The Hspa4l gene, also known as Apg1 or Osp94, belongs to the HSP110 heat shock gene family, which includes three genes encoding highly conserved proteins. This study shows that Hspa4l is expressed ubiquitously and predominantly in the testis. The protein is highly expressed in spermatogenic cells, from late pachytene spermatocytes to postmeiotic spermatids. In the kidney, the protein is restricted to cortical segments of distal tubules. To study the physiological role of this gene in vivo, we generated mice deficient in Hspa4l by gene targeting. Hspa4l-deficient mice were born at expected ratios and appeared healthy. However, approximately 42% of Hspa4l ؊/؊ male mice suffered from fertility defects. Whereas the seminiferous tubules of Hspa4ltestes contained all stages of germ cells, the number of mature sperm in the epididymis and sperm motility were drastically reduced. The reduction of the sperm count was due to the elimination of a significant number of developing germ cells via apoptosis. No defects in fertility were observed in female mutants. In addition, 12% of null mutant mice developed hydronephrosis. Concentrations of plasma and urine electrolytes in Hspa4lmice were similar to wild-type values, suggesting that the renal function was not impaired. However, Hspa4l؊/؊ animals were preferentially susceptible to osmotic stress. These results provide evidence that Hspa4l is required for normal spermatogenesis and suggest that Hspa4l plays a role in osmotolerance.Cells respond to protein-denaturing stress, such as heat, by rapidly inducing the expression of a wide array of heat shock genes. Heat shock proteins (HSPs) are a group of highly conserved proteins that are expressed constitutively and/or induced by different kinds of stress. HSPs participate in protein folding and assembly, elimination of misfolded proteins, and stabilization of newly synthesized proteins in various intercellular compartments (9). These proteins have been divided into families based on their structural similarities and apparent molecular weights (4).The HSP110/SSE gene family was shown to contain several distantly related genes, including two genes in Saccharomyces cerevisiae known as SSE1 and SSE2 (21, 25), the sea urchin sperm receptor gene (6), and several mammalian genes. The cellular functions of the HSP110/SSE gene family members are unclear. HSPs have been shown to prevent the aggregation of model substrates in vivo (7) and have been implicated in thermotolerance (23, 24). In S. cerevisiae, the loss of SSE1 results in a reduction of cell proliferation and temperature sensitivity, whereas the loss of SSE2 causes no overt phenotype (21). However, inactivation of both genes in some strain backgrounds is lethal (27).The mammalian HSP110 gene family consists of the genes for three proteins, namely, Hspa4l (also known as Apg1 or Osp94), Hspa4 (also known as Apg2), and Hsp110. Constitutive expression of Hspa4l is high in the testis and moderate in other tissues, while Hspa4 and Hsp110 are ubiquitously expressed in various tissues (1...
FAF1 was initially isolated as a Fas-associated factor and was subsequently found to interact with a subset of additional proteins that are involved in many cellular events including Fas-mediated apoptosis, heat shock signalling pathways and ubiquitin-dependent processes. Here, we describe that the 74-kDa FAF1 is ubiquitously expressed, while the expression of its post-translational-processed 49-kDa isoform is restricted to post-meiotic male germ cells. In ovary, FAF1 protein is localized predominantly in the cytoplasm of oocytes in all follicle stages. To determine the function of FAF1 in vivo, we analysed a mouse mutant line in which a gene trap vector was inserted in the Faf1 locus. The mutation disrupts the Faf1 and leads to lethality of the Faf1(GT/GT) embryos near the 2-cell stage. Analysis of FAF1 expression revealed that the protein is present in early preimplantation stages, while embryonic expression of Faf1 mRNA becomes appreciable at 4-cell stage. These results indicate that the death of Faf1(GT/GT) at the 2-cell stage may coincide with the depletion of maternal FAF1 in these embryos. Thus, our results indicate that the FAF1 gene product is necessary for early embryonic development.
Various types of toxic xenobiotic and electrophilic compounds, which were formed from the glutathione S-transferases cell metabolism and the oxidation stress, are the group enzymes with detoxification roles that are involved in the metabolism phase II. During the GSTM1 and GSTT1 gene homozygous deletion, the above enzymes completely lose their activity and consequently somatic mutation is formed. Furthermore, it is considered that it might have increased the risk of cancer. Therefore, the research works which connected the GSTMI and GSTTI gene deletion with the cancer of kidney, lung, prostate, breast, stomach, esophagus, large and narrow intestines. In this study, two gene deletion distribution is detected for cancer patients. We collected the blood samples of 60 patients who have been diagnosed with cancer. The DNA was extracted and the GSTM1 and GSTT1 genes were amplified using multiplex PCR. According to our research, the above two gene deletion is predominant among patients who have cancer. The results showed that from the total 60 patients GSTM1 and GSTT1 both deletions, GSTM1 gene deletion - 35%, GSTM1 gene deletion - 25%, GSTT1 gene deletion - 26.7%, GSTM1 and GSTT1 both positive -13.3 %. Therefore, we think that in order to prevent tumor and cancer, these gene mutations must be revealed and it is important to bring the risky group under medical control and assist them in order to prevent them from this disease.
Pasteurella multocida (P.multocida) a small gram-negative coccobacillus, is part of the normal oral flora of
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