoprotein ASGP-2. The sialomucin complex is synthesized as a high M(r) precursor, pre-sialomucin complex (pSMC-1). To characterize the structure of the membrane-associated component of this complex, a lambda gt11 cDNA expression library was constructed using mRNA from 13762 rat mammary adenocarcinoma cells and screened with polyclonal antibody against ASGP-2. The strongest antibody-binding clone, designated lambda ASGP2.9-1, had a 1.3-kilobase (kb) insert, and hybridized to a 9-kb transcript in 13762 cell mRNA. The large size of this transcript was expected, since the estimated molecular mass of pSMC-1 is greater than 250 kDa. To obtain the full sequence of ASGP-2, a longer cDNA (5.4 kb), designated pASGP1/2.1, was subsequently cloned by screening a plasmid library with an oligonucleotide complementary to the 5' end of the phage insert. The amino acid sequence derived from nucleotide sequence of pASGP1/2.1 showed a 12-amino acid identity with amino acid sequence obtained from the NH2 terminus of ASGP-2, indicating the entire ASGP-2 coding region was included in the cDNA. Furthermore, an 18-amino acid identity with the NH2 terminus of a 6-kDa CNBr fragment of ASGP-2 was also observed in the cDNA sequence. The polypeptide contains several distinct domains, including a hydrophobic transmembrane domain, a short (20 residue) COOH-terminal cytoplasmic tail, and a large extracellular domain with 24 potential N-glycosylation sites. These properties correspond to features of ASGP-2 and pSMC-1 predicted by previous biochemical studies. Most interestingly, the extracellular domain contains two cysteine-rich sequences, each of which has a segment with strong similarities to proteins with epidermal growth factor activity. Since our recent studies show that ASGP-2 can modulate epidermal growth factor receptor phosphorylation activity, these results provide structural evidence to support the role of the heterodimeric sialomucin complex as a bifunctional modulator of cellular interactions and cell proliferation. | lld:pubmed |
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pubmed-article:1379596 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1379596 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1379596 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1379596 | pubmed:month | Aug | lld:pubmed |
pubmed-article:1379596 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1379596 | pubmed:author | pubmed-author:CarrawayK LKL | lld:pubmed |
pubmed-article:1379596 | pubmed:author | pubmed-author:WuKK | lld:pubmed |
pubmed-article:1379596 | pubmed:author | pubmed-author:ShengZZ | lld:pubmed |
pubmed-article:1379596 | pubmed:author | pubmed-author:FregienNN | lld:pubmed |
pubmed-article:1379596 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1379596 | pubmed:day | 15 | lld:pubmed |
pubmed-article:1379596 | pubmed:volume | 267 | lld:pubmed |
pubmed-article:1379596 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1379596 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1379596 | pubmed:pagination | 16341-6 | lld:pubmed |
pubmed-article:1379596 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:1379596 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1379596 | pubmed:articleTitle | Molecular cloning of the transmembrane component of the 13762 mammary adenocarcinoma sialomucin complex. A new member of the epidermal growth factor superfamily. | lld:pubmed |
pubmed-article:1379596 | pubmed:affiliation | Department of Molecular Biology and Biochemistry, University of Miami School of Medicine, Florida 33101. | lld:pubmed |
pubmed-article:1379596 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1379596 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:1379596 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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