Candida albicans were isolated from patients with clinical symptoms of vaginal ulcer. Culture test for vaginal swab and scrapings were conducted on Sabouraud's dextrose broth and Sabouraud's dextrose agar plate respectively. Hichrome candida agar culture was used for differential identification of Candida. Smears from vaginal scrapings were prepared for gram staining. The suspected strain of Candida was inoculated on corn meal agar medium for chlamydospore formation. The suspected strain of Candida was inoculated in human serum for germ tube formation. Carbohydrate assimilation and fermentation tests were also conducted. The selected Candida colony was inoculated in YEPD medium for subculture and the cultured organism was harvested. The organisms were homogenized, centrifuged and the supernatant was filtered. The filtrate was extracted in chloroform. The extract was centrifuged and the aqueous phase was dialyzed. The dialyzed crude enolase was subjected to SDS-PAGE. The Sabouraud's dextrose broth inoculated with vaginal swab showed turbid growth. The scraping from vagina showed typical smooth creamy white colonies with a characteristic yeast odour on Sabouraud's dextrose agar plate. On Hichrome candida agar the Candida growth appeared as glistening green colored. Gram stained smears from vaginal scraps showed appearance of fungus as yeast January, 2010 85 budding. On corn meal agar the suspected Candida growth showed the formation of large, highly refractive, thick walled terminal chlamydospores. Germ tubes were seen as long tube like projections extending from the yeast cells on human serum inoculated with suspected strain of Candida. The carbohydrate assimilation tests were positive for dextrose, maltose, sucrose, galactose, xylose and trehalose, and negative for lactose, melibiose, ellobiose, inositol, reffinose and dulcitol. The carbohydrate fermentation tests showed positive for dextrose, maltose, galactose and trehalose, and negative for sucrose and lactose. SDS-PAGE for enolase from C. albicans showed a single polypeptide band of around 46 -48 kDa. International Journal of Biology
Cardiac remodeling is the process by which the heart adapts to stressful stimuli, such as hypertension and ischemia/reperfusion; it ultimately leads to heart failure upon longterm exposure. Autophagy, a cellular catabolic process that was originally considered as a mechanism of cell death in response to detrimental stimuli, is thought to be one of the main mechanisms that controls cardiac remodeling and induces heart failure. Dysregulation of the adipokines leptin and adiponectin, which plays essential roles in lipid and glucose metabolism, and in the pathophysiology of the neuroendocrine and cardiovascular systems, has been shown to affect the autophagic response in the heart and to contribute to accelerate cardiac remodeling. The obesity-associated protein leptin is a pro-inflammatory, tumor-promoting adipocytokine whose elevated levels in obesity are associated with acute cardiovascular events, and obesity-related hypertension. Adiponectin exerts anti-inflammatory and antitumor effects, and its reduced levels in obesity correlate with the pathogenesis of obesityassociated cardiovascular diseases. Leptin-and adiponectin-induced changes in autophagic flux have been linked to cardiac remodeling and heart failure. In this review, we describe the different molecular mechanisms of hyperleptinemia-and hypoadiponectinemia-mediated pathogenesis of cardiac remodeling and the involvement of autophagy in this process. A better understanding of the roles of leptin, adiponectin, and autophagy in cardiac functions and remodeling, and the exact signal transduction pathways by which they contribute to cardiac diseases may well lead to discovery of new therapeutic agents for the treatment of cardiovascular remodeling.
Post-translational modifications (PTMs) may affect functions of human serum albumin. Here we review reports of novel PTMs of human serum albumin. One hundred twenty-three recently reported novel O-phosphorylation, glycation, methylation, carbonylation, and acetylation of albumin are reviewed. Potential impact of these PTMs on albumin functions is discussed. Knowledge of these PTMs of albumin is of importance for use of albumin in medical applications, e.g., in transfusion, drug formulations and remedies.
Aim: Identify novel post-translational modifications in human serum albumin. Background: Serum albumin is the most abundant protein in plasma, has many physiological functions, and is in contact with most of the cells and tissues of the human body. Post-translational modifications (PTMs) may affect functions, stability, and localization of albumin. Objective: Identify novel PTMs in human serum albumin by mass spectrometry. Methods: Human serum albumin (HSA) was used for tryptic digestion in-solution or in-gel. Mass spectrometry was applied to identify PTMs in HSA. 3-dimensional modeling was applied to explore potential impact of PTMs on known functions of albumin. Results: Here we report the identification of 61 novel PTMs of human serum albumin. Phosphorylation, glycosylation, nitrosylation, deamidation, methylation, acetylation, palmitoylation, geranylation, and farnesylation are examples of the identified PTMs. Mass spectrometry was used for the identification of PTMs in a purified HSA and HSA from the human plasma. Three-dimensional modeling of albumin with selected PTMs showed the location of these PTMs in the regions involved in interactions of the albumin with drugs, metals, and fatty acids. The location of PTMs in these regions may modify the binding capacity of albumin. Conclusion: This report adds 61 novel PTMs to the catalog of human albumin.
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