Disease relevance of SLC2A4

• The nutritional regulation of glucose transporter GLUT4 was studied in eight muscles and four adipose tissues from two groups of preruminant (PR) or ruminant (R) calves of similar age (170 d), empty body weight (194 kg) at slaughter, and level of net energy intake from birth onwards [1].

High impact information on SLC2A4

• Insulin-perfused muscles showed significant increases in glucose uptake and GLUT4 translocation, but AMPK activation was not significantly changed from basal levels [2].
• 5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle [2].
• This study was designed to determine whether the increase in glucose uptake observed with AMPK activation by AICA-riboside is due to GLUT4 translocation from an intracellular location to the plasma membranes, similar to that seen in response to contraction [2].
• These results provide evidence that the increased glucose uptake observed with AMPK activation by AICA-riboside in perfused rat hindlimb muscles is due to an increase in the translocation of GLUT4 to surface membranes [2].
• A GLUT4-like protein was detected by immunoblot assay in all insulin-responsive tissues from calf and goat (heart, skeletal muscle, adipose tissue) but not in liver, brain, erythrocytes and intestine [3].

Biological context of SLC2A4

• The deduced amino acid sequence was 64% and 92% identical with bovine GLUT1 (GLUT ubiquitously expressed in all tissues) and rat GLUT4, respectively [4].
• The tissue distribution of GLUT4 was also examined by Northern blot analysis using a probe prepared from the bovine cDNA [4].
• Nucleotide sequence analysis of the cDNA clones revealed that bovine GLUT4 cDNA was composed of 2,656 base pairs with a coding region for a 509 amino acid protein [4].
• To clarify the molecular structure of bovine GLUT4, its GLUT4 cDNA was cloned by the RT-PCR method [4].
• Factors other than GLUT4 may be involved in insulin resistance [5].

Anatomical context of SLC2A4

• Moreover, GLUT4 mRNA amounts were quantified by Northern-blot analysis in heart and seven skeletal muscles with various oxidative and glycolytic activities from seven ruminant calves [6].
• GLUT4 mRNA was detected in skeletal muscle, heart, and adipose tissue, but not in liver, kidney, lung, brain, or spleen [4].
• The Rab4-(191-210) peptide also reduced insulin-induced GLUT4 translocation from the intracellular pool to the plasma membrane [7].
• There were no significant differences in the expression of insulin responsive glucose transporter (GLUT4) mRNA between the adipose tIssue of lactating and non-lactating cows, and GLUT4 mRNA was not detected in the mammary gland [8].
• This is the first report on the expression of the insulin-sensitive Glut4 isoform in mammalian preimplantation embryos [9].

Associations of SLC2A4 with chemical compounds

• Previous studies have shown that the expression of the insulin-sensitive glucose transporter (GLUT4) is lower in oxidative muscles than in glycolytic muscles in bovines and goats in contrast to observations in rats [6].
• Although the amino acid sequence of the GLUT4 COOH-terminal region is highly conserved among the species so far reported, one amino acid (Asp) of the region was replaced by His in bovine GLUT4 [4].
• METHODS AND RESULTS: Glucose deprivation and indinavir, a GLUT4 antagonist, were used to assess the role of GLUT4 and non-GLUT4 transporters in vascular reactivity [10].
• Indinavir caused a less profound attenuation of maximal 5-HT-mediated contraction in these vessels, corresponding to the lower GLUT4 levels in the hypertensive aortas [10].
• We also observed a 46% decrease in GLUT4 expression in aortas from angiotensin II hypertensive mice [10].

Other interactions of SLC2A4

• This PCR-amplified bovine GLUT4 probe was used to determine the distribution of GLUT4 mRNA in bovine tissues in comparison with that of GLUT1 mRNA [6].
• Whether the culture environment was in vitro or in vivo affected the expression of glucose transporter transcripts Glut-3, Glut-4 and Glut-8 [11].
• Nutritional status induces divergent variations of GLUT4 protein content, but not lipoprotein lipase activity, between adipose tissues and muscles in adult cattle [12].

Analytical, diagnostic and therapeutic context of SLC2A4

• GLUT4 mRNA was detected by Northern-blot analysis only in calf insulin-sensitive tissues [6].
• A 241-bp fragment of the bovine GLUT4 cDNA was cloned by polymerase chain reaction (PCR) [6].
• Molecular cloning and mRNA expression of the bovine insulin-responsive glucose transporter (GLUT4) [4].
• Perfusion medium containing AICA-riboside was found to significantly increase AMPK activity, glucose uptake, and GLUT4 translocation in skeletal muscle above basal levels [2].
• To examine the postnatal change in the GLUTs of ruminants, the protein levels of GLUT1 and GLUT4 were measured by Western blot analysis of skeletal muscles, adipose tissue and brain of Holstein male calves aged from 0 to 12 months [13].

References