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Effect of N-terminal modified analogs of growth hormone on collagen synthesis in avian skin fibroblasts
Year:
1993
Authors :
Granot, Irit
;
.
Hurvitz, Shmuel (Animal science)
;
.
Pines, Mark
;
.
Volume :
92
Co-Authors:
Granot, I., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, 50250, Israel
Halevy, O., Department of Animal Science, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Tchelet, A., Department of Biochemistry, Food Science and Nutrition, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Sakal, E., Department of Biochemistry, Food Science and Nutrition, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Gertler, A., Department of Biochemistry, Food Science and Nutrition, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Vogel, T., Biotechnology General Ltd., Rehovot, 76324, Israel
Hurwitz, S., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, 50250, Israel
Pines, M., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, 50250, Israel
Facilitators :
From page:
241
To page:
246
(
Total pages:
6
)
Abstract:
Human growth hormone (hGH) inhibits α1(I) collagen gene expression in cultured avian skin fibroblasts resulting in a decrease in the amount of collagenase-digestible proteins (CDP) in the medium. In addition, a synergism exists between GH and insulin-like growth factor-I (IGF-I) in their effect on CDP. Four N-terminal modified hGH analogs were tested for their ability to affect collagen metabolism in these cells. The truncated analog Des-7 hGH(R8M, D11A) was found to be a strong antagonist of the hGH-induced inhibition of the collagen synthesis but by itself did not inhibit collagen α1(I) gene expression or modify the CDP appearance in the medium. Some synergism between Des-7 hGH and IGF-I was observed. The analog Met-hGH(R19H, L20P), in which Arg19 was replaced by histidine, and Leu20 by proline was only partially potent compared with the native hormone in causing inhibition of collagen gene expression, in attenuating CDP appearance in the medium, and in antagonizing hGH. However, this analog was as potent as hGH in its ability to synergize with IGF-I. The importance of His18 was assessed by testing the response to Met-hGH(H18D), in which His18 was replaced by Asp, and to Met-hGH(H18Q), in which His18 was replaced by glutamine (as in chicken GH sequence). Substitution of His18 by a negatively charged amino acid abolished all the hormone activities tested whereas substitution with glutamine restored only part of the activity. These results demonstrate the importance of the N-terminal sequence of the GH molecule and suggest that various effects of GH are transduced through diverse pathways, each produced by structurally different sites in the hormone molecule. © 1993.
Note:
Related Files :
Animal
animal cell
gene expression
Insulin-Like Growth Factor I
protein synthesis inhibition
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Related Content
More details
DOI :
10.1016/0303-7207(93)90014-B
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
21722
Last updated date:
21/08/2022 07:45
Creation date:
16/04/2018 23:46
You may also be interested in
Scientific Publication
Effect of N-terminal modified analogs of growth hormone on collagen synthesis in avian skin fibroblasts
92
Granot, I., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, 50250, Israel
Halevy, O., Department of Animal Science, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Tchelet, A., Department of Biochemistry, Food Science and Nutrition, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Sakal, E., Department of Biochemistry, Food Science and Nutrition, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Gertler, A., Department of Biochemistry, Food Science and Nutrition, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Vogel, T., Biotechnology General Ltd., Rehovot, 76324, Israel
Hurwitz, S., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, 50250, Israel
Pines, M., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, 50250, Israel
Effect of N-terminal modified analogs of growth hormone on collagen synthesis in avian skin fibroblasts
Human growth hormone (hGH) inhibits α1(I) collagen gene expression in cultured avian skin fibroblasts resulting in a decrease in the amount of collagenase-digestible proteins (CDP) in the medium. In addition, a synergism exists between GH and insulin-like growth factor-I (IGF-I) in their effect on CDP. Four N-terminal modified hGH analogs were tested for their ability to affect collagen metabolism in these cells. The truncated analog Des-7 hGH(R8M, D11A) was found to be a strong antagonist of the hGH-induced inhibition of the collagen synthesis but by itself did not inhibit collagen α1(I) gene expression or modify the CDP appearance in the medium. Some synergism between Des-7 hGH and IGF-I was observed. The analog Met-hGH(R19H, L20P), in which Arg19 was replaced by histidine, and Leu20 by proline was only partially potent compared with the native hormone in causing inhibition of collagen gene expression, in attenuating CDP appearance in the medium, and in antagonizing hGH. However, this analog was as potent as hGH in its ability to synergize with IGF-I. The importance of His18 was assessed by testing the response to Met-hGH(H18D), in which His18 was replaced by Asp, and to Met-hGH(H18Q), in which His18 was replaced by glutamine (as in chicken GH sequence). Substitution of His18 by a negatively charged amino acid abolished all the hormone activities tested whereas substitution with glutamine restored only part of the activity. These results demonstrate the importance of the N-terminal sequence of the GH molecule and suggest that various effects of GH are transduced through diverse pathways, each produced by structurally different sites in the hormone molecule. © 1993.
Scientific Publication
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