| Helicobacter pylori (H. pylori) has been implicated as the major cause of gastrointestinal disorders such as chronic gastritis, peptic ulcer, carcinoma of stomach, mucosa associated lymphoid tissue lymphoma. In order to approach the pathogenesis and the pathophysiologic changes after H. pylori infection, many researchers have done numerous researches and found H. pylori itself contains HSP (heat shock protein, HSP) and possibly acts as a pathogen when H. pylori infection, furthermore, H. pylori infection also can stimulate the mucosal cells of stomach to produce different HSPs, and play a role of mucosal protection in H. pylori related gastric diseases.All the cells of organisms, including karyotic and eukaryotic cells will produce heat shock reaction under heat and many other injured factors, such as a-nemia, anoxemia, heavy metal ions i virus infection and DNA damage, then the stress will initiate a new kind of protein synthesizing gene heat shock protein gene to synthesize HSP. HSP is a kind of highly conservative protein , with its main function of protecting the proteins essential for cellular vitality can maintain the existences of cells. Generally, HSP forms complex with many kinds of proteins that have different functions in cell and participates in the folding of related proteins, the composition of subunit, intracellular transportation, the degradation of proteins and so on by the forming or disintegration of complexes, so as to regulate the activity and function of target proteins , but is not associated with the composition of target proteins, therefore , it is also considered as a kind of molecular chaperon Grp94 (glucose regulation protein) Grp78, PDI(protein disul-fide isomerase are important members of molecular chaperon family in endoplas-mic reticulum. In the early synthesizing stage of newly - produced peptide chains, with which Grp94 can form stable compounds to help it fold and assem-blage, besides,Grp94 can form complexes with protein s that havent assembled or are folded wrongly, meanwhile, it plays a role of presenting antigen in tumor cells.Grp78 and Bip (immunoglobulin binding protein) are the same substances which can be found in the cellular endoplasmic reticulu lumen of all kinds of mammals, under the circumstances of stress, they can combine with proteins, maintain the appropriate conformation, of the newly - synthesized protein molecules , prevent the unsuitable folding and accumulation of subunit before the formation of correct polymeric complex, can transport the abnormal proteins into degrading systems in endoplasmic reticulum to make them degraded, in order not to cause further damages to cells, in addition, they are able to reactivate the functions of certain enzymes , so as to maintain the function and living of cells. PDI, which acts as an enzyme to catalyze the formation of disulfide bond in protein molecular, is functioned as a molecular chaperon to be very important for the translation and the post - translation.However, at present, researches oh the relationship between Grp94, Grp78, PDI and H. pylori infection are rarely found, so we have studied the endoplasmic reticulum ultramicroscopic structural changes of the H. pylori infected and non - infected mucosal epithelial cells of stomach, and developed the examinations of the mRNA and protein levels of Grp94, Grp78, PDI in mucosa tissues of stomach to inquire their functions in H. pylori infection, The results were as follows:1. Apply transmission electron microscope to obsence 12 gastric mucosal specimens infected with H. pylori. Use Fast urease Test and Giemas stain to i-dentify whether it is infected with H. pylori or not. Tissue was obtained from gastric antrum sinus during endoscope, fixed by 2.5% gluta -raldelyde, and post-fixed by 1% osmic acid. Then it was. undergone dehydrationby gradient ethanol and acetone, embedding by Epon 812 resin, section and electron stain. Finally, it was observed under transmission electron microscope, Without H. pylroi infection , the microvilli of gastric mucos...
|
PDF Full Text Request