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α-Transforming Growth Factor in the Bovine Anterior Pituitary Gland: Secretion by Dispersed Cells and Immunohistochemical Localization

α-Transforming Growth Factor in the Bovine Anterior Pituitary Gland: Secretion by Dispersed Cells... Abstract A growth factor secreted by bovine calf anterior pituitary cells in culture was purified, and its N-terminal amino acid sequence was determined. This sequence shows near-identity with human and rat α-transforming growth factor (αTGF). With the use of an anti-αTGF monoclonal antibody generated against a C-terminal rat aTGF synthetic peptide, αTGF-like material was localized by immunohistochemical techniques in the cytoplasm of normal bovine adenohypophysial cells. The antibody staining was immunospecific because it could be completely inhibited by saturating concentrations of the synthetic peptide to which it was raised. There was no immunoreactivity in cells of the intermediate and posterior lobes. Some of the cells containing αTGF immunoreactivity also contained PRL; αTGF immunoreactivity was not demonstrated in cells containing ACTH, TSH, FSH, and LH. This is the first report documenting the secretion of αTGF by nonneoplastic adult cells and the presence of αTGF immunoreactivity in the corresponding normal adult tissue. (Endocrinology121: 1412–1416,1987) This content is only available as a PDF. Author notes * This work was supported by grants from the Medical Research Council of Canada and the NCI (Canada). † Medical Scholar of the Ontario Cancer Treatment and Research Foundation. Copyright © 1987 by The Endocrine Society http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Endocrinology Oxford University Press

α-Transforming Growth Factor in the Bovine Anterior Pituitary Gland: Secretion by Dispersed Cells and Immunohistochemical Localization

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References (21)

Publisher
Oxford University Press
Copyright
Copyright © 1987 by The Endocrine Society
ISSN
0013-7227
eISSN
1945-7170
DOI
10.1210/endo-121-4-1412
Publisher site
See Article on Publisher Site

Abstract

Abstract A growth factor secreted by bovine calf anterior pituitary cells in culture was purified, and its N-terminal amino acid sequence was determined. This sequence shows near-identity with human and rat α-transforming growth factor (αTGF). With the use of an anti-αTGF monoclonal antibody generated against a C-terminal rat aTGF synthetic peptide, αTGF-like material was localized by immunohistochemical techniques in the cytoplasm of normal bovine adenohypophysial cells. The antibody staining was immunospecific because it could be completely inhibited by saturating concentrations of the synthetic peptide to which it was raised. There was no immunoreactivity in cells of the intermediate and posterior lobes. Some of the cells containing αTGF immunoreactivity also contained PRL; αTGF immunoreactivity was not demonstrated in cells containing ACTH, TSH, FSH, and LH. This is the first report documenting the secretion of αTGF by nonneoplastic adult cells and the presence of αTGF immunoreactivity in the corresponding normal adult tissue. (Endocrinology121: 1412–1416,1987) This content is only available as a PDF. Author notes * This work was supported by grants from the Medical Research Council of Canada and the NCI (Canada). † Medical Scholar of the Ontario Cancer Treatment and Research Foundation. Copyright © 1987 by The Endocrine Society

Journal

Endocrinology – Oxford University Press

Published: Oct 1, 1987

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