Insulin Signaling and the Regulation of Glucose Transport

Chang, Louise; Chiang, Shian-Huey; Saltiel, Alan R.

doi:10.2119/2005-00029.saltiel

Cited by 409 publications

(262 citation statements)

References 82 publications

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“…Co-inheritance of α- and β-thalassaemia in Malaysia was studied to determine the different types and frequency of α-thalassaemia defects. An earlier study in Malaysia reported 3.5% of β-thalassaemia carriers as concurrent carriers of α-thalassaemia with the SEA deletion [16]. In this study, α-thalassaemia (-- SEA , -α 3.7 and -α 4.2 deletions, Hb Constant Spring) was found in 12.7% of the β-thalassaemia carriers.…”

Section: Discussionmentioning

confidence: 46%

“…Studies of co-inheritance of α- and β-thalassaemia in Malaysia has been limited to α⁰ (SEA) deletion; the other types of α-thalassaemia have not been studied [16]. The co-inheritance of both thalassaemias has been observed in 8–9% of patients in Hong Kong [17, 18] and 11.07–15.1% in the Guangdong district of Southern China [13, 19].…”

Section: Introductionmentioning

confidence: 99%

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Alpha-Thalassaemia in Association with Beta-Thalassaemia Patients in Malaysia: A Study on the Co-Inheritance of Both Disorders

Wee

Tan

Kuldip

et al. 2008

Public Health Genomics

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Background/Aims: Individuals with double heterozygosity for α- and β-thalassaemia and heterozygous β-thalassaemia show a similar haematological picture. Co-inheritance of α- and β-thalassaemia in both partners may result in pregnancies with either Hb Bart’s hydrops foetalis or β-thalassaemia major, or pregnancies with both disorders. Methods: The co-inheritance of α-thalassaemia in 322 β-thalassaemia carriers in Malaysia was studied. Results: The frequency of α-thalassaemia in the β-thalassaemia carriers was 12.7% (41/322), with a carrier frequency of 7.8% for the SEA deletion, 3.7% for the -α^3.7 deletion, 0.9% for Hb Constant Spring and 0.3% for the -α^4.2 deletion. Conclusion: Double heterozygosity for α- and β-thalassaemia was confirmed in 5 out of the 41 couples and the risk of the fatal condition Hb Bart’s hydrops foetalis was confirmed in two of these couples. Detection of the Southeast Asian (SEA) deletion in the Malaysian Malays in this study confirms that Hb Bart’s hydrops foetalis can occur in this ethnic group. Results of this study have provided new information on the frequency and different types of α-thalassaemia (--^SEA, -α^3.7 and -α^4.2 deletions, Hb Constant Spring) in Malaysian β-thalassaemia carriers.

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Section: Discussionmentioning

confidence: 46%

Section: Introductionmentioning

confidence: 99%

Alpha-Thalassaemia in Association with Beta-Thalassaemia Patients in Malaysia: A Study on the Co-Inheritance of Both Disorders

Wee

Tan

Kuldip

et al. 2008

Public Health Genomics

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“…Furthermore, SH2B2 mediates insulin-stimulated plasma membrane translocation of both c-Cbl and Cbl-b in adipocytes [140] . SH2B2 also binds to CAP [134,139] and mediates the activation of the CAP/Cbl/Crk/C3G/TC10 pathway in adipocytes [142] . The SH2B2/CAP/Cbl/Crk/C3G/TC10 pathway is believed to be required for insulin stimulation of GLUT4 trafficking and glucose uptake in adipocytes [142] ; consistently, overexpression of SH2B2(Y618F) inhibits insulin-stimulated GLUT4 trafficking [134] .…”

Section: Sh2b2 Structurementioning

confidence: 99%

“…SH2B2 also binds to CAP [134,139] and mediates the activation of the CAP/Cbl/Crk/C3G/TC10 pathway in adipocytes [142] . The SH2B2/CAP/Cbl/Crk/C3G/TC10 pathway is believed to be required for insulin stimulation of GLUT4 trafficking and glucose uptake in adipocytes [142] ; consistently, overexpression of SH2B2(Y618F) inhibits insulin-stimulated GLUT4 trafficking [134] . However, SH2B2 also promotes c-Cbl-mediated ubiquitination and internalization of insulin receptors, thus inhibiting insulin signaling [138,143] .…”

