Relevant bibliographies by topics / Insulin receptor tyrosine

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Insulin receptor tyrosine'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Insulin receptor tyrosine.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Insulin receptor tyrosine"

1

King, M. J., and G. J. Sale. "Dephosphorylation of insulin-receptor autophosphorylation sites by particulate and soluble phosphotyrosyl-protein phosphatases." Biochemical Journal 266, no. 1 (February 15, 1990): 251–59. http://dx.doi.org/10.1042/bj2660251.

Full text
Abstract:
Insulin stimulates autophosphorylation of the insulin receptor on multiple tyrosines in three domains: tyrosines 1316 and 1322 in the C-terminal tail, 1146, 1150 and 1151 in the tyrosine-1150 domain, and possibly 953, 960 or 972 in the juxtamembrane domain. In the present work the sequence of dephosphorylation of the various autophosphorylation sites by particulate and cytosolic preparations of phosphotyrosyl-protein phosphatase from rat liver was studied with autophosphorylated human placental insulin receptor as substrate. Both phosphatase preparations elicited a broadly similar pattern of dephosphorylation. The tyrosine-1150 domain in triphosphorylated form was found to be exquisitely sensitive to dephosphorylation, and was dephosphorylated 3-10-fold faster than the di- and monophosphorylated forms of the tyrosine-1150 domain or phosphorylation sites in other domains. The major route for dephosphorylation of the triphosphorylated tyrosine-1150 domain involved dephosphorylation of one of the phosphotyrosyl pair, 1150/1151, followed by phosphotyrosyl 1146 to generate a species monophosphorylated mainly (greater than 80%) at tyrosine 1150 or 1151. Insulin receptors monophosphorylated in the tyrosine-1150 domain disappeared slowly, and overall the other domains were completely dephosphorylated faster than the tyrosine-1150 domain. Dephosphorylation of the diphosphorylated C-terminal domain yielded insulin receptor in which the domain was singly phosphorylated at tyrosine 1322. Triphosphorylation of the insulin receptor in the tyrosine-1150 domain appears important in activating the receptor tyrosine kinase to phosphorylate other proteins. The extreme sensitivity of the triphosphorylated form of the tyrosine-1150 domain to dephosphorylation may thus be important in terminating or regulating insulin-receptor tyrosine kinase action and insulin signalling.
APA, Harvard, Vancouver, ISO, and other styles
2

Blake, A. D., N. S. Hayes, E. E. Slater, and C. D. Strader. "Insulin receptor desensitization correlates with attenuation of tyrosine kinase activity, but not of receptor endocytosis." Biochemical Journal 245, no. 2 (July 15, 1987): 357–64. http://dx.doi.org/10.1042/bj2450357.

Full text
Abstract:
A model of insulin-receptor down-regulation and desensitization has been developed and described. In this model, both insulin-receptor down-regulation and functional desensitization are induced in the human HepG2 cell line by a 16 h exposure of the cells to 0.1 microM-insulin. Insulin-receptor affinity is unchanged, but receptor number is decreased by 50%, as determined both by 125I-insulin binding and by protein immunoblotting with an antibody to the beta-subunit of the receptor. This down-regulation is accompanied by a disproportionate loss of insulin-stimulated glycogen synthesis, yielding a population of cell-surface insulin receptors which bind insulin normally but which are unable to mediate insulin-stimulated glycogen synthesis within the cell. Upon binding of insulin, the desensitized receptors are internalized rapidly, with characteristics indistinguishable from those of control cells. In contrast, this desensitization is accompanied by a loss of the insulin-sensitive tyrosine kinase activity of insulin receptors isolated from these cells. Receptors isolated from control cells show a 5-25-fold enhancement of autophosphorylation of the beta-subunit by insulin; this insulin-responsive autophosphorylation is severely attenuated after desensitization to a maximum of 0-2-fold stimulation by insulin. Likewise, the receptor-mediated phosphorylation of exogenous angiotensin II, which is stimulated 2-10-fold by insulin in receptors from control cells, is completely unresponsive to insulin in desensitized cells. These data provide evidence that the insulin-receptor tyrosine kinase activity correlates with insulin stimulation of an intracellular metabolic event. The data suggest that receptor endocytosis is not sufficient to mediate insulin's effects, and thereby argue for a role of the receptor tyrosine kinase activity in the mediation of insulin action.
APA, Harvard, Vancouver, ISO, and other styles
3

Backer, J. M., S. E. Shoelson, M. A. Weiss, Q. X. Hua, R. B. Cheatham, E. Haring, D. C. Cahill, and M. F. White. "The insulin receptor juxtamembrane region contains two independent tyrosine/beta-turn internalization signals." Journal of Cell Biology 118, no. 4 (August 15, 1992): 831–39. http://dx.doi.org/10.1083/jcb.118.4.831.

