Zobrazeno 1 - 10
of 102
pro vyhledávání: '"J, Kusari"'
Publikováno v:
Biochemical and Biophysical Research Communications. 217:304-312
Brain tissue mRNA was amplified using polymerase chain reaction (PCR) with eight overlapping sets of primers that span the cDNA coding sequence for the human placental insulin receptor. Only the A isoform (lacking exon 11) of the receptor was detecte
Publikováno v:
Journal of Biological Chemistry. 268:25455-25462
In this study, we have examined the effects of insulin and insulin-like growth factor (IGF)-I on protein tyrosine phosphatase (PTPase) activity in rat L6 skeletal muscle cells. Under basal conditions, about 85% of total cellular PTPase activity was a
Publikováno v:
Proceedings of the National Academy of Sciences. 90:4379-4383
To assess the function of the cytoplasmic domain of the insulin receptor (IR) beta subunit, we have studied a mutant IR truncated by 365 aa (HIR delta 978), thereby deleting > 90% of the cytoplasmic domain. HIR delta 978 receptors were processed norm
Autor:
T Sasaoka, Leonard Jarett, Y Takata, J Kusari, Neelima Shah, Jerrold M. Olefsky, Robert M. Smith
Publikováno v:
Endocrinology. 132:1453-1462
A previous study of tyrosine kinase-defective insulin receptors demonstrated that receptor autophosphorylation or tyrosine kinase activity was required for concentrating insulin receptors in coated pits, but not for their migration or aggregation on
Publikováno v:
Journal of Clinical Investigation. 88:1323-1330
Insulin resistance is a common feature of non-insulin-dependent diabetes mellitus (NIDDM) and "diabetes susceptibility genes" may be involved in this abnormality. Two potential candidate genes are the insulin receptor (IR) and the insulin-sensitive g
Publikováno v:
Molecular and cellular biochemistry. 221(1-2)
We have previously reported a direct in vivo interaction between the activated insulin receptor and protein-tyrosine phosphatase-1B (PTP1B), which leads to an increase in PTP1B tyrosine phosphorylation. In order to determine if PTP1B is a substrate f
Publikováno v:
Molecular and cellular biochemistry. 218(1-2)
Previously, we have reported that insulin induces the expression of the dual-specificity tyrosine phosphatase Mitogen-activated protein (MAP) kinase phosphatase-1 (MKP-1) and that this may represent a negative feedback mechanism to regulate insulin-s
Publikováno v:
Molecular and cellular biochemistry. 211(1-2)
Cells expressing mutant insulin receptors (Y/F2), in which tyrosines 1316 and 1322 have been replaced with phenylalanine, exhibit enhanced insulin-induced MAP kinase activity and DNA synthesis in comparison with cells expressing wild type insulin rec
Publikováno v:
Molecular and cellular biochemistry. 182(1-2)
Insulin signaling involves a dynamic cascade of protein tyrosine phosphorylation and dephosphorylation. Most of our understanding of this process comes from studies focusing on tyrosine kinases, which are signal activators. Our knowledge of the role
Publikováno v:
The Journal of clinical investigation. 93(3)
Particulate and cytosolic protein tyrosine phosphatase (PTPase) activity was measured in skeletal muscle from 15 insulin-sensitive subjects and 5 insulin-resistant nondiabetic subjects, as well as 18 subjects with non-insulin-dependent diabetes melli