scholarly journals Deletion of the Ron receptor tyrosine kinase domain in mice provides protection from endotoxin-induced acute liver failure

Hepatology ◽  
2002 ◽  
Vol 36 (5) ◽  
pp. 1053-1060 ◽  
Author(s):  
Mike A. Leonis ◽  
Kenya Toney-Earley ◽  
Sandra J. F. Degen ◽  
Susan E. Waltz
Keyword(s):  
Tyrosine Kinase ◽  
Liver Failure ◽  
Acute Liver Failure ◽  
Receptor Tyrosine Kinase ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Ron Receptor

scholarly journals 3′UTRs Regulate Mouse Ntrk2 mRNA Distribution in Cortical Neurons

2020 ◽  
Vol 70 (11) ◽  
pp. 1858-1870
Author(s):  
Shangqin Chen ◽  
Jinjin Zhu ◽  
Peijun Li ◽  
Zhaonan Xia ◽  
Mengjing Tu ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Cortical Neurons ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Mrna Levels ◽  
Tyrosine Kinase 2 ◽  
Mrna Transcripts ◽  
Cultured Cortical Neurons ◽  
Apical Dendrites

Abstract There are two major isoforms of NTRK2 (neurotrophic receptor tyrosine kinase 2, or TrkB), full-length isoform with tyrosine kinase (TK) domain intact (+) and spliced isoform without tyrosine kinase domain (TK(−)). Within each isoform, there exist subtypes with minor modifications of the protein sequences. In human, the NTRK2 mRNA transcripts encoding TK(+) have same 3′UTRs, while the transcripts encoding subtypes of NTRK2 TK(−) have two completely different 3′UTRs. In mouse, the mRNA transcripts encoding same NTRK2 protein sequence for either TK(+) or TK(−) have long or short 3′UTRs, respectively. The physiological functions of these different 3′UTRs are still unknown. Pilocarpine stimulation increased Ntrk2 mRNA levels in soma, while the increase in synaptosome was smaller. FISH results further showed that mouse Ntrk2 transcripts with different 3′UTRs were distributed differently in cultured cortical neurons. The transcripts with long 3′UTR were distributed more in apical dendrites compared with transcripts with short 3′UTR. Our results provide evidence of non-coding 3′UTR function in regulating mRNA distribution in neurons.

scholarly journals Structure of the FGF Receptor Tyrosine Kinase Domain Reveals a Novel Autoinhibitory Mechanism

Cell ◽  
1996 ◽  
Vol 86 (4) ◽  
pp. 577-587 ◽  
Author(s):  
Moosa Mohammadi ◽  
Joseph Schlessinger ◽  
Stevan R Hubbard
Keyword(s):  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Fgf Receptor

Mutations in the Receptor Tyrosine Kinase Pathway Are Associated with Clinical Outcome in Patients with Acute Myeloblastic Leukemia Harboring t(8;21)(q22;q22).

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 3000-3000
Author(s):  
Tomoko Nanri ◽  
Naofumi Matsuno ◽  
Toshiro Kawakita ◽  
Hitoshi Suzushima ◽  
Fumio Kawano ◽  
...  
Keyword(s):  
Clinical Outcome ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Disease Free Survival ◽  
Kinase Domain ◽  
Acute Myeloblastic Leukemia ◽  
Tyrosine Kinase Domain ◽  
Juxtamembrane Domain ◽  
Ras Gene ◽  
Hematopoietic Stem

Abstract AML1-MTG8 generated by t(8;21)(q22;q22) contributes to leukemic transformation but additional events are required for full leukemogenesis. We examined whether mutations in the receptor tyrosine kinase (RTK) pathway could be the genetic events that cause acute myeloblastic leukemia (AML) harboring t(8;21). Mutations in the second tyrosine kinase domain, juxtamembrane domain and exon 8 of the C-KIT gene were observed in 7, 1 and 3 of 37 AML patients with t(8;21), respectively. Three patients showed an internal tandem duplication in the juxtamembrane domain of the FLT3 gene. One patient had a mutation in the K-Ras gene at codon 12. As the occurrence of these mutations was mutually exclusive, a total of 15 (41%) patients showed mutations in the RTK pathway. These results suggest that AML1-MTG8 predisposes cells to the acquisition of activating mutations in the RTK pathway as an additional event leading to the development of AML. Ten of 15 patients with mutations in the RTK pathway relapsed, compared with only 3 of 19 patients lacking such mutations (p=0.0042). Furthermore, the 6-year disease-free survival (DFS) in patients with mutations was 12% compared to 55% in those without mutations (p=0.0344). When patients who underwent allogeneic hematopoietic stem cell transplantation (HSCT) were censored at the date of the HSCT, patients with mutations had a 6-year DFS of 0% versus 60% for the patients without mutations (p=0.0096) These observations indicate that RTK mutations are associated with the clinical outcome in t(8;21) AML.