Full text
Abstract:
We have investigated the role of tyrosine residues in the insulin receptor cytoplasmic juxtamembrane region (Tyr953 and Tyr960) during endocytosis. Analysis of the secondary structure of the juxtamembrane region by the Chou-Fasman algorithms predicts that both the sequences GPLY953 and NPEY960 form tyrosine-containing beta-turns. Similarly, analysis of model peptides by 1-D and 2-D NMR show that these sequences form beta-turns in solution, whereas replacement of the tyrosine residues with alanine destabilizes the beta-turn. CHO cell lines were prepared expressing mutant receptors in which each tyrosine was mutated to phenylalanine or alanine, and an additional mutant contained alanine at both positions. These mutations had no effect on insulin binding or receptor autophosphorylation. Replacements with phenylalanine had no effect on the rate of [125I]insulin endocytosis, whereas single substitutions with alanine reduced [125I]insulin endocytosis by 40-50%. Replacement of both tyrosines with alanine reduced internalization by 70%. These data suggest that the insulin receptor contains two tyrosine/beta-turns which contribute independently and additively to insulin-stimulated endocytosis.
APA, Harvard, Vancouver, ISO, and other styles
4

Issad, T., J. M. Tavaré, and R. M. Denton. "Analysis of insulin receptor phosphorylation sites in intact rat liver cells by two-dimensional phosphopeptide mapping. Predominance of the tris-phosphorylated form of the kinase domain after stimulation by insulin." Biochemical Journal 275, no. 1 (April 1, 1991): 15–21. http://dx.doi.org/10.1042/bj2750015.

Full text
Abstract:
1. Insulin receptors were partially purified from rat liver by chromatography on wheat-germ-lectin-Sepharose. Incubation with [gamma-32P]ATP in the presence of insulin resulted in increased phosphorylation of the beta-subunit on both tyrosine and serine residues. Two-dimensional mapping of tryptic peptides showed that, in agreement with previous studies using preparations of receptors from other sources, the tyrosine residues involved were the three tyrosines in the kinase domain (corresponding to tyrosines 1158, 1162 and 1163 of the human receptor) plus two tyrosines close to the C-terminus (corresponding to tyrosines 1328 and 1334). 2. The effects of insulin on the phosphorylation of receptors within intact rat liver cells were determined by incubating cells in the presence of [32P]Pi for 50 min and then with or without insulin for a further 10 min. The labelled receptors were then rapidly isolated by sequential use of wheat-germ-lectin-Sepharose chromatography and immuno-isolation using a monoclonal antibody to the C-terminal end of the beta-subunit. 3. Insulin was found to increase overall phosphorylation of the receptor nearly 3-fold. Two-dimensional mapping was then carried out in combination with phosphoamino acid analysis. This revealed that the pattern of phosphorylation of the receptors in cells incubated in the absence and presence of insulin exhibited a number of marked differences from that observed in previous studies on intact cells, which had been restricted to cells expressing very high levels of insulin receptors such as certain hepatoma-derived cells or cells transfected with insulin receptor cDNA. The differences in the effects of insulin included a larger increase in the proportion of receptors being phosphorylated on the three tyrosine residues of the kinase domain, no apparent phosphorylation of the two tyrosine residues close to the C-terminus and no increase in either threonine or overall serine phosphorylation. 4. The receptors appeared to be phosphorylated on a number of different serine residues in cells incubated in the absence of insulin. Evidence for both increases and decreases in the phosphorylation of specific serine residues on addition of insulin was obtained. 5. It is concluded that care should be taken when extrapolating findings on the phosphorylation of the insulin receptor within cultured cells to more physiological situations.
APA, Harvard, Vancouver, ISO, and other styles
5

Heffetz, D., W. J. Rutter, and Y. Zick. "The insulinomimetic agents H2O2 and vanadate stimulate tyrosine phosphorylation of potential target proteins for the insulin receptor kinase in intact cells." Biochemical Journal 288, no. 2 (December 1, 1992): 631–35. http://dx.doi.org/10.1042/bj2880631.

