ABSTRACT
Vitiligo is a common skin disorder, characterized by depigmented patches due to selective destruction of melanocytes. The etiology of this disease is unknown. A number of hypotheses including viral theory have been proposed to explain the etiology. To determine the prevalence of antibody to hepatitis C virus infection in vitiligo patients, the present study was performed. Third generation ELISA test was used for detection of antibodies to HCV in human sera. All normal controls were anti-HCV negative whereas only one patient was positive for anti-HCV and there was no significant difference in the prevalence of anti-HCV between patients and controls. These results indicate that hepatitis C virus has not a direct causal role in the pathogenesis of vitiligo, however, this does not rul out a "hit and run" virus induced disease
Subject(s)
Humans , Male , Female , Vitiligo/etiology , Skin Diseases , Melanocytes , Enzyme-Linked Immunosorbent Assay , Serum , Viruses , AutoimmunityABSTRACT
Bakground: Granulocyte colony-stimulating factor [G-CSF] is a cytokine that stimulates hematopoiesis and induces proliferation and differentiation of granulocyte progenitor cells as well as production of bone marrow neutrophilic granulocyte colonies. Nowadays, human recombinant G-CSF[hr G-CSF] is used for the treatment of chemotherapy- and radiotherapy-induced neutropenia, and also in patients with bone marrow transplantation. A cDNA of human G-CSF [hG-CSF] was synthesized by PCR from recombinant cloning vector, with two altered nucleotides for increasing mRNA stability and overexpression, then inserted into a pET expression vector under the control of T7 promoter and cloned in E. coli strain BL21 [DE3]. After culture and induction of recombinant E. coli with IPTG, we achieved a high level expression of the hG-CSF, where it represented approximately 35% of the total protein as determined by SDS-PAGE and confirmed by western blotting with polyclonal and monoclonal hG-CSF antibodies. rhG-CSF was produced in a significantly high quantity with a yield of 35% of total protein as determined by SDS-PAGE. Since it is easily obtained by simple purification steps, it may be cost-effective, even on an industrial scale