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2017 ; 2
(6
): e91738
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Retinol-binding protein 7 is an endothelium-specific PPAR? cofactor mediating an
antioxidant response through adiponectin
#MMPMID28352663
Hu C
; Keen HL
; Lu KT
; Liu X
; Wu J
; Davis DR
; Ibeawuchi SC
; Vogel S
; Quelle FW
; Sigmund CD
JCI Insight
2017[Mar]; 2
(6
): e91738
PMID28352663
show ga
Impaired PPAR? activity in endothelial cells causes oxidative stress and
endothelial dysfunction which causes a predisposition to hypertension, but the
identity of key PPAR? target genes that protect the endothelium remain unclear.
Retinol-binding protein 7 (RBP7) is a PPAR? target gene that is essentially
endothelium specific. Whereas RBP7-deficient mice exhibit normal endothelial
function at baseline, they exhibit severe endothelial dysfunction in response to
cardiovascular stressors, including high-fat diet and subpressor angiotensin II.
Endothelial dysfunction was not due to differences in weight gain, impaired
glucose homeostasis, or hepatosteatosis, but occurred through an oxidative
stress-dependent mechanism which can be rescued by scavengers of superoxide. RNA
sequencing revealed that RBP7 was required to mediate induction of a subset of
PPAR? target genes by rosiglitazone in the endothelium including adiponectin.
Adiponectin was selectively induced in the endothelium of control mice by
high-fat diet and rosiglitazone, whereas RBP7 deficiency abolished this
induction. Adiponectin inhibition caused endothelial dysfunction in control
vessels, whereas adiponectin treatment of RBP7-deficient vessels improved
endothelium-dependent relaxation and reduced oxidative stress. We conclude that
RBP7 is required to mediate the protective effects of PPAR? in the endothelium
through adiponectin, and RBP7 is an endothelium-specific PPAR? target and
regulator of PPAR? activity.