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Basic fibroblast growth factor (bFGF) was quantitated in human primary thyrocyte cultures and thyroid cell lines produced by transfection with pSV3_neo. Immunoreactive-bFGF (ir-bFGF) bound to heparin–Sepharose affinity columns eluted with 1·8–2·0 mol NaCl/l and had a molecular weight of approximately 17 000. Recombinant human bFGF in the presence of 5% serum increased the growth of transfected human thyrocytes but not the growth of primary human thyrocytes. Preincubation of cells with up to 100 µg bFGF/l potentiated TSH-stimulated cAMP release from the transfected cells but inhibited release from primary human thyroid cultures. bFGF may be an important modulator of thyroid cell function and growth.

Journal of Endocrinology (1993) 136, 339–344

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