Immunocytochemical identification of basic fibroblast growth factor in the developing rat mammary gland: variations in location are dependent on glandular structure and differentiationPS Rudland, AM Platt-Higgins, MC Wilkinson and DG Fernig Department of Biochemistry, University of Liverpool, United Kingdom. We raised antiserum to human recombinant basic fibroblast growth factor (rbFGF) in rabbits. With this affinity-purified antiserum, other antisera to rbFGF, and commercial antiserum to bovine pituitary bFGF, we undertook immunocytochemical detection of bFGF in histological sections of rat mammary glands at different developmental stages. In non-growing ducts, anti-bFGF serum stains the basement membrane/myoepithelial cells, whereas in serial sections most of this stain is observed to be associated with anti-laminin-staining basement membranes rather than with anti-callus-keratin-staining myoepithelial cells. The weak staining of the myoepithelial cells is enhanced when NiCl2 is included in the detection system, but little staining for bFGF is observed in the epithelial cells. In growing neonatal ducts from 1- day-old rats, in growing terminal end buds (TEBs) and, to a lesser extent, in growing alveolar buds (ABs) in prepubescent (21-day) and pubescent (50-day) rats, both their inner and outer cells are stained moderately by anti-bFGF sera. In non-growing ducts from rats aged 6 days, in non-growing ABs of rats aged 60 days and more, and in alveoli from pregnant and lactating rats, only the basement membrane/myoepithelial cell area is stained by anti-bFGF sera; the epithelial cells are unstained. Staining of the myoepithelial cells is enhanced by mixtures of rbFGF and anti-bFGF sera in non-growing ducts, but there is little change in the staining of growing TEBs. All staining by anti-bFGF sera is abolished with heparin in the reactions. We suggest that the immunoreactive bFGF is present mainly bound to heparan sulfate glycosaminoglycans in the basement membrane of resting structures, but that immunoreactive bFGF becomes associated with proliferating cells, particularly those intermediate in characteristics between epithelial and myoepithelial cells in growing structures such as TEBs.
Volume 41,
Issue 6,
pp. 887-898,
06/01/1993
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G. Wang, A. Platt-Higgins, J. Carroll, S. de Silva Rudland, J. Winstanley, R. Barraclough, and P. S. Rudland Induction of Metastasis by S100P in a Rat Mammary Model and Its Association with Poor Survival of Breast Cancer Patients Cancer Res., January 15, 2006; 66(2): 1199 - 1207. [Abstract] [Full Text] [PDF] |
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H. Rahmoune, H.-L. Chen, J. T. Gallagher, P. S. Rudland, and D. G. Fernig Interaction of Heparan Sulfate from Mammary Cells with Acidic Fibroblast Growth Factor (FGF) and Basic FGF. REGULATION OF THE ACTIVITY OF BASIC FGF BY HIGH AND LOW AFFINITY BINDING SITES IN HEPARAN SULFATE J. Biol. Chem., March 27, 1998; 273(13): 7303 - 7310. [Abstract] [Full Text] [PDF] |
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D. Ledoux, D. Caruelle, J.-C. Sabourin, J. Liu, M. Crepin, D. Barritault, and J. Courty Cellular Distribution of the Angiogenic Factor Heparin Affin Regulatory Peptide (HARP) mRNA and Protein in the Human Mammary Gland J. Histochem. Cytochem., September 1, 1997; 45(9): 1239 - 1246. [Abstract] [Full Text] [PDF] |
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N. Sergeant, M. Lyon, P. S. Rudland, D. G. Fernig, and M. Delehedde Stimulation of DNA Synthesis and Cell Proliferation of Human Mammary Myoepithelial-like Cells by Hepatocyte Growth Factor/Scatter Factor Depends on Heparan Sulfate Proteoglycans and Sustained Phosphorylation of Mitogen-activated Protein Kinases p42/44 J. Biol. Chem., May 26, 2000; 275(22): 17094 - 17099. [Abstract] [Full Text] [PDF] |
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V. Nurcombe, C. E. Smart, H. Chipperfield, S. M. Cool, B. Boilly, and H. Hondermarck The Proliferative and Migratory Activities of Breast Cancer Cells Can Be Differentially Regulated by Heparan Sulfates J. Biol. Chem., September 22, 2000; 275(39): 30009 - 30018. [Abstract] [Full Text] [PDF] |
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