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Department of Physiology, University of Massachusetts Medical School (H.M.G., L.-R.TJ Worcester, Massachusetts 01655
the Howard Hughes Medical Institute, Departments of Human Genetics (J.R., N.E.C., S.A.L.) and Medicine (N.E.C., S.A.L.), University of Pennsylvania Philadelphia, Pennsylvania 19104-6145
Address requests for reprints to: Dr. H. Maurice Goodman, Department of Physiology, University of Massachusetts School of Medicine, 55 Lake Avenue North, Worcester, Massachusetts 01605.
Abstract
Genes for normal human pituitary GH (hGHN) and the GH variant (hGH-V) were expressed in stably transfected mouse mammary cells. The biological properties of hGH-N and hGH-V secreted into the medium were examined using Tat adipocytes or epididymal fat segments. MethionylhGH produced in E. coli served as a reference standard. The three preparations were quite similar in their ability to bind specifically to intact fat cells and were virtually indistinguishable in their ability to increase glucose oxidation (an insulin-like response), induce refractoriness to insulin-like stimulation, and induce lipolysis in the presence of glucocorticoid. We conclude that placentally expressed hGH-V has a spectrum of metabolic activity comparable to pituitary hGH-N and may contribute to regulation of carbohydrate and lipid metabolism during pregnancy. (Endocrinology 129: 1779–1783, 1991)
Footnotes
* This work was supported by NIH Grant DDK-19392 (to H.M.G.), NIH Grant HD-25147 (to N.E.C. and S.A.L.), and March of Dimes Grant 1-1015 (to N.E.C.).
Associate Investigator of the Howard Hughes Medical Institute.
Received January 4, 1991.
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