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hSP, the domain‐duplicated homolog of pS2 protein, is co‐expressed with pS2 in stomach but not in breast carcinoma.
Author(s) -
Tomasetto C.,
Rio M.C.,
Gautier C.,
Wolf C.,
Hareuveni M.,
Chambon P.,
Lathe R.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb08125.x
Subject(s) - library science , physics , computer science
Approximately 50% of human breast tumors secrete a small cysteine‐rich protein, pS2, of unknown function. pS2 protein was recently found to be homologous to a porcine protein with hormonogastric activity, pancreatic spasmolytic polypeptide (PSP), in which the 5‐cysteine domain present in pS2 is tandemly duplicated. We have characterized cDNA species encoding PSP and its human and mouse counterparts, hSP and mSP. We show that hSP and pS2 are separately encoded in the genome, and that the two proteins are co‐expressed in normal stomach epithelium. However, expression of hSP was not detected in breast tumors. Computer analysis revealed that the pattern of conserved cysteine residues in hSP and pS2, the P domain, is present at the N termini of two other mammalian proteins, intestinal sucrase‐isomaltase and lysosomal alpha‐glucosidase.