Full text
Abstract:
H2O2 and vanadate are known insulinomimetic agents. Together they induce insulin's bioeffects with a potency which exceeds that seen with insulin, vanadate or H2O2 alone. We have previously shown that a combination of H2O2 and vanadate, when added to intact cells, rapidly stimulates protein tyrosine phosphorylation, owing to the inhibitory effects of these agents on intracellular protein tyrosine phosphatases (PTPases). Employing Western blotting with anti-phosphotyrosine antibodies, we have now identified in Chinese-hamster ovary (CHO) cells transfected with a wild-type insulin-receptor gene (CHO.T cells) several proteins (e.g. pp180, 125, 100, 60 and 52) whose phosphotyrosine content is rapidly increased upon treatment of the cells with a combination of insulin and 3 mM-H2O2. Tyrosine phosphorylation of these and additional proteins was further potentiated when 100 microM-sodium orthovanadate was added together with H2O2. The effects of insulin, insulin/H2O2, and H2O2/vanadate on tyrosine phosphorylation were markedly decreased in CHO cells transfected with an insulin-receptor gene where the twin tyrosines 1162 and 1163 were replaced with phenylalanine (CHO.YF-3 cells). Similarly, most of these proteins failed to undergo enhanced tyrosine phosphorylation in parental CHO cells incubated in the presence of insulin or the insulinomimetic agents. Our findings suggest that inhibition of PTPase activity by H2O2/vanadate augments the autophosphorylation of tyrosines 1162 and 1163 of the insulin receptor kinase, leading to its activation in an insulin-independent manner. As a result, tyrosine phosphorylation of potential targets for this enzyme takes place. Failure of H2O2/vanadate to induce phosphorylation of these proteins in receptor mutants lacking these twin tyrosine residues supports this hypothesis.
APA, Harvard, Vancouver, ISO, and other styles
6

Viñals, F., X. Testar, M. Palacín, and A. Zorzano. "Inhibitory effect of fluoride on insulin receptor autophosphorylation and tyrosine kinase activity." Biochemical Journal 291, no. 2 (April 15, 1993): 615–22. http://dx.doi.org/10.1042/bj2910615.

Full text
Abstract:
Fluoride is a nucleophilic reagent which has been reported to inhibit a variety of different enzymes such as esterases, asymmetrical hydrolases and phosphatases. In this report, we demonstrate that fluoride inhibits tyrosine kinase activity of insulin receptors partially purified from rat skeletal muscle and human placenta. Fluoride inhibited in a similar dose-dependent manner both beta-subunit autophosphorylation and tyrosine kinase activity for exogenous substrates. This inhibitory effect of fluoride was not due to the formation of complexes with aluminum and took place in the absence of modifications of insulin-binding properties of the insulin receptor. Fluoride did not complete with the binding site for ATP or Mn2+. Fluoride also inhibited the autophosphorylation and tyrosine kinase activity of receptors for insulin-like growth factor I from human placenta. Addition of fluoride to the pre-phosphorylated insulin receptor produced a slow (time range of minutes) inhibition of receptor kinase activity. Furthermore, fluoride inhibited tyrosine kinase activity in the absence of changes in the phosphorylation of prephosphorylated insulin receptors, and the sensitivity to fluoride was similar to the sensitivity of the unphosphorylated insulin receptor. The effect of fluoride-on tyrosine kinase activity was markedly decreased when insulin receptors were preincubated with the copolymer of glutamate/tyrosine. Prior exposure of receptors to free tyrosine or phosphotyrosine also prevented the inhibitory effect of fluoride. However, the protective effect of tyrosine or phosphotyrosine was maximal at low concentrations, suggesting the interaction of these compounds with the receptor itself rather than with fluoride. These data suggest: (i) that fluoride interacts directly and slowly with the insulin receptor, which causes inhibition of its phosphotransferase activity; (ii) that the binding site of fluoride is not structurally modified by receptor phosphorylation; and (iii) based on the fact that fluoride inhibits phosphotransferase activity in the absence of alterations in the binding of ATP, Mn2+ or insulin, we speculate that fluoride binding might affect the transfer of phosphate from ATP to the tyrosine residues of the beta-subunit of the insulin receptor and to the tyrosine residues of exogenous substrates.
APA, Harvard, Vancouver, ISO, and other styles
7

Koshio, O., Y. Akanuma, and M. Kasuga. "Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells." Biochemical Journal 250, no. 1 (February 15, 1988): 95–101. http://dx.doi.org/10.1042/bj2500095.

Full text
Abstract:
H-35 rat hepatoma cells were labelled with [32P]orthophosphate and their insulin receptors isolated on wheat germ agglutinin (WGA)-agarose and anti-(insulin receptor) serum. The incubation of these cells with 10 mM-H2O2 for 10 min increased the phosphorylation of both the serine and tyrosine residues of the beta subunit of the insulin receptor. Next, insulin receptors were purified on WGA-agarose from control and H2O2-treated H-35 cells and the purified fractions incubated with [gamma-32P]ATP and Mn2+. Phosphorylation of the beta subunit of insulin receptors obtained from H2O2-treated cells was 150% of that of control cells. The kinase activity of the WGA-purified receptor preparation obtained from H2O2-treated cells, as measured by phosphorylation of src-related synthetic peptide, was increased about 4-fold over control cells. These data suggest that in intact cell systems, H2O2 may increase the insulin receptor kinase activity by inducing phosphorylation of the beta subunit of insulin receptor.
APA, Harvard, Vancouver, ISO, and other styles
8

