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Heat Shock Protein 40 ( Hsp 40 ) and Hsp 70 Protein Expression in Oral Squamous Cell Carcinoma ( OSCC )
| Content Provider | Semantic Scholar |
|---|---|
| Author | Prayitno, Adi Asnar, Elyana Astirin, Okid Parama Rosmala, Dinar Putra, Suhartono Taat |
| Copyright Year | 2013 |
| Abstract | Introduction: As a chaperone, heat shock protein acts as central integrators of protein homeostasis in cell. The form of these functions is to help setting up a complex protein molecular fold (folded protein) in many important settings, such as growth, differentiation, and the ability to live. It has become clear that the control system plays an important role if the folding process fails or an error occurs, causing folding abnormalities and targeted functionality to accumulate. The accumulation of faulty protein folding would harm cells and can result in death. Apparently, there is a correlation between protein folding error with various diseases, such as diabetes mellitus and cancer. Method: We examined protein levels in all samples using Dotblott with monoclonal antibody anti-Hsp40 and anti-Hsp70. Levels of the protein content was read using a densitometer. Modification of Dot Blot was as follows: treatment was conducted with 3 × SSC, added with 20 mL blocking solution, add with total protein samples of 10 mg/ml on nitrocellulose paper, prehybridized, incubated at 70 ̊ for 30 seconds, incubated at 70 ̊ for 30 seconds with primary antibody anti-Hsp40 or Hsp70 protein and then added with second antibody HRP anti-Hsp40 or Hsp70 protein, treated with 3 × SSC and visualized with TSA HRP, and then administered with streptavidin, biothynil tyramide, and, finally, added with chromogen (DAB) in a confined space. Result: From the analysis of the data using Manova test with Wilk’s Lambda, there were significant differences in the levels of Hsp40 between Benign Oral Lesion (mean 688.31 area) and OSCC (mean 1354.59 area) patients (p < 0.070), there was also a highly significant difference in Hsp70 levels between patients who experienced Benign Oral Lesion (mean 529.82 area) and OSCC (mean 1346.32 area) patients (p < 0.006). Conclusion: OSCC patients have increased Hsp70 levels, so it is possible that something is going wrong in protein folding. Errors in protein folding result in a new homeostasis or inhibition of apoptosis and increasing cell proliferation that triggers carcinogenesis. Hsp40 acts as co-chaperones. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://file.scirp.org/pdf/JCT_2013052311020976.pdf |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Apoptosis Blocking (computing) Carcinogenesis Carmoisine A Cell Proliferation Cessation of life Congenital Abnormality Control system DNAJB1 wt Allele Densitometer Device Component Diabetes Mellitus FITC-tyramide HSP72 Heat-Shock Proteins Heat shock proteins Heat-Shock Proteins 70 Heat-Shock Response Homeostasis Horseradish Peroxidase Kilogram per Cubic Meter Leukemia, B-Cell Molecular Chaperones Monoclonal Antibodies Patients Precipitating Factors SQL Server Compact Streptavidin Tree accumulation Western Blot incubated p-Dimethylaminoazobenzene protein expression protein folding |
| Content Type | Text |
| Resource Type | Article |