Section: Sh2b2 Structurementioning

confidence: 99%

SH2B1 regulation of energy balance, body weight, and glucose metabolism

Rui

2014

WJD

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The Src homology 2B (SH2B) family members (SH2B1, SH2B2 and SH2B3) are adaptor signaling proteins containing characteristic SH2 and PH domains. SH2B1 (also called SH2-B and PSM) and SH2B2 (also called APS) are able to form homo-or hetero-dimers via their N-terminal dimerization domains. Their C-terminal SH2 domains bind to tyrosyl phosphorylated proteins, including Janus kinase 2 (JAK2), TrkA, insulin receptors, insulin-like growth factor-1 receptors, insulin receptor substrate-1 (IRS1), and IRS2. SH2B1 enhances leptin signaling by both stimulating JAK2 activity and assembling a JAK2/ IRS1/2 signaling complex. SH2B1 promotes insulin signaling by both enhancing insulin receptor catalytic activity and protecting against dephosphorylation of IRS proteins. Accordingly, genetic deletion of SH2B1 results in severe leptin resistance, insulin resistance, hyperphagia, obesity, and type 2 diabetes in mice. Neuronspecific overexpression of SH2B1β transgenes protects against diet-induced obesity and insulin resistance. SH2B1 in pancreatic β cells promotes β cell expansion and insulin secretion to counteract insulin resistance in obesity. Moreover, numerous SH2B1 mutations are genetically linked to leptin resistance, insulin resistance, obesity, and type 2 diabetes in humans. Unlike SH2B1, SH2B2 and SH2B3 are not required for the maintenance of normal energy and glucose homeostasis. The metabolic function of the SH2B family is conserved from insects to humans. Key words: Obesity; Type 2 diabetes; Leptin resistance; Insulin resistance; Glucose intolerance; Hypothalamus; Energy balance; Food intake; Hyperphagia; Nonalcoholic fatty liver disease Core tip: The Src homology 2B (SH2B) family members mediate cell signaling in response to a variety of hormones, cytokines, and growth factors. In the brain, SH2B1 enhances leptin signaling and leptin's antiobesity action. In peripheral tissues, SH2B1 cell-autonomously enhances insulin signaling. In pancreatic islets, SH2B1 is required for compensatory β cell expansion in response to insulin resistance and β cell stress. SH2B1-deficiency results in severe leptin resistance, energy imbalance, obesity, and type 2 diabetes. SH2B1 mutations are linked to leptin resistance, insulin resistance, obesity, and type 2 diabetes in humans. Thus, SH2B1 is a critical metabolic regulator in mammals.Rui L. SH2B1 regulation of energy balance, body weight, and glucose metabolism. World J Diabetes 2014; 5(4): 511-526 Available from:

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“…Glucose transporter-4 (GLUT4), the predominant insulin-responsive glucose transporter isoform, plays a key role in the process of transporting extracellular glucose into insulin-sensitive cells in vivo (Chang et al, 2004;Asano et al, 2007;Huang and Czech, 2007). It exists only in skeletal muscle and adipose tissues (Suárez et al, 2001), which are responsible for 50% to 80% of glucose transportation in the body.…”

Section: Introductionmentioning

confidence: 99%

Effects of GLUT4 expression on insulin resistance in patients with advanced liver cirrhosis

Shan

Chen

Zhu

et al. 2011

J. Zhejiang Univ. Sci. B

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Abstract:Decreased glucose tolerance and diabetes are frequently observed in advanced liver cirrhosis patients and may be related to insulin resistance. Glucose transporter-4 (GLUT4), one of the most important glucose transporters, plays a key role in the development of type 2 diabetes. In order to study the mechanism of insulin resistance in liver cirrhosis patients, we measured the insulin sensitivity index and determined the GLUT4 protein and mRNA contents of skeletal muscle by Western blotting and reverse transcription-polymerase chain reaction (RT-PCR), respectively, in normal people and liver cirrhosis patients. The results showed that the levels of glucose, insulin, and C-peptide in two liver cirrhosis groups were higher and the insulin sensitivity index lower than those of the normal control group. The sensitivity of insulin may decrease with the decline of liver function. However, the contents of GLUT4 protein and mRNA in patients with advanced liver cirrhosis were similar to those of normal controls. In conclusion, insulin resistance is observed in patients with advanced liver cirrhosis but may not be correlated with the skeletal contents of GLUT4 protein and mRNA.

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Insulin Signaling and the Regulation of Glucose Transport

Cited by 409 publications

References 82 publications

Alpha-Thalassaemia in Association with Beta-Thalassaemia Patients in Malaysia: A Study on the Co-Inheritance of Both Disorders

Alpha-Thalassaemia in Association with Beta-Thalassaemia Patients in Malaysia: A Study on the Co-Inheritance of Both Disorders

SH2B1 regulation of energy balance, body weight, and glucose metabolism

Effects of GLUT4 expression on insulin resistance in patients with advanced liver cirrhosis

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