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1.
Iranian Journal of Cancer Prevention. 2015; 8 (1): 69-70
en Inglés | IMEMR | ID: emr-159993
2.
Journal of Paramedical Sciences. 2014; 5 (1): 81-91
en Inglés | IMEMR | ID: emr-188309

RESUMEN

Human serum albumin [HSA] is the most abundant protein constituent of blood plasma. This protein consists of a single polypeptide chain of 585 amino acid residues, which has many important physiological functions. HSA can bind and carry many drugs, including anticoagulants, tranquilizers, and general Anesthetics. Some technique such as: fluorescence spectroscopy, three-dimensional fluorescence, UV-visible, FT-IR, circular dichroism [CD], X-ray scattering [SAXS] technique and molecular modeling was utilized to investigate the effects of acceptor on conformation of the donor [HSA]. The binding site number n and apparent binding constant K[A] drugs corresponding thermodynamic parameters, the free energy change [DELTA G], enthalpy change [DELTA H], and entropy change [DELTA S] were calculated. The hydrophobic effect, van der Waals forces, hydrogen bond and electrostatic interactions play a major role in stabilizing the complex. More investigation also revealed that these drugs bind to the amino acids on the hydrophobic pocket of HSA and induce changes to the secondary structure of the HSA. In this study for better understanding of HSA-drug interactions, we categorized drugs into ten groups from years 2006 to 2012 and are suggested that two important parameters such as Delta G[0][H20] and [D] [½] can be calculated for each groups and refer to ten categories to finally indicate that fine structural change in human serum albumin

3.
IJPR-Iranian Journal of Pharmaceutical Research. 2013; 12 (1): 185-191
en Inglés | IMEMR | ID: emr-193156

RESUMEN

Human serum albumin has been used as a model protein for protein folding and ligand binding studies over many decades. Due to its long life period and high concentration in plasma, HSA is highly sensitive to glycation. It is reported that 175 mg/dL glucose concentration is a threshold of kidney activity for the beginning of excretion of glucose. PH denaturation of HSA in absence and presence of different concentrations of glucose is studied and based on the Pace two-state model, the findings are analyzed. In addition, florescence emission data of albumin range in the period of 300-500 nm was depicted. The amounts of free energy change and [D] [1/2] parameters of unfolding in correspond to florescence date indicate that glucose induces fine structural change in human serum albumin. Results showed that 175 mg/dL glucose concentration is a critical point for albumin structural and functional alteration

4.
Journal of Paramedical Sciences. 2013; 4 (Supp.): 72-77
en Inglés | IMEMR | ID: emr-194192

RESUMEN

Nutritional status during adolescence plays an important role in human lifecycle. The aim of this study was Nutritional status and dietary intake among adolescent girls. In a cross sectional study, using two stage cluster sampling 256 adolescent girls were randomly selected from 8 Semnan secondary schools. Weight and height were measured and body mass index [BMI] was calculated. In adolescents, anthropometric indices were defined based on the CDC 2000 cut-off points for age and gender-specific BMI. Data of energy and nutrient intake was collected with the 24-hour dietary recall and food record questionnaires. The results showed that the prevalence of underweight, normal weight, overweight, and obese was 5.7%, 77.7%, 11.7%, and 4.7% in Semnan adolescent girls, respectively. In comparison with DRI recommended values, the intake of energy and some micronutrients such as vitamin B12, folate, calcium, zinc, and fiber was insufficient among adolescent girls in Semnan. Malnutrition [underweight and overweight] is higher than the expected rate. Findings of our study showed that micronutrients deficiency among adolescent girls is a major problem among adolescent girls in Semnan and prevention measures are necessary to induct

5.
Journal of Paramedical Sciences. 2010; 1 (1): 9-15
en Inglés | IMEMR | ID: emr-198000

RESUMEN

One of the prominent types of connective tissue cells is fibroblast that synthesizes and maintains the extracellular matrix of many animal tissues. Previous studies illustrated that calprotectin protein has different cytotoxicity effects on fibroblast cells. Calprotectin is abundant in the mneutrophil cytosol; it has growth-inhibitory and apoptosis-inducing activities against various mcell types such mas tumor cells. The present study tries to introduce mechanism of growth inhibitory effect of calprotectin on human foreskin fibroblast cells [HFFF] and compare to etoposide [chemotherapy agent as control]. Calprotectin was purified from human neutrophil by chromatography methods. HFFF cell lines were used, maintained in RPMI 1640 medium supplemented with 10% FCS in a humidified incubator [37 degreeC and 5% CO2]. The HFFF cells were exposed to the different concentrations of calprotectin and etoposide for 24, 48 and 72 hours. Cell proliferation was assessed by using dimethylthiazol diphenyl tetrazolium bromide assay. Flow cytometric analysis was performed to evaluate the cytotoxic mechanism of calprotectin on HFFF cells. Our results revealed that calprotectin and etoposide induce growth inhibition of HFFF in dose- and time-dependent manners. Sensitivity of HFFF cells to cytotoxic effect of human calprotectin was highly remarkable. In addition, growth inhibitory effect of this cytotoxic agent mostly was governed through induction of apoptosis in the HFFF cells. Taken together, calprotectin not only has more potent anticancer activity in comparison with the etoposide, but it also is an apoptosis inducer that acts on the proliferation of normal cells like fibroblasts

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