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Biophysical Characterization Of The Membrane Binding Domain Of The Pro-Apoptotic Protein Bax, Pranav Garg
Biophysical Characterization Of The Membrane Binding Domain Of The Pro-Apoptotic Protein Bax, Pranav Garg
Electronic Theses and Dissertations
The BCL-2 family of proteins tightly regulates the delicate balance between life and death. The pore forming Bax is a pro-apoptotic member belonging to this protein family. At the onset of apoptosis, monomeric cytoplasmic Bax translocates to the outer mitochondrial membrane, forms oligomeric pores thereby letting mitochondrial cytochrome c enter the cytosol and initiate the apoptotic cascade. The C-terminal "helix 9" is thought to mediate the membrane binding of BAX. A 20-amino acid peptide corresponding to Bax C-terminus (VTIFVAGVLTASLTIWKKMG) and two mutants where the two lysines are replaced with Glu (charge reversal mutant, EE) or Leu (charge neutralization mutant, LL) …
The Sheddase Activity Of Adam10/Adam17 On Cxcl16 Increases Proliferation And Survival Of Colorectal Cancer Cells, Tamu C. Talton
The Sheddase Activity Of Adam10/Adam17 On Cxcl16 Increases Proliferation And Survival Of Colorectal Cancer Cells, Tamu C. Talton
Electronic Theses and Dissertations
CXCL16 is an interferon-inducible chemokine of the CXC-subfamily and functions as an adhesion molecule, when membrane bound, and a chemoattractant when soluble. Upregulation of cell associated CXCL16 (cCXCL16) in colorectal cancer is associated with increased tumor infiltrating lymphocytes and good prognosis. ADAM10 and ADAM17 are metalloproteinases responsible for cleaving CXCL16, releasing soluble CXCL16 (sCXCL16) and contributing to proliferation and migration of mesangial cells, in kidney inflammatory disease. We hypothesize that cCXCL16 is a substrate for ADAM10 and ADAM17 cleavage in colorectal cancer, releasing sCXCL16, which mediates cell proliferation. To this end, we first identified CXCL16 in the human colon carcinoma …