Intestinal trefoil factor (TFF 3) and pS2 (TFF 1), but not spasmolytic polypeptide (TFF 2) mRNAs are co-expressed in normal, hyperplastic, and neoplastic human breast epithelium

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Intestinal trefoil factor (TFF 3) and pS2 (TFF 1), but not spasmolytic polypeptide (TFF 2) mRNAs are co-expressed in normal, hyperplastic, and neoplastic human breast epithelium. / Poulsom, R; Hanby, A M; Lalani, E N; Hauser, F; Hoffmann, W; Stamp, G W.

In: Journal of Pathology, Vol. 183, No. 1, 09.1997, p. 30-8.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Poulsom, R, Hanby, AM, Lalani, EN, Hauser, F, Hoffmann, W & Stamp, GW 1997, 'Intestinal trefoil factor (TFF 3) and pS2 (TFF 1), but not spasmolytic polypeptide (TFF 2) mRNAs are co-expressed in normal, hyperplastic, and neoplastic human breast epithelium', Journal of Pathology, vol. 183, no. 1, pp. 30-8. https://doi.org/10.1002/(SICI)1096-9896(199709)183:1<30::AID-PATH1085>3.0.CO;2-K

APA

Poulsom, R., Hanby, A. M., Lalani, E. N., Hauser, F., Hoffmann, W., & Stamp, G. W. (1997). Intestinal trefoil factor (TFF 3) and pS2 (TFF 1), but not spasmolytic polypeptide (TFF 2) mRNAs are co-expressed in normal, hyperplastic, and neoplastic human breast epithelium. Journal of Pathology, 183(1), 30-8. https://doi.org/10.1002/(SICI)1096-9896(199709)183:1<30::AID-PATH1085>3.0.CO;2-K

Vancouver

Poulsom R, Hanby AM, Lalani EN, Hauser F, Hoffmann W, Stamp GW. Intestinal trefoil factor (TFF 3) and pS2 (TFF 1), but not spasmolytic polypeptide (TFF 2) mRNAs are co-expressed in normal, hyperplastic, and neoplastic human breast epithelium. Journal of Pathology. 1997 Sep;183(1):30-8. https://doi.org/10.1002/(SICI)1096-9896(199709)183:1<30::AID-PATH1085>3.0.CO;2-K

Author

Poulsom, R ; Hanby, A M ; Lalani, E N ; Hauser, F ; Hoffmann, W ; Stamp, G W. / Intestinal trefoil factor (TFF 3) and pS2 (TFF 1), but not spasmolytic polypeptide (TFF 2) mRNAs are co-expressed in normal, hyperplastic, and neoplastic human breast epithelium. In: Journal of Pathology. 1997 ; Vol. 183, No. 1. pp. 30-8.

