חיפוש מתקדם
Endocrinology
Gertler, A., Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel, The Department of Physiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB, R3E 0W3, Canada
Shamay, A., Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Cohen, N., Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Ashkenazi, A., Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Friesen, H.G., The Department of Physiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB, R3E 0W3, Canada
Levanon, A., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Gorecki, M., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Aviv, H., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Hadary, D., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Vogel, T., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
A recombinant analog of human GH (hGH) lacking 13 amino acids at the amino-terminus (Met14hGH) inhibited the hGH- or ovine PRL (oPRL)-stimulated proliferation of Nb2 lymphoma cells and bovine PRL-stimulated fat synthesis and a-lactalbumin secretion in explants from bovine lactating mammary gland. The inhibition was competitive in nature, and in Nb2 cells could be abolished by an excess of hGH or oPRL. Inhibition of oPRL-stimulated proliferation of Nb2 cells by Met14hGH could also be specifically abolished by anti-hGH monoclonal antibodies. Met14hGH had no growth-stimulating activity in Nb2 cells and was not cytotoxic. It also did not affect glucose uptake by the mammary gland explants. Met14hGH competed with [125I]hGH for binding to intact Nb2 cells, IM-9 lymphocytes, solubilized microsomal fraction from lactating bovine mammary gland, and microsomal fraction from the liver of female virgin rats, but its affinity for those receptors was 2 orders of magnitude lower than the affinity of hGH. Since Met14hGH used in most experiments contained about 25% impurities and degradation products, a small amount of it was further purified by immunoaffinity chromatography. Two purified fractions, one consisting of a single 20K protein and the other accompanied by a small amount of 25K protein, were obtained. Both fractions exhibited increased inhibition of hGH-or oPRL-stimulated proliferation of Nb2 cells, thus indicating that the inhibitory activity results from the intact Met14hGH molecule. To the best of our knowledge, this is the first report describing the inhibition of lactogenic hormone activities by a modified hGH. © 1986 by The Endocrine Society.
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
אודות
תנאי שימוש
Inhibition of lactogenic activities of ovine prolactin and human growth hormone (hGH) by a novel form of a modified recombinant hGH
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Gertler, A., Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel, The Department of Physiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB, R3E 0W3, Canada
Shamay, A., Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Cohen, N., Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Ashkenazi, A., Department of Agricultural Biochemistry, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, 76100, Israel
Friesen, H.G., The Department of Physiology, Faculty of Medicine, University of Manitoba, Winnipeg, MB, R3E 0W3, Canada
Levanon, A., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Gorecki, M., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Aviv, H., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Hadary, D., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Vogel, T., Bio-technology General (Israel) Ltd., Rehovot, 76326, Israel
Inhibition of lactogenic activities of ovine prolactin and human growth hormone (hGH) by a novel form of a modified recombinant hGH
A recombinant analog of human GH (hGH) lacking 13 amino acids at the amino-terminus (Met14hGH) inhibited the hGH- or ovine PRL (oPRL)-stimulated proliferation of Nb2 lymphoma cells and bovine PRL-stimulated fat synthesis and a-lactalbumin secretion in explants from bovine lactating mammary gland. The inhibition was competitive in nature, and in Nb2 cells could be abolished by an excess of hGH or oPRL. Inhibition of oPRL-stimulated proliferation of Nb2 cells by Met14hGH could also be specifically abolished by anti-hGH monoclonal antibodies. Met14hGH had no growth-stimulating activity in Nb2 cells and was not cytotoxic. It also did not affect glucose uptake by the mammary gland explants. Met14hGH competed with [125I]hGH for binding to intact Nb2 cells, IM-9 lymphocytes, solubilized microsomal fraction from lactating bovine mammary gland, and microsomal fraction from the liver of female virgin rats, but its affinity for those receptors was 2 orders of magnitude lower than the affinity of hGH. Since Met14hGH used in most experiments contained about 25% impurities and degradation products, a small amount of it was further purified by immunoaffinity chromatography. Two purified fractions, one consisting of a single 20K protein and the other accompanied by a small amount of 25K protein, were obtained. Both fractions exhibited increased inhibition of hGH-or oPRL-stimulated proliferation of Nb2 cells, thus indicating that the inhibitory activity results from the intact Met14hGH molecule. To the best of our knowledge, this is the first report describing the inhibition of lactogenic hormone activities by a modified hGH. © 1986 by The Endocrine Society.
Scientific Publication
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