Blood and urine were collected for determination of biochemical parameters. Histological changes in the aorta and kidney were examined. At the end of the experiment, blood glucose, HbA1c and microalbumin showed at higher level. All of the high fat diet plus STZ injection rats exhibit remarkable lesions and plaque in their aorta representing damage to large blood vessels. However, they demonstrated features of different glomerulopathy. Rats suffered from hyperglycemia in whole studying time exhibit global glomerulosclerosis, hyaline arteriosclerosis and glomerular nodule which are comparable with characteristics observed in later stage of human nephropathy. The rest diabetic rats demonstrated features of mild nephropathy corresponding with a former stage of kidney disease.

The yeast Saccharomyces cerevisiae was used as a model eukaryotic organism to study the uptake of diamino acid derivatives of porphyrins and their phototoxicity with particular emphasis on possible mutagenic effects. The water-soluble hematoporphyrin derivatives diarginate (HpD[Arg]2) and 1-arginin di(N-amino acid)-protoporphyrinate used in this study are effective photosensitizers in tumor photodynamic therapy. Depending on the amino acid substituent, the porphyrin derivatives differ in their affinity for yeast cells. It is shown that HpD(Arg)2 and PP(Met)2 (Arg)2 penetrate into the yeast cell and are metabolized. Both compounds sensitize yeast cells to photodamage but have no mutagenic effect on nuclear or mitochondrial genomes.

Lung cancer (LC) is one of the leading causes of cancer deaths worldwide and approximately 3 million individuals die from this disease each year. Therefore, detecting LC at its early stages is very important to achieve decreased LC mortality. While gene expression profiling has been successfully used to classify various tumors and assess tumor stages, the gene-based prediction for LC is not yet entirely dependable. In serum, glycosylation is one of the most common post-translational modifications, and glycoproteins play a core role in a diversity of biological processes and pathogenesis. The development of an analytical approach for the study of variations of human serum glycoproteins has been limited by the structural heterogeneity of the post-translational modifications and the complexity of glycomics. Thus, in this report we present a strategy of using Concavanalin A (Con A) as an affinity agent combined with twodimensional electrophoresis (2-DE) and nanoLC ESI-MS/MS to enrich and characterize the N-linked glycoproteins that are the most common glycosylation motifs in serum. By comparison of serum samples between LC patients and the healthy, we found that 8 glycoproteins were significantly up regulated in LC serum and 3 glycoproteins were down regulated. The useful information related to LC was discovered while we investigated changes of glycosylation in LC serum. The results suggested that the combination of proteomic techniques could be used for mining protein biomarkers for LC.

Mutants of Saccharomyces cerevisiae accumulating uroporphyrin (UP) or protoporphyrin (PP) were used as a model for the in vivo phototoxic effect of porphyrins observed in the human skin photosensitivity associated with porphyrias (porphyria cutanea tarda and erythropoietic protoporphyria). We have found that UP is localized in vacuoles and PP is present in all compartments except vacuoles in yeast cells. Endogenous PP is much more effective as a photosensitizer of yeast cells than UP. Protoporphyrin action is strictly dependent on the presence of oxygen. In contrast, UP displays a phototoxic effect even if oxygen is not present in the suspension, implicating a free radical mechanism that operates in anaerobiosis upon photosensitization by UP. Catalase or superoxide dismutase deficiency affects photosensitization by UP. A possible mechanism of UP photosensitizing activity is discussed.

Serum is an exceptional and special proteome in many respects. It contains a lot of essential information for the study and disease diagnosis. However, the analysis of serum is analytically challenging due to the high dynamic concentration range of constituent protein species. Therefore, the fractionation of serum proteome is very necessary. In this study, a combination of different methods: depletion by Aurum Serum Protein MiniKit, thermostable fraction, affinity chromatography, was used to separate proteins from type 2 diabetes mellitus (T2DM) serum. The protein fractions were then digested by trypsin and analyzed by 2DnanoESI-LC-MS/MS. The proteins were named, classified and used to built database by using bioinformatics tools including ID mapping, Swiss-Prot.... It was shown that 468 glycoproteins, 1110 proteins in thermostable fraction, and totally 4044 proteins from 30 T2DM serum samples were identified. Moreover, 26 proteins were found positively associated with T2DM.