Bibtex

@article{8143f13170254b9faee4d6fbf5b13820,
title = "Intestinal trefoil factor (TFF 3) and pS2 (TFF 1), but not spasmolytic polypeptide (TFF 2) mRNAs are co-expressed in normal, hyperplastic, and neoplastic human breast epithelium",
abstract = "pS2-TFF 1 is expressed in breast cancers and has been investigated as a potential prognostic factor reflecting oestrogen dependence. The relationship to the expression of other trefoil peptides, human spasmolytic polypeptide (hSP-TFF 2) and intestinal trefoil factor (hITF/hPI.B-TFF 3) is documented here. Fifty-seven breast specimens were selected from surgical pathology archives and included five normal breasts (two lactating), seven benign proliferative lesions, 11 ductal carcinomas in situ (DCIS), three lobular carcinomas in situ (LCIS), 24 invasive ductal carcinomas (IDC), and seven invasive lobular carcinomas (ILC). The comparative distribution of trefoil mRNAs was assessed by in situ hybridization using 35S-labelled riboprobes and immunohistochemical staining for pS2-TFF 1 and hSP-TFF 2. pS2-TFF 1 and hITF/hPI.B-TFF 3 mRNA were focally present at low signal intensity in normal and benign breast. Both pS2-TFF 1 and hITF/hPI.B-TFF 3 were expressed in all DCIS, LCIS and ILC, and 21/24 IDC. Overall, expression patterns of pS2-TFF 1 and hITF/hPI.B-TFF 3 coincided, but hITF/hPI.B-TFF 3 mRNA was usually found in a greater proportion of cells. Expression of hSP-TFF 2 peptide or mRNA was not detected in any of these cases. MCF 7 breast carcinoma cells also expressed hITF/hPI.B-TFF 3 and pS2-TFF 1 mRNAs but not hSP-TFF 2. hITF/hPI.B-TFF 3 co-expression with pS2-TFF 1 may act as a prognostic factor, but also raises questions about the regulatory pathway for pS2-TFF 1 hITF/hPI.B-TFF 3. Trefoil factors have effects on cell motility and spreading in vitro, and co-expression of hITF/hPI.B-TFF 3 with pS2-TFF 1 could be functionally significant if they form a heterodimer or compete for receptor binding. Absence of hSP-TFF 2 expression may be of equal relevance to tumour cell biology.",
keywords = "Blotting, Northern, Breast/metabolism, Breast Neoplasms/metabolism, Carcinoma, Ductal, Breast/metabolism, Carcinoma, Lobular/metabolism, Female, Growth Substances/genetics, Humans, Hyperplasia/metabolism, Immunoenzyme Techniques, In Situ Hybridization, Mucins, Muscle Proteins, Neoplasm Invasiveness, Neoplasm Proteins/metabolism, Neuropeptides, Peptides/genetics, Precancerous Conditions/metabolism, Proteins/genetics, RNA, Messenger/genetics, Trefoil Factor-1, Trefoil Factor-2, Trefoil Factor-3, Tumor Suppressor Proteins",
author = "R Poulsom and Hanby, {A M} and Lalani, {E N} and F Hauser and W Hoffmann and Stamp, {G W}",
year = "1997",
month = sep,
doi = "10.1002/(SICI)1096-9896(199709)183:1<30::AID-PATH1085>3.0.CO;2-K",
language = "English",
volume = "183",
pages = "30--8",
journal = "Journal of Pathology",
issn = "0022-3417",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - Intestinal trefoil factor (TFF 3) and pS2 (TFF 1), but not spasmolytic polypeptide (TFF 2) mRNAs are co-expressed in normal, hyperplastic, and neoplastic human breast epithelium

AU - Poulsom, R

AU - Hanby, A M

AU - Lalani, E N

AU - Hauser, F

AU - Hoffmann, W

AU - Stamp, G W

PY - 1997/9

Y1 - 1997/9

N2 - pS2-TFF 1 is expressed in breast cancers and has been investigated as a potential prognostic factor reflecting oestrogen dependence. The relationship to the expression of other trefoil peptides, human spasmolytic polypeptide (hSP-TFF 2) and intestinal trefoil factor (hITF/hPI.B-TFF 3) is documented here. Fifty-seven breast specimens were selected from surgical pathology archives and included five normal breasts (two lactating), seven benign proliferative lesions, 11 ductal carcinomas in situ (DCIS), three lobular carcinomas in situ (LCIS), 24 invasive ductal carcinomas (IDC), and seven invasive lobular carcinomas (ILC). The comparative distribution of trefoil mRNAs was assessed by in situ hybridization using 35S-labelled riboprobes and immunohistochemical staining for pS2-TFF 1 and hSP-TFF 2. pS2-TFF 1 and hITF/hPI.B-TFF 3 mRNA were focally present at low signal intensity in normal and benign breast. Both pS2-TFF 1 and hITF/hPI.B-TFF 3 were expressed in all DCIS, LCIS and ILC, and 21/24 IDC. Overall, expression patterns of pS2-TFF 1 and hITF/hPI.B-TFF 3 coincided, but hITF/hPI.B-TFF 3 mRNA was usually found in a greater proportion of cells. Expression of hSP-TFF 2 peptide or mRNA was not detected in any of these cases. MCF 7 breast carcinoma cells also expressed hITF/hPI.B-TFF 3 and pS2-TFF 1 mRNAs but not hSP-TFF 2. hITF/hPI.B-TFF 3 co-expression with pS2-TFF 1 may act as a prognostic factor, but also raises questions about the regulatory pathway for pS2-TFF 1 hITF/hPI.B-TFF 3. Trefoil factors have effects on cell motility and spreading in vitro, and co-expression of hITF/hPI.B-TFF 3 with pS2-TFF 1 could be functionally significant if they form a heterodimer or compete for receptor binding. Absence of hSP-TFF 2 expression may be of equal relevance to tumour cell biology.

