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pubmed-article:3146413pubmed:abstractTextWe have previously reported that pS2 mRNA expressed in cultured epithelial cells derived from a hormone-dependent breast carcinoma (MCF-7 cells) is also expressed in mucosa cells of normal human stomach. This mRNA encodes a putative 84 amino-acid-long protein, which is secreted by both cell types after elimination of a signal peptide. We report here the purification of the pS2 protein, its trypsin digestion and amino-acid sequencing. The MCF-7 cell-secreted protein is 60 amino-acid-long and its sequence is in complete agreement with that deduced from the mRNA sequence. The presence of an N-terminal glutamic acid indicates that the signal peptidase releases a 24 amino-acid-long signal peptide. Analysis of tryptic peptides derived from the secreted gastric pS2 protein indicates that the signal peptide and the sequence of the first 48 amino-acids are identical to those of secreted MCF-7 pS2 protein, although the N-terminal amino-acid of the gastric protein may be cyclized as a pyroglumatic acid.lld:pubmed
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pubmed-article:3146413pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:3146413pubmed:articleTitle[Primary structure of human protein pS2].lld:pubmed
pubmed-article:3146413pubmed:affiliationLaboratoire de Génétique moléculaire des Eucaryotes du C.N.R.S., Strasbourg.lld:pubmed
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