Yenush, L., R. Fernandez, M. G. Myers, T. C. Grammer, X. J. Sun, J. Blenis, J. H. Pierce, J. Schlessinger, and M. F. White. "The Drosophila insulin receptor activates multiple signaling pathways but requires insulin receptor substrate proteins for DNA synthesis." Molecular and Cellular Biology 16, no. 5 (May 1996): 2509–17. http://dx.doi.org/10.1128/mcb.16.5.2509.

Full text
Abstract:
The Drosophila insulin receptor (DIR) contains a 368-amino-acid COOH-terminal extension that contains several tyrosine phosphorylation sites in YXXM motifs. This extension is absent from the human insulin receptor but resembles a region in insulin receptor substrate (IRS) proteins which binds to the phosphatidylinositol (PI) 3-kinase and mediates mitogenesis. The function of a chimeric DIR containing the human insulin receptor binding domain (hDIR) was investigated in 32D cells, which contain few insulin receptors and no IRS proteins. Insulin stimulated tyrosine autophosphorylation of the human insulin receptor and hDIR, and both receptors mediated tyrosine phosphorylation of Shc and activated mitogen-activated protein kinase. IRS-1 was required by the human insulin receptor to activate PI 3-kinase and p70s6k, whereas hDIR associated with PI 3-kinase and activated p70s6k without IRS-1. However, both receptors required IRS-1 to mediate insulin-stimulated mitogenesis. These data demonstrate that the DIR possesses additional signaling capabilities compared with its mammalian counterpart but still requires IRS-1 for the complete insulin response in mammalian cells.
APA, Harvard, Vancouver, ISO, and other styles
9

Tavaré, J. M., and M. Dickens. "Changes in insulin-receptor tyrosine, serine and threonine phosphorylation as a result of substitution of tyrosine-1162 with phenylalanine." Biochemical Journal 274, no. 1 (February 15, 1991): 173–79. http://dx.doi.org/10.1042/bj2740173.

Full text
Abstract:
Previous studies, by ourselves and others, have shown that tyrosine residues 1158, 1162 and 1163 are very rapidly autophosphorylated on the human insulin receptor after insulin binding and that this is followed by the autophosphorylation of tyrosine residues 1328 and 1334. The autophosphorylation of these tyrosine residues, and their role in transmembrane signalling, were examined by using Chinese-hamster ovary cells transfected with either normal intact insulin receptors or receptors in which tyrosine residues 1162 or 1162/1163 were substituted with phenylalanine. These studies show the following. (1) Tyrosine-1158 could still be autophosphorylated when tyrosine-1162 and -1163 were substituted with phenylalanine. (2) Insulin-stimulated insulin-receptor tyrosine phosphorylation in intact cells was complete within 30 s and was accompanied, after a lag of 2-5 min, by a rise in serine and threonine phosphorylation the beta-subunit. (3) Replacement of tyrosine-1162 with phenylalanine blocked insulin-stimulated threonine phosphorylation of the insulin receptor in intact cells. (4) Insulin-stimulated serine phosphorylation of the beta-subunit was found in both intact cells and partially purified receptor preparations incubated with [gamma-32P]ATP and was still apparent after the replacement of tyrosine-1162 with phenylalanine. (5) Our data strongly suggest that insulin-stimulated insulin-receptor serine and threonine phosphorylations are initiated through two distinct pathways, with only the latter showing a strict dependence on autophosphorylation of tyrosine-1162.
APA, Harvard, Vancouver, ISO, and other styles
10

Tanti, J. F., T. Grémeaux, N. Rochet, E. Van Obberghen, and Y. Le Marchand-Brustel. "Effect of cyclic AMP-dependent protein kinase on insulin receptor tyrosine kinase activity." Biochemical Journal 245, no. 1 (July 1, 1987): 19–26. http://dx.doi.org/10.1042/bj2450019.

