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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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. / Hauser, F; Poulsom, R; Chinery, R; Rogers, L A; Hanby, A M; Wright, N A; Hoffmann, W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 90, No. 15, 01.08.1993, p. 6961-5.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hauser, F, Poulsom, R, Chinery, R, Rogers, LA, Hanby, AM, Wright, NA & Hoffmann, W 1993, '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', Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 15, pp. 6961-5. https://doi.org/10.1073/pnas.90.15.6961

APA

Hauser, F., Poulsom, R., Chinery, R., Rogers, L. A., Hanby, A. M., Wright, N. A., & Hoffmann, W. (1993). 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. Proceedings of the National Academy of Sciences of the United States of America, 90(15), 6961-5. https://doi.org/10.1073/pnas.90.15.6961

Vancouver

Hauser F, Poulsom R, Chinery R, Rogers LA, Hanby AM, Wright NA et al. 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. Proceedings of the National Academy of Sciences of the United States of America. 1993 Aug 1;90(15):6961-5. https://doi.org/10.1073/pnas.90.15.6961

Author

Hauser, F ; Poulsom, R ; Chinery, R ; Rogers, L A ; Hanby, A M ; Wright, N A ; Hoffmann, W. / 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. In: Proceedings of the National Academy of Sciences of the United States of America. 1993 ; Vol. 90, No. 15. pp. 6961-5.

Bibtex

@article{8b44ce4a46394ec0875398bf5fe62a9e,
title = "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",
abstract = "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.",
keywords = "Amino Acid Sequence, Base Sequence, Cloning, Molecular, Digestive System/metabolism, Female, Gene Expression, Genes, Growth Substances/genetics, Humans, In Situ Hybridization, Molecular Sequence Data, Mucins, Muscle Proteins, Neuropeptides, Oligodeoxyribonucleotides/chemistry, Peptides, Proteins/genetics, RNA, Messenger/genetics, Sequence Alignment, Trefoil Factor-2, Trefoil Factor-3, Uterus/metabolism",
author = "F Hauser and R Poulsom and R Chinery and Rogers, {L A} and Hanby, {A M} and Wright, {N A} and W Hoffmann",
year = "1993",
month = aug,
day = "1",
doi = "10.1073/pnas.90.15.6961",
language = "English",
volume = "90",
pages = "6961--5",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "15",

}

RIS

TY - JOUR

T1 - 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

AU - Hauser, F

AU - Poulsom, R

AU - Chinery, R

AU - Rogers, L A

AU - Hanby, A M

AU - Wright, N A

AU - Hoffmann, W

PY - 1993/8/1

Y1 - 1993/8/1

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Base Sequence

KW - Cloning, Molecular

KW - Digestive System/metabolism

KW - Female

KW - Gene Expression

KW - Genes

KW - Growth Substances/genetics

KW - Humans

KW - In Situ Hybridization

KW - Molecular Sequence Data

KW - Mucins

KW - Muscle Proteins

KW - Neuropeptides

KW - Oligodeoxyribonucleotides/chemistry

KW - Peptides

KW - Proteins/genetics

KW - RNA, Messenger/genetics

KW - Sequence Alignment

KW - Trefoil Factor-2

KW - Trefoil Factor-3

KW - Uterus/metabolism

U2 - 10.1073/pnas.90.15.6961

DO - 10.1073/pnas.90.15.6961

M3 - Journal article

C2 - 8346203

VL - 90

SP - 6961

EP - 6965

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 15

ER -

ID: 347885881