Zobrazeno 1 - 10
of 41
pro vyhledávání: '"B, Ermel"'
Publikováno v:
Diabetes. 40:1440-1448
Hyperglycemia causes insulin-receptor kinase (IRK) resistance in fat cells. We characterized the mechanism of IRK inhibition and studied whether it is the consequence of a glucose-induced stimulation of protein kinase C (PKC). Fat cells were incubate
Publikováno v:
Journal of Biological Chemistry. 265:9340-9345
We have characterized and analyzed IGF-I- and insulin-stimulated cell growth, receptor binding, and autophosphorylation in the human leukemic cell line HL-60. IGF-I-stimulated cell growth occurred at low (5 ng/ml) and insulin stimulated only at high
Autor:
Monika Kellerer, Axel Ullrich, S. Tippmer, B Ermel, B Vogt, B. Obermaier-Kusser, Hans-Ulrich Häring, Reiner Lammers
Publikováno v:
Biochemistry. 31(19)
Human insulin receptor isoforms (HIR-A and -B) differ in their alpha-subunit structures which result from alternatively spliced precursor mRNAs. This structural difference causes distinct binding affinities for insulin. To determine the impact of the
Publikováno v:
The Journal of biological chemistry. 265(16)
We have characterized and analyzed IGF-I- and insulin-stimulated cell growth, receptor binding, and autophosphorylation in the human leukemic cell line HL-60. IGF-I-stimulated cell growth occurred at low (5 ng/ml) and insulin stimulated only at high
Publikováno v:
The Biochemical journal. 266(3)
The mechanism of insulin signalling is not yet understood in detail. Recently, a role for inositol phosphate (IP)-oligosaccharides as second messengers transmitting the insulin signal at the post-kinase level was proposed. To evaluate this hypothesis
Publikováno v:
Biochemical Journal. 234:59-66
Catecholamine treatment of isolated rat adipocytes decreases insulin binding and inhibits insulin stimulation of the glucose-transport system. There is increasing evidence that the insulin signal is transmitted after insulin is bound to the receptor
Autor:
B Ermel, B. Obermaier-Kusser, Zenghua Su, Hans-Ulrich Häring, Morris F. White, D. E. Pongratz, C Mühlbacher
Publikováno v:
Journal of Biological Chemistry. 264:9497-9504
The insulin receptor purified from skeletal muscle of patients with non-insulin-dependent diabetes mellitus (NIDDM) displayed a 25-55% reduction in insulin-stimulated autophosphorylation and tyrosyl-specific phosphotransferase activity relative to co
Publikováno v:
Proceedings of the National Academy of Sciences. 84:113-117
It is speculated that the transmission of an insulin signal across the plasma membrane of cells occurs through activation of the tyrosine-specific receptor kinase, autophosphorylation of the receptor, and subsequent phosphorylation of unidentified su
Autor:
Fausto Machicao, B Ermel, HU Häring, E. Biemer, E Rattenhuber, J. Mushack, D. Kirsch, B. Obermaier
Publikováno v:
Diabetologia. 30:93-99
The effect of the catecholamine isoprenaline (10(-5) mol/l) and of the tumour promoting phorbolester tetradecanoyl-beta-phorbol acetate (10(-9) mol/l) on insulin stimulated 3-O-methyl-glucose transport was studied in freshly isolated human adipocytes
Publikováno v:
FEBS Letters. (1):85-88
Receptor-associated protein kinase activity has been shown in all primary target tissues of insulin action in the rat and a function of insulin receptor phosphorylation in signal transmission was proposed. Insulin receptor phosphorylation so far has