Full text
Abstract:
To explain the insulin resistance induced by catecholamines, we studied the tyrosine kinase activity of insulin receptors in a state characterized by elevated noradrenaline concentrations in vivo, i.e. cold-acclimation. Insulin receptors were partially purified from brown adipose tissue of 3-week- or 48 h-cold-acclimated mice. Insulin-stimulated receptor autophosphorylation and tyrosine kinase activity of insulin receptors prepared from cold-acclimated mice were decreased. Since the effect of noradrenaline is mediated by cyclic AMP and cyclic AMP-dependent protein kinase, we tested the effect of the purified catalytic subunit of this enzyme on insulin receptors purified by wheat-germ agglutinin chromatography. The catalytic subunit had no effect on basal phosphorylation, but completely inhibited the insulin-stimulated receptor phosphorylation. Similarly, receptor kinase activity towards exogenous substrates such as histone or a tyrosine-containing copolymer was abolished. This inhibitory effect was observed with receptors prepared from brown adipose tissue, isolated hepatocytes and skeletal muscle. The same results were obtained on epidermal-growth-factor receptors. Further, the catalytic subunit exerted a comparable effect on the phosphorylation of highly purified insulin receptors. To explain this inhibition, we were able to rule out the following phenomena: a change in insulin binding, a change in the Km of the enzyme for ATP, activation of a phosphatase activity present in the insulin-receptor preparation, depletion of ATP, and phosphorylation of a serine residue of the receptor. These results suggest that the alteration in the insulin-receptor tyrosine kinase activity induced by cyclic AMP-dependent protein kinase could contribute to the insulin resistance produced by catecholamines.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Insulin receptor tyrosine"

1

Lew, Gregory John. "Studies on protein phosphorylation in response to insulin in isolated cellular fractions reconstituted with insulin receptors." Thesis, University of British Columbia, 1988. http://hdl.handle.net/2429/27979.

Full text
Abstract:
The mechanism by which insulin and other polypeptide growth factors alter cellular metabolism is not fully understood. In the case of insulin, it is thought that phosphorylation/dephosphorylation mechanisms may play a central role in the signalling pathway. This is based on evidence which includes demonstration that the receptor for insulin is a tyrosine-specific protein kinase which is activated in response to insulin binding. Ultimately, insulin binding to its receptor on the surface of intact fat cells leads to altered levels of serine phosphorylation of several soluble proteins, including the phosphorylation of ATP-citrate lyase and acetyi-CoA carboxylase. Recently, studies involving site-specific mutagenesis have shown that the tyrosine kinase function of the insulin receptor is essential for insulin signalling. The studies described in this thesis have addressed the problem of how activation of the insulin receptor/tyrosine kinase results in the altered serine phosphorylation observed in intact cells in response to insulin. To gain further understanding of the cellular components required for insulin signalling, reconstitution experiments have been carried out mixing isolated cellular fractions with preparations of insulin receptors. The effects of insulin on altering protein-serine and protein-tyrosine phosphorylation have been determined in this reconstituted system. Results show that in a high-speed (100,000 x g) supernatant fraction prepared from rat adipose tissue endogenous protein-serine kinases are sensitive to conditions which are commonly employed for assaying insulin receptor/kinase activity. This includes inhibition by micromolar concentrations of MnCI₂, by 40 mM NaF, and by low reaction temperature (0°C). When the insulin receptor, present in a WGA-Sepharose-purified preparation of detergent-solublized rat liver membranes, was assayed in the complete absence of both MnCI₂ and NaF, receptor/tyrosine kinase activity was only slightly reduced with little or no decrease in the responsiveness to insulin. Furthermore, when the WGA-Sepharose-purified membrane fraction was incubated at 37°C in the presence of [ɣ -³²P]ATP several endogenous proteins were observed to be phosphorylated in addition to the β-subunit of the insulin receptor. These membrane proteins appear to be phosphorylated on tyrosine as indicated by their resistance to alkali hydrolysis. Upon reconstitution of the adipose tissue high-speed supernatant fraction with the WGA-Sepharose-purified preparation of insulin receptors the most striking effects observed were the phosphorylation of a 40 kd protein subunit (pp40) and the dephosphorylation of a 25 kd protein subunit (pp25) present in adipose tissue. The phosphorylation of pp40 occurs on tyrosine and is insulin-responsive, whereas the dephosphorylation of pp25 occurs following reconstitution with either untreated control, or insulin-activated insulin receptors. To assess the effect that reconstituted insulin receptors may have on the phosphorylation of endogenous ATP-citrate lyase in adipose tissue high-speed supernatant, it was found that a more pure preparation of insulin receptors was required. Further purification of the insulin receptor to homogeneity was therefore attempted using insulin-agarose affinity chromatography. However, difficulties including low yield and instability of the receptor through purification have prevented progress with these studies at present. In a separate study, highly purified acetyl-CoA carboxylase was reconstituted with a crude fraction consisting of total Triton-solublized membrane proteins. In this reconstituted system phosphorylation of acetyl-CoA carboxylase was enhanced to an extent greater than 6-fold after incubation with [ɣ -³²P]ATP. Following chromatography of the crude Triton-solublized extract over WGA-Sepharose this acetyl-CoA carboxylase kinase activity was found to be present in the flow-through void fraction and not in the N-acetylglucosamine eluted fraction. The acetyl-CoA carboxylase kinase, at present, does not appear to be insulin-responsive, but further studies are needed to confirm this observation.
Medicine, Faculty of
Biochemistry and Molecular Biology, Department of
Graduate
APA, Harvard, Vancouver, ISO, and other styles
2

