TAILIEUCHUNG - Báo cáo khoa học: Affinity and kinetics of proprotein convertase subtilisin ⁄ kexin type 9 binding to low-density lipoprotein receptors on HepG2 cells

Proprotein convertase subtilisin⁄kexin type 9 (PCSK9) is a secreted protein that regulates the number of cell surface low-density lipoprotein receptors (LDLRs) and the levels of low-density lipoprotein cholesterol in plasma. | IFEBS Journal Affinity and kinetics of proprotein convertase subtilisin kexin type 9 binding to low-density lipoprotein receptors on HepG2 cells Seyed A. Mousavi1 Knut E. Berge1 Trond Berg2 and Trond P. Leren1 1 Unit for Cardiac and Cardiovascular Genetics Department of MedicalGenetics Oslo University HospitalRikshospitalet Norway 2 Department of Molecular Biosciences University of Oslo Norway Keywords association dissociation dissociation constants low-density lipoprotein receptor proprotein convertase subtilisin kexin 9 Correspondence T. P. Leren Unit for Cardiac and Cardiovascular Genetics Department of MedicalGenetics Oslo University Hospital Rikshospitalet . Box 4950 Nydalen NO-0424 Oslo Norway Fax 47 23075561 Tel 47 23075552 E-mail Received 29 March 2011 revised 7 June 2011 accepted 16 June 2011 doi Proprotein convertase subtilisin type 9 PCSK9 is a secreted protein that regulates the number of cell surface low-density lipoprotein receptors LDLRs and the levels of low-density lipoprotein cholesterol in plasma. Intact cells have not previously been used to determine the characteristics of binding of PCSK9 to LDLR. Using PCSK9 iodinated by the tyramine cellobiose TC method 125I TC-PCSK9 we measured the affinity and kinetics of binding of PCSK9 to LDLR on HepG2 cells at 4 C. The extent of 125I TC-PCSK9 binding increased as cell surface LDLR density increased. Unlabeled wild-type and two gain-of-function mutants of PCSK9 reduced binding of 125I TC-PCSK9. The Scatchard plot of the binding-inhibition curve was curvilinear indicative of high-affinity and low-affinity sites for PCSK9 binding on HepG2 cells. Nonlinear regression analysis of the binding data also indicated that a two-site model better fitted the data. The time course of 125I TC-PCSK9 binding showed two phases in the association kinetics. Dissociation of 125I TC-PCSK9 also occurred in two phases. Unlabeled PCSK9 accelerated the .

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