TY - JOUR
T1 - Growth hormone binding proteins in pig adipose tissue
T2 - Number, size and effects of pGH treatment on pGH and bGH binding
AU - Sørensen, M. T.
AU - Chaudhuri, S.
AU - Louveau, I.
AU - Coleman, M. E.
AU - Etherton, T. D.
N1 - Funding Information:
This work was supported in part by USDA Grant 88-37266-3985 (to T.D.E.). Address reprint requests to T.D. Etherton, 301 W.L. Henning Bldg., Penn State University, University Park, PA 16802. ~Visiting scientist on leave from The National Institute of Animal Science, Foulum, DK-8830 Tjele, Denmark. 2Present address: Department of Biology, Case Western Reserve University, Cleveland, OH. 3Visiting scientist on leave from the Institut National de la Recherche Agronomique, Station de Recherches Porcines, Saint Gilles, 35590 L'Hermitage, France.
PY - 1992/1
Y1 - 1992/1
N2 - The present study was undertaken to determine the number and size of growth hormone binding proteins present in pig adipose tissue, determine if there were differences in binding of pGH and bGH to adipose tissue membranes and establish the effects of pGH treatment on GH binding. Administration of pGH (0, 25, 50 or 100 μg pGH/kg BW/d) for 7 d did not affect binding of [125I]bGH to adipose tissue microsomes. Maximum binding of bGH was approximately 8-fold higher than that observed for pGH. Half-maximal inhibition of [125I]bGH binding was observed at 11 ng/ml of bGH. In contrast, a more than 10-fold greater concentration of pGH was required to half-maximally inhibit [125I]pGH binding. bGH and pGH both bound to the same GH binding proteins (Mr of 92,000, 73,000 and 53,000). The GH binding proteins appear to be produced by post-translational modification of a single GH receptor transcript rather than alternative splicing of a primary transcript since only one GH receptor mRNA transcript (4.2 kb) was detected on Northern analysis. Our findings indicate that: 1) bGH is the preferred ligand to use to study GH binding in pig adipose tissue membranes (or adipocytes); 2) exogenous pGH does not alter GH binding; and 3) only one GH receptor mRNA transcript is present in pig adipose tissue.
AB - The present study was undertaken to determine the number and size of growth hormone binding proteins present in pig adipose tissue, determine if there were differences in binding of pGH and bGH to adipose tissue membranes and establish the effects of pGH treatment on GH binding. Administration of pGH (0, 25, 50 or 100 μg pGH/kg BW/d) for 7 d did not affect binding of [125I]bGH to adipose tissue microsomes. Maximum binding of bGH was approximately 8-fold higher than that observed for pGH. Half-maximal inhibition of [125I]bGH binding was observed at 11 ng/ml of bGH. In contrast, a more than 10-fold greater concentration of pGH was required to half-maximally inhibit [125I]pGH binding. bGH and pGH both bound to the same GH binding proteins (Mr of 92,000, 73,000 and 53,000). The GH binding proteins appear to be produced by post-translational modification of a single GH receptor transcript rather than alternative splicing of a primary transcript since only one GH receptor mRNA transcript (4.2 kb) was detected on Northern analysis. Our findings indicate that: 1) bGH is the preferred ligand to use to study GH binding in pig adipose tissue membranes (or adipocytes); 2) exogenous pGH does not alter GH binding; and 3) only one GH receptor mRNA transcript is present in pig adipose tissue.
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U2 - 10.1016/0739-7240(92)90005-I
DO - 10.1016/0739-7240(92)90005-I
M3 - Article
C2 - 1582195
AN - SCOPUS:0342277395
SN - 0739-7240
VL - 9
SP - 13
EP - 24
JO - Domestic Animal Endocrinology
JF - Domestic Animal Endocrinology
IS - 1
ER -