title: The mouse one P-domain (pS2) and two P-domain (mSP) genes exhibit distinct patterns of expression.
abstract: We have previously shown that the human pS2 gene, which codes for a secreted peptide of 60 amino acids, is expressed in a number of human carcinomas, including carcinomas of the breast, the pancreas, and the large bowel. Strong pS2 gene expression was also observed in the normal gastric mucosa and in the regenerative tissues surrounding ulcerous lesions of the gastrointestinal tract. A number of pS2 similar peptides, designated as P-domain peptides, have been described, notably the porcine (PSP), murine (mSP), and human (hSP) spasmolytic polypeptides, which correspond to duplicated pS2 proteins. We have now cloned a mouse homolog of the human pS2 cDNA to dispose of an animal model to study the pS2 protein function, which remains unknown at the present time. We show that the mouse putative pS2 protein sequence and the physiological pattern of expression of the mouse pS2 gene are well conserved. The mouse pS2 gene is highly expressed in the stomach mucosa cells, whereas no pS2 gene expression could be detected in the mouse mammary gland, even during postnatal development processes dependent on growth factors or hormones. Using in situ hybridization, we show that although coexpressed in the fundus, the antrum and the antrum-pyloric regions of the stomach, the mouse pS2 and mSP genes exhibit distinct and complementary cellular patterns of expression.
authors.affiliation: Laboratoire de Génétique Moléculaire des Eucaryotes du Centre National de la Recherche Scientific, Institut National de la Santé et de la Recherche Médicale, Strasbourg, France.
authors.forename: O
authors.initials: O
authors.lastname: Lefebvre
authors.forename: C
authors.initials: C
authors.lastname: Wolf
authors.forename: M
authors.initials: M
authors.lastname: Kédinger
authors.forename: M P
authors.initials: MP
authors.lastname: Chenard
authors.forename: C
authors.initials: C
authors.lastname: Tomasetto
authors.forename: P
authors.initials: P
authors.lastname: Chambon
authors.forename: M C
authors.initials: MC
authors.lastname: Rio
mesh_terms: D000375:Aging / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics*; D001483:Base Sequence; D015152:Blotting, Northern; D004247:DNA; D004064:Digestive System / Q000378:metabolism; D005753:Gastric Mucosa / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D017403:In Situ Hybridization; D007413:Intestinal Mucosa / Q000378:metabolism; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000096:biosynthesis* / Q000235:genetics*; D009838:Oligodeoxyribonucleotides; D009928:Organ Specificity; D045332:Photosystem II Protein Complex; D016133:Polymerase Chain Reaction; D011506:Proteins; D012333:RNA, Messenger / Q000032:analysis / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D000071163:Trefoil Factor-1; D025521:Tumor Suppressor Proteins; D014981:Xenopus
chemical_list: D001426:Bacterial Proteins; D009363:Neoplasm Proteins; D009838:Oligodeoxyribonucleotides; D045332:Photosystem II Protein Complex; D011506:Proteins; D012333:RNA, Messenger; C051838:TFF1 protein, human; D000071163:Trefoil Factor-1; D025521:Tumor Suppressor Proteins; C054266:photosystem II manganese-stabilizing protein; D004247:DNA