title: Association of the human spasmolytic polypeptide and an estrogen-induced breast cancer protein (pS2) with human pancreatic carcinoma.
abstract: The human pS2 gene, isolated from the breast carcinoma cell line MCF-7 and shown to be under estrogen transcriptional control in a subclass of breast cancer cells was reported to be secreted in normal stomach surface epithelial cells, whereas additional gastrointestinal tissues like pancreas and colon do not secrete pS2 at all. In porcine pancreas, a spasmolytic polypeptide (sharing domains of homology with pS2) was observed; a corresponding human gene (hSP) was shown to be active in normal stomach mucosa. hSP and pS2 gene activity in normal and neoplastic pancreas tissues was then compared. Whereas both genes are inactive in normal pancreatic cells, activation of the pS2 sequence in a primary pancreatic carcinoma cell culture and in 23 tumor tissues was noted when investigated by immunostaining. In all cases when pS2 showed a regular 0.6 kb transcript, hSP displayed a transcript of 0.7 kb. Six of these tumors showed a reduced pS2 immunoreactivity and, at the same time, aberrant pS2 mRNA bands and a complete shut-down of the hSP gene were noted. In one case, whereas normal pancreas remained negative, the corresponding tumor and its metastasis displayed regular transcripts of pS2 and hSP. This remarkably high correlation suggests that pS2 and hSP expression in the pancreatic tumors, but not in their corresponding healthy tissue is significantly linked to molecular steps leading to tumorigenesis.
authors.affiliation: Institut für Humangenetik, Homburg/Saar, Federal Republic of Germany.
authors.forename: C
authors.initials: C
authors.lastname: Welter
authors.forename: B
authors.initials: B
authors.lastname: Theisinger
authors.forename: G
authors.initials: G
authors.lastname: Seitz
authors.forename: C
authors.initials: C
authors.lastname: Tomasetto
authors.forename: M C
authors.initials: MC
authors.lastname: Rio
authors.forename: P
authors.initials: P
authors.lastname: Chambon
authors.forename: N
authors.initials: N
authors.lastname: Blin
mesh_terms: D000230:Adenocarcinoma / Q000737:chemistry* / Q000235:genetics; D001943:Breast Neoplasms / Q000737:chemistry / Q000235:genetics; D015870:Gene Expression; D006801:Humans; D007124:Immunoenzyme Techniques; D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009363:Neoplasm Proteins / Q000032:analysis* / Q000235:genetics; D009479:Neuropeptides; D010190:Pancreatic Neoplasms / Q000737:chemistry* / Q000235:genetics; D010455:Peptides / Q000032:analysis*; D011506:Proteins / Q000032:analysis*; D012334:RNA, Neoplasm / Q000032:analysis; D011960:Receptors, Estrogen; D000071163:Trefoil Factor-1; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D025521:Tumor Suppressor Proteins
chemical_list: C059917:ERD5 protein, human; D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009363:Neoplasm Proteins; D009479:Neuropeptides; D010455:Peptides; D011506:Proteins; D012334:RNA, Neoplasm; D011960:Receptors, Estrogen; C051838:TFF1 protein, human; C099037:TFF3 protein, rat; C000604008:Tff2 protein, rat; D000071163:Trefoil Factor-1; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D025521:Tumor Suppressor Proteins; C034407:pancreatic spasmolytic polypeptide