hP1.B, a human P-domain peptide homologous with rat intestinal trefoil factor, is expressed also in the ulcer-associated cell lineage and the uterus.
The six-cysteine P-domain motif forms the basic repeat unit of a growing family of mucin-associated peptides. A precursor for a human secretory polypeptide has been discovered by molecular cloning and deduced to have a single P-domain, termed hP1.B. The pre-pro-peptide has 67% amino acid identity with rat intestinal trefoil factor. We find, using the techniques of RNA analysis and in situ hybridization, that this P-domain peptide is expressed in the human gastrointestinal tract, where a number of pathological conditions affect its expression, and surprisingly find it is expressed in the uterus also. In the intestine, hP1.B is expressed by goblet cells, but in Crohn disease this peptide is synthesized and secreted additionally by the ulcer-associated cell lineage that is known to secrete two other trefoil peptides, pS2 and spasmolytic polypeptide (hSP). In the stomach, hP1.B mRNA is relatively scarce but is more abundant in foci of intestinal metaplasia and near to ulceration. Mucin-rich epithelial cells in hyperplastic polyps of the colon also express this peptide. The discovery of this P-domain peptide and its expression in association with mucins support the hypothesis that P-domains with mucins may subserve related functions in the maintenance and repair of mucosal function.
Hauser
F
F
Max-Planck-Institut für Psychiatrie, Abteilung Neurochemie, Martinsried, Federal Republic of Germany.
Poulsom
R
R
Chinery
R
R
Rogers
L A
LA
Hanby
A M
AM
Wright
N A
NA
Hoffmann
W
W
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004064:Digestive System / Q000378:metabolism*; D005260:Female; D015870:Gene Expression; D005796:Genes; D006133:Growth Substances / Q000235:genetics*; D006801:Humans; D017403:In Situ Hybridization; D008969:Molecular Sequence Data; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D010455:Peptides; D011506:Proteins / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics; D016415:Sequence Alignment; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D014599:Uterus / Q000378:metabolism
D006133:Growth Substances; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D009838:Oligodeoxyribonucleotides; D010455:Peptides; D011506:Proteins; D012333:RNA, Messenger; C082495:TFF3 protein, human; C099037:TFF3 protein, rat; C000604008:Tff2 protein, rat; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3