| The s100 protein is a sort of neural protein. It is calcium combined protein which is include of s100αand s100β. s100αis constituted of an αchain and a βchain,and s100βis constituted of two βchain. The main function of s100 protein is to promote neuraxon extroverted growth and bringing into play the function of nerve growth gene or maintain livingness,while the nerve cell grew or damnificate. In the central neural system of manniferous,ascrocyte can excrete s100 protein,especially s100β. Creutzfeldt-Jakob disease (CJD) is a sort of prion protein disease. The main presentation of it is prompting dementia,and senior citizen suffer mainly. The state of CJD is developing very fast,and the putrescenceing of never cell and hypreplasia of glia is very serious. During the course,the values of s100βin cerebrospinal fluid(CSF) and serum will hoist.Alzheimer`s disease (AD) is a sort of denaturalized diseased of central neurous system, the main presentation of it is also dementia,and senior citizen suffer mainly. In clinic,it is difficult to distinguish CJD from AD. But,the prompting of AD is not so serious as CJD, and in pathology the hyperplasia of glia is not as distinct as CJD,then it is can be confered that the hoist s100βprotein in CSF and serum in AD is not as high as that of CJD. The study of the values of s100βprotein in CSF and serum will give some help to diagnose CJD in early stage,and distinguish CJD from AD. The pathogeny of prion disease is that the sequence of prion protein amino acid does not change,but the space configuration changees,and the pathological scrapie prion protein (PrPsc) is formed. One PrPsc can induce an PrP into a PrPsc, And the new PrPsc can induce another PrP into PrPsc with the original PrPsc. Then the rising course of PrPsc in index is formed. The PrP gene lie in the twentith chromosome small arm, and some point mutation and inserting mutation have relationship with prion protein disease,such as Gerstmann-Straussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI), and has affinity relationship with their clinic symptom, objective sign, the course of disease and pathlogy. Every variation of PrP stand a type of prion protein disease. . It is little report that if the s100 protein exist mutation or polymorphism and the relationship of it with CJD. For s100βgene can coding a βsub-unit of s100 protein, and s100βprotein is constituted of two βsub-unit withnot αsub-unit,so we can definitude the rule of CJD in gene level by determining the sequence of s100βgene. Material and Method 1.We select 13 cases of CJD,6 cases of AD and 18 case of central nervous system disease with no demensia , using Enzyme-Linked Immuno Sorbent Assay (ELISA) to detect the value of s100βin CSF and serum,so as to find a assistant way to dingnose the CJD and distinguish CJD from AD. 2.We adope the method of RNA polymerase chain reaction (RT-PCR), then detect the sequence of cDNA of 5 healthy control; and adopt the method of PCR to amplificate DNA, then detect the sequence of s100βgene coding section,and observe the mutation or polymormhism. Result The values of s100βprotein in CSF and serum of CJD were higher than those of AD (P<0.01). The values of s100βprotein in CSF and serum of CJD were higher that those of central nervous system disease with no demensia (P<0.01). After the detecting of DNA,no polymorphism or mutation is found. Conclusion 1.The increase of s100βprotein in CSF and serum can distinguish CJD from AD. Selected a proper intercept point, the sensitivity and the specificity are all 92.3% and 83.3%, and the the positive rediction rate and the negative rediction rate are all 92% and 83%..
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