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Horm Metab Res 1987; 19(6): 242-248
DOI: 10.1055/s-2007-1011790
ORIGINALS

© Georg Thieme Verlag, Stuttgart · New York

Growth Hormone Receptor Structure in Adipocytes from Normal and Growth Hormone-Deficient Rats

Jessica Schwartz1 , Christin Carter-Su2
  • Department of Physiology, University of Michigan Medical School, Ann Arbor, Michigan, U.S.A.
1>To whom all correspondence and requests for reprints should besent. 2Recipient of a Career Development Award from the Juvenile Diabetes Foundation.
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Publication History

1986

1986

Publication Date:
14 March 2008 (online)

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Summary

Using cross-linking techniques, we compared the properties of the growth hormone (GH) receptor in freshly isolated adipocytes from normal rats, from GH deficient rats, and in preincubated adipocytes from normal rats. Bound [125l]iodo-hGH was cross-linked to adipocytes with disuccinimidyl suberate, and membrane proteins labelled with [125l]iodo-hGH were visualized using sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography. All of the adipocytes tested exhibited a prominent Mr = 134,000 band and additional less intense bands in the presence of reductant. No significant differences in the overall banding pattern of membrane proteins were evident in reducing or nonreducing gels, using adipocytes from rats made GH deficient by hypophysectomy or by treatment with antibodies against rat GH, or in fresh and preincubated cells from normal rats. Taken together with binding studies, these findings suggest that differences in the ability of GH to stimulate glucose oxidation in rat adipose tissue probably involve differences distal to the GH receptor.

Key-Words

Growth Hormone - Growth Hormone Deficiency - Growth Hormone Receptor - Adipocyte - Cross-Linking - Glucose Oxidation

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