Honors Theses
Date of Award
2008
Document Type
Undergraduate Thesis
Department
Chemistry and Biochemistry
First Advisor
Ziaeddin Shariat-Madar
Relational Format
Dissertation/Thesis
Abstract
Prolylcarboxypeptidase (PRCP) is involved in the conversion of angiotensin II (Ang II, a potent vasoconstrictor) to angiotensin 1-7 and conversion of bradykinin (BK, a vasodilator) to form des Arg9 bradykinin. PRCP converts plasma prekallikrein (PK) to plasma kallikrein when the high molecular weight kininogen (HK) combines with PK, forming the HK-PK complex that binds to human umbilical vein endothelial cells (HUVEC) membranes. Formed kallikrein then liberates BK jfrom HK, which leads to vasodilation. This physiological function is mediated by the BK type 2 receptor in the G protein-coupled receptor family. The balance between BK production and Ang II inactivation is important for wound healing, angiogenesis and high blood pressure regulation. Our goal was to determine the post translational regulation of PRCP in Chinese hamster ovary (CHO) cells. CHO cells were transfected with full-length PRCP under the control of a cytomegalovirus (CMV) promoter and rPRCP was expressed as a fusion protein with C-terminal enhanced green fluorescent protein (EGFP). The binding of biotinylated HK to wild type CHO cells was time dependent, dose dependent. saturable and reversible. The PRCP-induced PK activation was similar on wild type and PRCP-transfected CHO cells. PRCP inhibitor, Z-Pro-Prolinal did not block PK activation on wild type or PRCP-transfected CHO cells. In addition, since PRCP-induced PK activation was similar on both wild type and PRCP-transfected CHO cells; there is a possibility of the existence of a novel enzymatic substance that activates the kallikreinkinin system (KKS).
Recommended Citation
Isani, Mubina Aziz, "The Expression and Characterization of Full-Length PRCP in Chinese Hamster Ovary Cells" (2008). Honors Theses. 2033.
https://egrove.olemiss.edu/hon_thesis/2033
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