[Effect of low - level He - Ne laser irradiation on biomechanical property of wound healing process in healthy and streptozotocin induced diabetic rats]

The aim of present investigation was to determine the effects of low-level He-Ne laser therapy on biomechanical property of skin wound of healthy and streptozotocin induced diabetic [STZ-D] rats. The study was performed by experimental method. 36 male adult Wistar rats weighing above 250 gr. were used. Rats were divided equally into control and experimental groups, each group [n=18] were equally divided into 3 subgroups in order to radiate 3 different energy densities of laser. Weight of healthy and diabetic rats were recorded in the beginning and at the end of study. Blood glucose of rats in the beginning of study was recorded and rats with more than 120 mg/dl were excluded from study. Diabetes was induced by one time intra peritoneal injection of 55 mg/kg STZ. After one month, hyperglycemia was established in experimental group. Two 15-mm, vertical incision wounds were made on the dorsum of rats. Three groups of healthy and diabetic rats were received 22.4J/cm[2], 1.2J/cm[2] and 4J/cm[2] energy densities He-Ne laser for two weeks. At the end of study, rats were killed and skin sample were extracted and were submitted to a biomechanical evaluation [maximum force] examination. Data was analyzed by paired student t test methods. Mean value of blood glucose of diabetic rats was 518.37 +/- 23.3. Laser-treated healthy rats with 1.2J/cm[2] energy density showed significant increase of maximum force [p=0.05]. Laser-treated diabetic rats with 4J/cm[2] energy density showed significant increase of maximum force [p=0.05]. It seems ideal parameters for effectiveness of Low- Level He-Ne laser in healthy and diabetic rats are different. Wounds of diabetic rats should be radiated with more energy density of low- level laser for accelerating wound healing process in comparison with healthy rats

Recombinant SAG1 antigen to detect Toxoplasma gondii specific immunoglobulin G in human sera by ELISA test

Although some serological tests for the detection of Toxoplasma gondii-specific immunoglobulin are commercially available, better diagnostic tools are needed. The aim of present study was to evaluate the usefulness of the recombinant Toxoplasma gondii SAG1 antigen for the recognition of toxoplasmosis by ELISA. This study was conducted in Cellular and Molecular Biology Research Centers, Shahid Beheshti University, M.C., Tehran, Iran in 2008-2009. Surface antigen 1 [SAG1], a tachyzoite stage-specific protein, was subcloned into an expression vector and was subsequently transformed into BL21 [DE3] pLyss competent bacterial cells. After inducing expression of the recombinant antigen, the protein product was purified using Ni-affinity chromatography. The immunoreactivity of recombinant SAG1 [rSAG1] was analyzed by SDS-PAGE and western blotting. The reactivity of the rec-SAG1 protein was evaluated using an ELISA. Sensitivity and specificity of the generated recombinant-ELISA [rec-ELISA] compared to a commercially available ELISA [com-ELISA] were 88.4% and 88%, respectively. Recombinant SAG1 produced in E. coli is a promising antigen that can be used in diagnostic assays for the detection of specific antibodies against T. gondii

Subcloning and expression of recombinant Echinococcus granulosus antigen B, in Pqe-30 expression Vector

Echinococcosis or hydatid disease is a zoonotic infection caused by larval [metacestode] stages of cestodes belonging to the genus Echinococcus, family Taeniidae. We aimed to subclone antigen B gene in pQE-30 plasmid, its expression, and purification. We subcloned HI gene into pQE-30 expression vector. The recombinant vector was transformed into E. coli, M15 and mass cultured. The subcloned gene was expressed by IPTG. Subcloning of gene was confirmed by both PCR and enzyme digestion. Production of recombinant protein was confirmed by SDS-PAGE. Western blot analysis was carried out by both His-Tag monoclonal Ab and human serum to estimate the expressed potein in E. coli cells. Recombinant protein was purified and its specificity was proved by Western blotting. Production of this recombinant protein can increased sensitivity and specificity in serological test [ELISA]