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2015 ; 5
(ä): 18045
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Proteome Analysis of Renoprotection Mediated by a Novel Cyclic Helix B Peptide in
Acute Kidney Injury
#MMPMID26655840
Yang C
; Liu J
; Li L
; Hu M
; Long Y
; Liu X
; Zhu T
; Huang X
; Zhao S
; Liu S
; Rong R
Sci Rep
2015[Dec]; 5
(ä): 18045
PMID26655840
show ga
We developed a novel, erythropoietin-derived, non-erythropoiesis, cyclic helix B
peptide (CHBP) that displays potent renoprotection against acute kidney injury
(AKI). To determine the mechanism of CHBP-mediated protection, we investigated
the proteomic profile of mice treated with CHBP in a kidney ischemia-reperfusion
(IR) injury model. The isobaric tags for relative and absolute quantitation
(iTRAQ)-labeled samples were analyzed using a QSTAR XL LC/MS system. In total, 38
differentially expressed proteins (DEPs) were shared by all experimental groups,
while 3 DEPs were detected specifically in the IR?+?CHBP group. Eight significant
pathways were identified, and oxidative phosphorylation was shown to be the most
important pathway in CHBP-mediated renoprotection. The significant DEPs in the
oxidative phosphorylation pathway elicited by CHBP are NADH-ubiquinone
oxidoreductase Fe-S protein 6 (NDUFS6), alpha-aminoadipic semialdehyde synthase
(AASS) and ATP-binding cassette sub-family D member 3 (ABCD3). The DEPs mentioned
above were verified by RT-qPCR and immunostaining in mouse kidneys. We tested 6
DEPs in human biopsy samples from kidney transplant recipients. The trend of
differential expression was consistent with that in the murine model. In
conclusion, this study helps to elucidate the pharmacological mechanisms of CHBP
before clinical translation.
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