Site-1 protease is required for the generation of soluble (pro)renin receptor

被引：80

作者：

Nakagawa, Tsutomu ^{[1
]}

Suzuki-Nakagawa, Chiharu ^{[1
]}

Watanabe, Akiko ^{[2
]}

Asami, Eriko ^{[2
]}

Matsumoto, Mizuki ^{[1
]}

Nakano, Mami ^{[1
]}

Ebihara, Akio ^{[1
]}

Uddin, Mohammad Nasir ^{[3
,4
]}

Suzuki, Fumiaki ^{[1
]}

机构：

[1] Gifu Univ, Fac Appl Biol Sci, Dept Appl Life Sci, 1-1 Yanagido, Gifu 5011193, Japan

[2] Gifu Univ, Grad Sch Appl Biol Sci, Dept Appl Life Sci, 1-1 Yanagido, Gifu 5011193, Japan

[3] Scott & White Healthcare, Dept Obstet & Gynecol, Temple, TX 76508 USA

[4] Texas A&M Hlth Sci Ctr, Coll Med, Temple, TX 76508 USA

来源：

JOURNAL OF BIOCHEMISTRY | 2017年 / 161卷 / 04期

关键词：

ATP6AP2; furin; site-1; protease; SKI-1; soluble (pro)renin receptor; PRO RENIN RECEPTOR; TRANS-GOLGI NETWORK; KEX2-LIKE PROCESSING ENDOPROTEASE; BZIP TRANSCRIPTION FACTOR; PROPROTEIN CONVERTASE; BREFELDIN-A; PRORENIN RECEPTOR; CELL-SURFACE; CYTOPLASMIC DOMAIN; CLEAVAGE;

D O I：

10.1093/jb/mvw080

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The extracellular domain of the (pro)renin receptor [(P)RR] is cleaved to generate the soluble form of (P)RR [s(P)RR]. Multiple clinical studies have revealed the association between serum/plasma s(P)RR levels and certain diseases, thereby suggesting a potential role for s(P)RR as a disease biomarker. Here, we investigated whether site-1 protease (S1P) is responsible for cleaving (P)RR to generate s(P)RR. Reduction of endogenous S1P with siRNA attenuated s(P)RR generation in Chinese hamster ovary (CHO) cells exogenously expressing human (P)RR with a C-terminal decahistidine tag [CHO/h(P)RR-10His cells]; conversely, overexpression of S1P by transient transfection increased s(P)RR generation. The S1P inhibitor PF429242 suppressed s(P)RR generation in CHO/h(P)RR-10His and human cervical carcinoma HeLa cells; however, the ADAM inhibitor GM6001 had no effect. The furin inhibitor Dec-RVKR-CMK had no effect on the amount of s(P)RR, but caused a slight increase in the size of the s(P)RR. Moreover, the reversible vesicle-trafficking inhibitor brefeldin A (BFA) enhanced the generation of large-sized s(P)RR; PF429242, but not Dec-RVKR-CMK, suppressed this BFA-induced s(P)RR formation. The size of s(P)RR generated during BFA treatment was reduced after removal of BFA; Dec-RVKR-CMK, but not PF429242, suppressed this conversion. Together, these results suggest that s(P)RR is generated by sequential processing by S1P and furin.

引用

页码：369 / 379

页数：11

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