O'Brien, Richard Mark. "Studies on the insulin receptor tyrosine-specific protein kinase." Thesis, University of Cambridge, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252645.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Lynch, Deborah Frances. "The role of tyrosine, serine and threonine phosphorylation in the regulation of the insulin receptor tyrosine kinase activity." Thesis, University of Bristol, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282141.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Jozic, Ivan. "Selective and Specific Activation of Rab5 during Endocytosis of Receptor Tyrosine Kinases." FIU Digital Commons, 2013. http://digitalcommons.fiu.edu/etd/813.

Full text
Abstract:
The Rab family of proteins are low molecular weight GTPases that have the ability to switch between GTP- (active) and GDP- (inactive) bound form, and in that sense act as molecular switches. Through distinct localization on various vesicles and organelles and by cycling through GTP/GDP bound forms, Rabs are able to recruit and activate numerous effector proteins, both spatially and temporally, and hence behave as key regulators of trafficking in both endocytic and biosynhtetic pathways. The Rab5 protein has been shown to regulate transport from plasma membrane to the early endosome as well as activate signaling pathways from the early endosome. This dissertation focused on understanding Rab5 activation via endocytosis of receptor tyrosine kinases (RTKs). First, tyrosine kinase activity of RTKs was linked to endosome fusion by demonstrating that tyrosine kinase inhibitors block endosome fusion and activation of Rab5, and a constitutively active form of Rab5 is able to rescue endosome fusion. However, depending on how much ligand is available at the cell surface, the receptor-ligand complexes can be internalized via a number of distinct pathways. Similarly, Rab5 was activated in a ligand-dependent concentration dependent manner via clathrin- and caveolin-mediated pathways, as well as a pathway independent of both. However, overexpression Rabex-5, a nucleotide exchange factor for Rab5, is able to rescue activation even when all of the pathways of EGF-receptor internalization were blocked. Next, the three naturally occurring splice variants of Rabex-5 selectively activated Rab5. Lastly, Rabex-5 inhibits differentiation of 3T3-L1 and PC12 cells through 1) degradation of signaling endosome via Rab5-dependent fusion with the early endosome, 2) and inhibition of signaling cascade via ubiquitination of Ras through the ZnF domain at the N-terminus of Rabex-5. In conclusion, these data shed light on complexity of the endosomal trafficking system where tyrosine kinase activity of the receptor is able to affect endosome fusion; how different endocytic pathways affect activation of one of the key regulators of early endocytic events; and how selective activation of Rab5 via Rabex-5 can control adipogenesis and neurogenesis.
APA, Harvard, Vancouver, ISO, and other styles
5

Hughes, Stephen Bernard. "Development of real-time reverse transcription polymerase chain reaction assays to quantify insulin-like growth factor-1 receptor and insulin receptor expression in equine tissue." Diss., University of Pretoria, 2011. http://hdl.handle.net/2263/31135.

Full text
Abstract:
has been significant progress in the development of new technologies and methodologies to characterize gene expression. The fluorescent-based real-time reverse transcription (RT) polymerase chain reaction (PCR) is an important tool used for clinical and molecular research, biotechnology and as a diagnostic test. Insulin-like growth factors (IGF-1 and IGF-2) and insulin are ubiquitously expressed and play important roles in the regulation of cell growth, differentiation and the maintenance of cell differentiation in mammals. The IGF system (IGF-1, IGF-2, IGF -1 receptor, IGF-2 receptor and six IGF-binding proteins) and insulin are consequently essential to most aspects of male and female reproduction. IGF-1 is produced in multiple tissues but predominately in the liver, from where it enters the circulation. Insulin is secreted by β-cells of the pancreas’ islets of Langerhans. Both IGF-1 and insulin polypeptides bind to specific cell surface receptors. These receptors are members of the superfamily known as tyrosine protein kinases, and are composed of two α and two β subunits linked by disulfide bonds to form an αβ–αβ heterotetramer. The α subunits include ligand binding sites, whereas the β subunits contain tyrosine kinase activity. The aim of this project was to develop real-time RT-PCR assays for quantification of equine insulin-like growth factor-1 receptor (IGF-1R) and insulin receptor (INS-R) mRNA. The assays were developed using stallion testicular tissue samples, obtained by excisional biopsy, from three horse breeds (Friesan, Thoroughbred and Warmblood). The assays developed were efficient, sensitive and had a broad linear range of detection (seven logs for IGF-1R and six logs for INS-R). The assays worked well in our hands and were both sensitive and specific for the detection of equine IGF-1R and INS-R mRNA in a variety of equine tissues.
Dissertation (MMedVet)--University of Pretoria, 2011.
Production Animal Studies
Unrestricted
APA, Harvard, Vancouver, ISO, and other styles
6

