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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
In Situ Regulation Of Cytosolic Phospolipase A₂, Beverly A. Rzigalinski
In Situ Regulation Of Cytosolic Phospolipase A₂, Beverly A. Rzigalinski
Theses and Dissertations in Biomedical Sciences
The 85 kDa cytosolic phospholipase A2 (cPLA2) is an agonist-responsive effector for intracellular signal transduction through the arachidonate cascade. In vitro studies have demonstrated that this enzyme is regulated by sub-micromolar calcium and is specific for arachidonate as the sn-2 fatty acyl group of phospholipid substrates. However, very little data is available regarding in situ mechanisms which govern the activity of cPLA2. The primarily objective of these studies was to develop an in situ system for the study of cPLA2, and investigate mobilization of arachidonate during signal transduction events.
Dimethylsulfoxide differentiation of the …
Role Of Heat Shock Protein 70 Kda Cognate In Limiting Thermal Inactivation And Refolding Of Heat-Denatured Nuclear Type I Topoisomerase, Kuo-Kuang Wen
Role Of Heat Shock Protein 70 Kda Cognate In Limiting Thermal Inactivation And Refolding Of Heat-Denatured Nuclear Type I Topoisomerase, Kuo-Kuang Wen
Theses and Dissertations in Biomedical Sciences
Previous studies (Ciavarra et al., 1994) demonstrated that the constitutive 70 kDa heat shock protein (hsc70) protected purified topoisomerase I from thermal injury. In addition, hsc70 was capable of regenerating catalytic activity of heat-denatured topoisomerase I. A whole cell lysate was also active in this reaction assay. The present study demonstrates that heat-denatured topoisomerase I is reactivated by a cytosolic fraction and that this activity is dependent on the presence of cytosolic hsc70. The efficacy of hsc70-mediated refolding of heat-denatured topoisomerase I is greatly enhanced by a cytosolic cofactor(s). In all these refolding reactions, exogenous ATP is not required. Size …
Translational Regulation Of The C-Jun Proto-Oncogene, Anil Sehgal
Translational Regulation Of The C-Jun Proto-Oncogene, Anil Sehgal
Theses and Dissertations in Biomedical Sciences
The v-jun oncogene was originally isolated from the ASV17 virus in 1987. Ever since its isolation, extensive work has been done to understand the role of the v-jun oncogene in cell transformation. The c-Jun protein is a transcription factor which binds to the DNA target TGACTCA. The c-Jun protein binds to DNA in the form of dimers. It can form homodimers with itself and heterodimers with Jun family (JunB and JunD), Fos family (FosB, Fra1 and Fra2), or with CREB family members through the leucine zipper motif. Because the c-jun proto-oncogene plays an important role in cell transformation, extensive work …