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Camelus dromedarius glucose transporter 4: in silico analysis, cloning, expression, purification and characterisation
Anwar Ahmed1,2, Mohammed Arshad1, Ajamaluddin Malik1
1a Protein Research Chair, Department of Biochemistry, College of Science , King Saud University , Riyadh , Saudi Arabia.
Abstract:
Camels have exceptional carbohydrate metabolism as their plasma glucose level is high and have low whole body insulin sensitivity, similar to that observed in type 2 diabetes patients. We aimed at studing an important component of insulin signalling pathway, the GLUT4, in camel. Camelus dromedarius GLUT4 (CdGLUT4) CDS is 1530 nucleotide in length that encodes for a 55KDa protein. CdGLUT4 has 23 amino acid substitutions and 3N-glycosylation sites, compared to 2 in Human GLUT4. 3 D structures of CdGLUT4 and HsGLUT4 generated by homology modelling revealed conservation of characteristic signature motifs. CdGLUT4 was cloned and expressed optimally in C43(DE3)pLysS strain and maximum detergent solubility was observed in n-Dodecyl-β-d-maltopyranoside. These preliminary data provide information on residual differences between CdGLUT4 and HsGLUT4 that may be responsible for camel's unique glucose metabolism. These differences are postulated to assist in designing and development of efficacious GLUT4 that might help in management of diabetic patients.
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