Kupzig, Sabine. "Identification and characterisation of two novel proteins of the secretory pathway." Thesis, University of Bristol, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.245577.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Sun, Clement. "Function of receptor tyrosine kinases in G¦i-deficient cells, preferential suppression of insulin signalling." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0023/MQ50413.pdf.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Dool, Carly Jade 1985. "Pharmacologic inhibition of insulin receptor tyrosine kinase activity has antineoplastic effects similar to alloxan-induced insulin deficiency with less acute metabolic toxicity." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=111555.

Full text
Abstract:
Recent population studies provide evidence that individuals with high circulating insulin levels have a poor prognosis and/or increased risk of cancer development; however, laboratory studies concerning the role of insulin in breast cancer biology are sparse. We compared the growth of 4T1 murine breast cancer allografts in control mice, alloxan-induced hypoinsulinemic mice, and mice treated with the insulin/insulin-like growth factor-1 receptor tyrosine kinase inhibitor BMS-536924. Both interventions significantly decreased tumor growth versus control and decreased pathway activation downstream of the insulin receptor as reflected by Aktser473 phosphorylation status in the neoplastic tissue. Alloxan-treated mice exhibited signs of insulin deficiency, while BMS-536924-treated animals showed only minor metabolic derangements. Skeletal muscle displayed reduced pAktser473 in alloxan-treated mice. In contrast, BMS-536924 treatment increased pAktser473 in muscle. This raises the possibility that the relative lack of metabolic toxicity of BMS-536924 involves varying tissue levels of the drug. These results support the view that host insulin physiology is a potentially modifiable determinant of breast cancer behaviour.
APA, Harvard, Vancouver, ISO, and other styles
9

Abhyankar, Lalita. "The effect of reducing insulin degrading enzyme in HEPG2 cells on activation of insulin receptor, IRS-1 and SHC by tyrosine phosphorylation." Thesis, The University of Arizona, 2009. http://hdl.handle.net/10150/192259.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Zapf-Colby, Antje. "Mechanisms of specificity in the tyrosine kinase receptor signal transduction pathways of nerve growth factor, insulin-like growth factor-I, and insulin /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 1997. http://wwwlib.umi.com/cr/ucsd/fullcit?p9814555.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Insulin receptor tyrosine"

1

Keane, Noeleen Emily. Nuclear magnetic resonance studies of the human insulin receptor tyrosine kinase autophosphorylation and activity. Birmingham: University of Birmingham, 1994.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Alaimo, Darrick James. Hepatic insulin receptor tyrosine kinase activity in diabetes: Modulation by assorted adenosine triphosphatases/phosphatases which copurify in partially purified preparations of the insulin receptor. [s.l: s.n.], 1992.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Function of receptor tyrosine kinases in Gi-deficient cells: Preferential suppression of insulin signalling. Ottawa: National Library of Canada, 2000.

Find full text
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Insulin receptor tyrosine"

1

Rothenberg, P., M. F. White, and C. R. Kahn. "The Insulin Receptor Tyrosine Kinase." In Insulin, 209–36. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-74098-5_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Van Obberghen, E., S. Gammeltoft, Y. Le Marchand-Brustel, and R. Ballotti. "Insulin receptor tyrosine kinase and insulin action." In Cell to Cell Signals in Mammalian Development, 183–92. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73142-6_15.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Youngren, Jack F., Ira D. Goldfine, Vincenzo Trischitta, and Betty A. Maddux. "Insulin Resistance and Inhibitors of Insulin Receptor Tyrosine Kinase." In Insulin Resistance, 139–58. Totowa, NJ: Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-716-1_8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Drake, Paul G., and Barry I. Posner. "Insulin receptor-associated protein tyrosine phosphatase(s): Role in insulin action." In Insulin Action, 79–89. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5647-3_9.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Van Obberghen, E., S. Gammeltoft, Y. Le Marchand-Brustel, and R. Ballotti. "Insulin Receptor: Role of Receptor Tyrosine Kinase in Insulin Signalling and Action." In Bayer AG Centenary Symposium, 73–81. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74255-2_6.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Petruzzelli, Lilli M., Laurel Stadtmauer, Roman Herrera, Mary Makowske, Sabyasachi Ganguly, Diane Tabarini, Hua Lee, Yetunde Olowe, and Ora M. Rosen. "The Insulin Receptor as a Tyrosine- Specific Protein Kinase." In Mechanisms of Receptor Regulation, 53–64. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4613-2131-6_4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Youngren, Jack F. "Insulin Resistance and Inhibitors of the Insulin Receptor Tyrosine Kinase." In The Metabolic Syndrome, 279–305. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-116-5_15.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

