Insulin resistance mediated biochemical alterations in eye lens of neonatal streptozotocin-induced diabetic rat

Cataract, the leading cause of blindness worldwide, is associated with many risk factors including diabetes. Impaired glucose tolerance (IGT) and impaired fasting glucose (IFG) states are associated with pre-diabetes and insulin resistance. This condition subsequently leads to the development of type-2 diabetes. Epidemiological studies indicated that not only diabetes but IGT/IFG will also lead to the development of microvascular disorders and cataract. However, there are no studies on the mechanism of insulin resistance induced changes in the eye lens. In the present study, IGT/IFG-induced changes in lens using neonatal-streptozotocin (nSTZ) rat model have been investigated. Though, nSTZ rats showed the signs of IGT and insulin resistance starting from two months old, they did not develop cataract even at the age of 8-months. However, biochemical analysis indicates a three-fold increase in sorbitol levels in nSTZ lens upon prolonged (6-months) IGT and insulin resistance. Also there was an increase in lipid peroxidation and alterations in antioxidant enzymes. Results of this study showed that activation of polyol pathway and increased oxidative stress, commonly associated with long-term complications of diabetes, have been observed in eye lens due to prolonged IGT and insulin resistance which may lead to cataract.     

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Primary structure of belladonna mottle virus coat protein

The coat protein of belladonna mottle virus (a tymovirus) was cleaved by trypsin and chymotrypsin, and the peptides were separated by high performance liquid chromatography using a combination of gel permeation, reverse phase, and ion pair chromatography. The peptides were sequenced manually using the 4-N, N-dimethylaminoazobenzene-4'-isothiocyanate/phenyl isothiocyanate double-coupling method. The chymotryptic peptides were aligned by overlapping sequences of tryptic peptides and by homology with another tymovirus, eggplant mosaic virus. The belladonna mottle virus is more closely related to eggplant mosaic virus than to turnip yellow mosaic virus, the type member of this group, as evident from the sequence homologies of 57 and 32%, respectively. The accumulation of basic residues at the amino terminus implicated in RNA-protein interactions in many spherical plant viruses was absent in all the three sequences. Interestingly, the amino-terminal region is the least conserved among the tymoviruses. The longest stretch of conserved sequence between belladonna mottle virus and eggplant mosaic virus was residues 34-44, whereas it was residues 96-102 in the case of belladonna mottle virus and turnip yellow mosaic virus. A tetrapeptide in the region (residues 154-157) was found to be common for all the three sequences. It is possible that these conserved regions (residues 34-44, 96-102, 154-157) are involved in either intersubunit or RNA-protein interactions.     

Expression inE. coli of the cloned cDNA for the major antigen of foot and mouth disease virus Asia 1 63/72

Double stranded cDNA for the foot and mouth disease virus was prepared, restricted withBamH 1 or ligated to linkers withBamH 1 sticky ends and cloned inBamH 1 site in the expression vector, pU R222. The cDNA was also cloned at thePst 1 site in the same vector by the dC/dG tailing method. They were transferred intoE. coli to give colourless colonies in the presence of the dye, X-gal. Many of them showed positive signal on hybridization with³²P-labelled viral RNA. The middleBamH1 fragment of the cDNA is known to carry the gene for the major antigen and some non-structural proteins. The clones carrying the recombinant DNA produced proteins which cross-reacted with the antibodies generated against the structural proteins of the virus in an enzyme linked immunosorbent assay, indicating that the cDNA of the major antigen is expressed in the cloned cell.