AB - pS2-TFF 1 is expressed in breast cancers and has been investigated as a potential prognostic factor reflecting oestrogen dependence. The relationship to the expression of other trefoil peptides, human spasmolytic polypeptide (hSP-TFF 2) and intestinal trefoil factor (hITF/hPI.B-TFF 3) is documented here. Fifty-seven breast specimens were selected from surgical pathology archives and included five normal breasts (two lactating), seven benign proliferative lesions, 11 ductal carcinomas in situ (DCIS), three lobular carcinomas in situ (LCIS), 24 invasive ductal carcinomas (IDC), and seven invasive lobular carcinomas (ILC). The comparative distribution of trefoil mRNAs was assessed by in situ hybridization using 35S-labelled riboprobes and immunohistochemical staining for pS2-TFF 1 and hSP-TFF 2. pS2-TFF 1 and hITF/hPI.B-TFF 3 mRNA were focally present at low signal intensity in normal and benign breast. Both pS2-TFF 1 and hITF/hPI.B-TFF 3 were expressed in all DCIS, LCIS and ILC, and 21/24 IDC. Overall, expression patterns of pS2-TFF 1 and hITF/hPI.B-TFF 3 coincided, but hITF/hPI.B-TFF 3 mRNA was usually found in a greater proportion of cells. Expression of hSP-TFF 2 peptide or mRNA was not detected in any of these cases. MCF 7 breast carcinoma cells also expressed hITF/hPI.B-TFF 3 and pS2-TFF 1 mRNAs but not hSP-TFF 2. hITF/hPI.B-TFF 3 co-expression with pS2-TFF 1 may act as a prognostic factor, but also raises questions about the regulatory pathway for pS2-TFF 1 hITF/hPI.B-TFF 3. Trefoil factors have effects on cell motility and spreading in vitro, and co-expression of hITF/hPI.B-TFF 3 with pS2-TFF 1 could be functionally significant if they form a heterodimer or compete for receptor binding. Absence of hSP-TFF 2 expression may be of equal relevance to tumour cell biology.

KW - Blotting, Northern

KW - Breast/metabolism

KW - Breast Neoplasms/metabolism

KW - Carcinoma, Ductal, Breast/metabolism

KW - Carcinoma, Lobular/metabolism

KW - Female

KW - Growth Substances/genetics

KW - Humans

KW - Hyperplasia/metabolism

KW - Immunoenzyme Techniques

KW - In Situ Hybridization

KW - Mucins

KW - Muscle Proteins

KW - Neoplasm Invasiveness

KW - Neoplasm Proteins/metabolism

KW - Neuropeptides

KW - Peptides/genetics

KW - Precancerous Conditions/metabolism

KW - Proteins/genetics

KW - RNA, Messenger/genetics

KW - Trefoil Factor-1

KW - Trefoil Factor-2

KW - Trefoil Factor-3

KW - Tumor Suppressor Proteins

U2 - 10.1002/(SICI)1096-9896(199709)183:1<30::AID-PATH1085>3.0.CO;2-K

DO - 10.1002/(SICI)1096-9896(199709)183:1<30::AID-PATH1085>3.0.CO;2-K

M3 - Journal article

C2 - 9370944

VL - 183

SP - 30

EP - 38

JO - Journal of Pathology

JF - Journal of Pathology

SN - 0022-3417

IS - 1

ER -

ID: 347885748