White, Morris F. "Receptor Tyrosine Kinases and the Insulin Signaling System." In Endocrinology, 1–34. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-27318-1_7-1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

White, Morris F. "Receptor Tyrosine Kinases and the Insulin Signaling System." In Endocrinology, 121–55. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-44675-2_7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Carboni, Joan M., Mark Wittman, and Fei Huang. "Targeting Insulin-Like Growth Factor Receptor 1 (IGF-1R) and Insulin Receptor Signaling by Tyrosine Kinase Inhibitors in Cancer." In Insulin-like Growth Factors and Cancer, 215–29. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0598-6_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Insulin receptor tyrosine"

1

Beeler, D., L. Fritze, G. Soff, R. Jackman, and R. Rosenberg. "HUMAN THROMBOMODULIN cDNA:SEQUENCE AND TRANSLATED STRUCTURE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643967.

Full text
Abstract:
A 750 bp bovine Thrombomodulin (TM) cDNA fragment was used as an hybridization probe to screen an oligo-dT primed Lambda gtll. cDNA library prepared from human umbilical vein endothelial cell mRNA. A 2.4 kb positive human clone was isolated which showed an 80% nucleotide sequence homology with bovine TM cDNA. This clone and a 550 bp fragment from its 5' end were used to further screen the oligo-dT primed library as well as randomly primed library prepared from the same mRNA. The cDNA clones obtained allow us to describe the overall structure of human TM and reveal that it is extremely similar to the structure of bovine TM, especially as the bovine TM is organized like the receptor for low density lipoprotein (LDL R). Both TM and LDL R exhibit short cytoplasmic C-terminal tails which are either neutral or negatively charged. Other coated pit receptors such as the insulin receptor or the epidermal growth factor (EGF) receptor have very large cytoplasmic regions with a complex tyrosine kinase segment as well as multiple sites for phosphorylation. Both TM and LDL R possess a transmembrane region and an immediately adjacent extracellular serine/threonine rich region which in LDL R has been shown to bear 0-1inked sugars. Both TM and LDL R contain a more distal area of cysteine rich repeats, first noted in the EGF precursor and termed EGF type B. However, the TM EGF type B repeats appear to have been duplicated in TM resulting in their being 6 of them rather than the 3 found in LDL R. The N-terminal half of LDL R is thought to contain the ligand binding region of the receptor and is constructed from multiple cysteine rich repeats similar to those of Complement factor C9. The structure of this region of TM is quite different from that of LDL R, possessing few cysteines. We suspect that protein C and/or thrombin may bind to this unique domain of TM.
APA, Harvard, Vancouver, ISO, and other styles
2

Wang, Gary T., Robert A. Mantei, Robert D. Hubbard, Julie L. Wilsbacher, Qian Zhang, Lora Tucker, Xiaoming Hu, et al. "Abstract A248: Substituted 4‐amino‐1H‐pyrazolo[3,4‐d]pyrimidines as multitargeted inhibitors targeting insulin‐like growth factor‐1 receptor (IGF1R) and members of ErbB‐family receptor tyrosine kinases." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-a248.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Stanicka, Joanna, Leonie Rieger, Orla T. Cox, Sandra O'Shea, Michael Coleman, Ciara O'Flanagan, Barbara Addario, Nuala McCabe, Richard Kennedy, and Rosemary O'Connor. "Abstract 1794: The FES-related tyrosine kinase associates with and activates the insulin-like growth factor 1 receptor at sites of cell adhesion." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1794.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Gedrich, Richard, Srini Poondru, Andrew Stephens, Tiffany Logan, Karen Hart, Elizabeth Buck, Craig Carden, et al. "Abstract A46: Pharmacodynamic biomarkers for OSI‐906, an insulin‐like growth factor‐1 receptor (IGF‐1R) tyrosine kinase inhibitor, in cancer patients with advanced solid tumors." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-a46.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Ioannou, Nikolaos, Alan M. Seddon, Angus Dalgleish, David Mackintosh, and Helmout Modjtahedi. "Abstract 630: Responses of human pancreatic cancer cells to treatment with insulin-like growth factor receptor (IGF-IR) tyrosine kinase inhibitor NVP-AEW541 alone and in combination with anti-EGFR mAb ICR62 or cytotoxic drugs." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-630.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Insulin receptor tyrosine' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography