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2014 ; 289
(25
): 17732-46
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Annexin A2 reduces PCSK9 protein levels via a translational mechanism and
interacts with the M1 and M2 domains of PCSK9
#MMPMID24808179
Ly K
; Saavedra YG
; Canuel M
; Routhier S
; Desjardins R
; Hamelin J
; Mayne J
; Lazure C
; Seidah NG
; Day R
J Biol Chem
2014[Jun]; 289
(25
): 17732-46
PMID24808179
show ga
Annexin A2 (AnxA2) was reported to be an extracellular endogenous inhibitor of
proprotein convertase subtilisin kexin type 9 (PCSK9) activity on cell-surface
LDL receptor degradation. In this study, we investigated the effect of silencing
the expression of AnxA2 and PCSK9 in HepG2 and Huh7 cells to better define the
role of AnxA2 in PCSK9 regulation. AnxA2 knockdown in Huh7 cells significantly
increased PCSK9 protein levels as opposed to AnxA2 knockdown in HepG2 cells.
However, HepG2 cells overexpressing AnxA2 had lower levels of PCSK9 protein.
Overall, our data revealed a plausible new role of AnxA2 in the reduction of
PCSK9 protein levels via a translational mechanism. Moreover, the C-terminal
Cys/His-rich domain of PCSK9 is crucial in the regulation of PCSK9 activity, and
we demonstrated by far-Western blot assay that the M1 and M2 domains are
necessary for the specific interaction of PCSK9's C-terminal Cys/His-rich domain
and AnxA2. Finally, we produced and purified recombinant PCSK9 from humans and
mice, which was characterized and used to perform
1,1'-dioctadecyl-3,3,3',3'-tetramethylindocarbocyanine perchlorate LDL cell-based
assays on the stable knockdown HepG2 and Huh7 cells. We also demonstrated for the
first time the equipotency of human and mouse PCSK9 R218S on human cells.
free
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