scholarly journals Antibodies to insulin receptor tyrosine kinase stimulate its activity towards exogenous substrates without inducing receptor autophosphorylation

1989 ◽  
Vol 260 (3) ◽  
pp. 749-756 ◽  
Author(s):  
V Baron ◽  
N Gautier ◽  
N Rochet ◽  
R Ballotti ◽  
B Rossi ◽  
...  
Keyword(s):  
Growth Factor ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Receptor Tyrosine Kinase ◽  
Kinase Activity ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Insulin Receptor Tyrosine Kinase ◽  
Substrate Phosphorylation ◽  
Exogenous Substrates

Anti-peptide antibodies directed against a highly-conserved sequence of the insulin receptor tyrosine kinase domain have been used to study the relationship between this specific region and kinase activation. Antibodies have been prepared by the injection into a rabbit of a synthetic peptide (P2) corresponding to residues 1110-1125 of the proreceptor. The peptide exhibits 88-95% sequence similarity with the corresponding sequence in the v-ros protein and in receptors for epidermal growth factor and for insulin-like growth factor 1. Two antibodies with different specificities could be separated from total antiserum obtained after immunization with P2. One antibody [anti-(P-Tyr)] cross-reacted with phosphotyrosine and immunoprecipitated solely autophosphorylated receptors. This antibody was shown to increase or decrease the receptor tyrosine kinase activity depending on its concentration. In all circumstances receptor autophosphorylation and substrate phosphorylation were modulated in a parallel fashion. The second antibody (anti-P2) failed to immunoprecipitate the insulin receptor, but was found to interact with both the peptide and the receptor by e.l.i.s.a. assay. Using a tyrosine co-polymer we found that anti-P2 activated the insulin receptor kinase leading to substrate phosphorylation at a level similar to that observed with insulin. This effect was additive to the hormonal effect. In contrast, receptor autophosphorylation was not modified by the anti-peptide. The differential effect of this anti-peptide further supports the idea that receptor autophosphorylation and kinase activity towards exogenous substrates might be independently regulated. Finally, our data suggest that conformational changes in the receptor tyrosine kinase domain may be sufficient for activation of its enzymic activity.

Substrate specificity of the insulin receptor tyrosine kinase domain

1993 ◽  
Vol 21 (3) ◽  
pp. 266S-266S
Author(s):  
Noeleen E. Keane ◽  
Barry A. Levine ◽  
Philip Quirk ◽  
Bernard Calas ◽  
Alain Chavanieu ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Receptor Tyrosine Kinase ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Insulin Receptor Tyrosine Kinase

scholarly journals Insulin Resistance Induced by Hyperinsulinemia Coincides with a Persistent Alteration at the Insulin Receptor Tyrosine Kinase Domain

PLoS ONE ◽  
2014 ◽  
Vol 9 (9) ◽  
pp. e108693 ◽  
Author(s):  
Karyn J. Catalano ◽  
Betty A. Maddux ◽  
Jaroslaw Szary ◽  
Jack F. Youngren ◽  
Ira D. Goldfine ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Receptor Tyrosine Kinase ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Insulin Receptor Tyrosine Kinase

Insulin receptor tyrosine kinase domain auto-dephosphorylation

1992 ◽  
Vol 189 (3) ◽  
pp. 1457-1463 ◽  
Author(s):  
Philip A. Gruppuso ◽  
Joan M. Boylan ◽  
Barry A. Levine ◽  
Leland Ellis
Keyword(s):  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Receptor Tyrosine Kinase ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Insulin Receptor Tyrosine Kinase
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