The Differential Effects of pp120 (Ceacam 1) on the Mitogenic Action of Insulin and Insulin-Like Growth Factor 1 Are Regulated by the Nonconserved Tyrosine 1316 in the Insulin Receptor [PDF]
Molecular and Cellular Biology, 2000 pp120 (Ceacam 1) undergoes ligand-stimulated phosphorylation by the insulin receptor, but not by the insulin-like growth factor 1 receptor (IGF-1R). This differential phosphorylation is regulated by the C terminus of the beta-subunit of the insulin receptor, the least conserved domain of the two receptors.
Matthew N Poy, Sonia M Najjar
exaly +4 more sources
Pro-Tumorigenic Phosphorylation of p120 Catenin in Renal and Breast Cancer. [PDF]
PLoS ONE, 2015 Altered protein expression and phosphorylation are common events during malignant transformation. These perturbations have been widely explored in the context of E-cadherin cell-cell adhesion complexes, which are central in the maintenance of the normal ...
Antonis Kourtidis +4 more
doaj +2 more sources
Insulin Stimulates pp120 Endocytosis in Cells Co-Expressing Insulin Receptors [PDF]
Journal of Biological Chemistry, 1998 pp120, a substrate of the insulin receptor tyrosine kinase, is a plasma membrane glycoprotein that is expressed in the hepatocyte as two spliced isoforms differing by the presence (full-length) or absence (truncated) of most of the intracellular domain including all phosphorylation sites.
Mark J Howard +2 more
exaly +3 more sources
Effect of pp120 on Receptor-Mediated Insulin Endocytosis Is Regulated by the Juxtamembrane Domain of the Insulin Receptor [PDF]
Journal of Biological Chemistry, 1998 pp120, a substrate of the insulin receptor tyrosine kinase, does not undergo ligand-stimulated phosphorylation by the insulin-like growth factor-1 (IGF-1) receptor. However, replacement of the C-terminal domain of the IGF-1 receptor beta-subunit with the corresponding segment of the insulin receptor restored pp120 phosphorylation by the chimeric ...
Matthew N Poy, Sonia M Najjar
exaly +3 more sources
PP120 Fluorescent In Situ Hybridization (FISH) Vs Conventional Cytogenetic (CC) For Detecting High-Risk Genetic Mutations In Multiple Myeloma [PDF]
International Journal of Technology Assessment in Health Care, 2022 IntroductionThe Revised International Staging System (R-ISS) International Myeloma Working Group (IMWG) recommends a minimal panel to detect high-risk cytogenetics (del17p, t[4;14], t[14;16]) for patients with multiple myeloma (MM). In the Brazilian Public Health System, the use of FISH is currently authorized for rare diseases only, not including MM ...
Denis Satoshi Komoda +5 more
openaire +2 more sources
The Cytoplasmic Tyrosine Kinase FER Is Associated With the Catenin-Like Substrate pp120 and Is Activated by Growth Factors [PDF]
Molecular and Cellular Biology, 1995 The FER gene encodes a cytoplasmic tyrosine kinase with a single SH2 domain and an extensive amino terminus. In order to understand the cellular function of the FER kinase, we analyzed the effect of growth factor stimulation on the phosphorylation and activity of FER.
T W Wong, L Kim
exaly +3 more sources
Identification of pp120, an Endogenous Substrate for the Hepatocyte Insulin Receptor Tyrosine Kinase, as an Integral Membrane Glycoprotein of the Bile Canalicular Domain. [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 1988 An endogenous membrane-bound substrate of the insulin receptor beta-subunit tyrosine kinase in liver, pp120, has been identified as HA4, a 110-kDa membrane glycoprotein localized primarily to the bile canalicular domain of the hepatocyte. HA4 has been implicated in bile salt transport and cell adhesion.
Simeon I Taylor +2 more
exaly +3 more sources
Cloning and Characterization of a Functional Promoter of the Rat pp120 Gene, Encoding a Substrate of the Insulin Receptor Tyrosine Kinase [PDF]
Journal of Biological Chemistry, 1996 Cloning of the 5 -flanking region of the rat pp120 gene has indicated that it is a housekeeping gene: it lacks a functional TATA box and contains several Sp1 binding sites and multiple transcription initiation sites at nucleotides -101, -71, -41, and -27 spread over a GC-rich area.
Yumi Imai +2 more
exaly +3 more sources
Biochemistry, 1995 Insulin binding to the alpha-subunit of its receptor stimulates the receptor tyrosine kinase to phosphorylate the beta-subunit and several endogenous protein substrates, including pp120/HA4, a liver-specific plasma membrane glycoprotein of M(r) 20,000.
Pietro Formisano +2 more
exaly +6 more sources
Insulin Stimulates Phosphorylation of a 120-kDa Glycoprotein Substrate (pp120) for the Receptor-Associated Protein Kinase in Intact H-35 Hepatoma Cells. [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 1987 The insulin receptor possesses protein kinase activity, which may play a role in mediating insulin action. Recently, we have identified a glycoprotein (pp120) in rat liver plasma membranes that is phosphorylated by the solubilized insulin receptor in a cell-free system. We now report that insulin stimulates phosphorylation of pp120 in intact H-35 cells.
Simeon I Taylor +2 more
exaly +3 more sources