{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T19:02:55Z","timestamp":1780340575197,"version":"3.54.1"},"reference-count":38,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2021,2,25]],"date-time":"2021-02-25T00:00:00Z","timestamp":1614211200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Honor Scientist program grant","award":["2006-05106"],"award-info":[{"award-number":["2006-05106"]}]},{"name":"BioR&amp;D program grant","award":["M10642040001- 07N4204-00110"],"award-info":[{"award-number":["M10642040001- 07N4204-00110"]}]},{"name":"Korean National Research Foundation","award":["NRF-2015R1D1A1A01059571"],"award-info":[{"award-number":["NRF-2015R1D1A1A01059571"]}]},{"name":"Korean National Research Foundation","award":["NRF-2020R1A6C103B074"],"award-info":[{"award-number":["NRF-2020R1A6C103B074"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Prx V mRNA contains two in-frame AUG codons, producing a long (L-Prx V) and short form of Prx V (S-Prx V), and mouse L-Prx V is expressed as a precursor protein containing a 49-amino acid N-terminal mitochondria targeting sequence. Here, we show that the N-terminal 41-residue sequence of L-Prx V is cleaved by mitochondrial processing peptidase (MPP) in the mitochondrial matrix to produce an intermediate Prx V (I-Prx V) with a destabilizing phenylalanine at its N-terminus, and further, that the next 8-residue sequence is cleaved by mitochondrial intermediate peptidase (MIP) to convert I-Prx V to a stabilized mature form that is identical to S-Prx V. Further, we show that when mitochondrial H2O2 levels are increased in HeLa cells using rotenone, in several mouse tissues by deleting Prx III, and in the adrenal gland by deleting Srx or by exposing mice to immobilized stress, I-Prx V accumulates transiently and mature S-Prx V levels decrease in mitochondria over time. These findings support the view that MIP is inhibited by H2O2, resulting in the accumulation and subsequent degradation of I-Prx V, identifying a role for redox mediated regulation of Prx V proteolytic maturation and expression in mitochondria.<\/jats:p>","DOI":"10.3390\/antiox10030346","type":"journal-article","created":{"date-parts":[[2021,2,25]],"date-time":"2021-02-25T21:16:53Z","timestamp":1614287813000},"page":"346","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Maturation of Mitochondrially Targeted Prx V Involves a Second Cleavage by Mitochondrial Intermediate Peptidase That Is Sensitive to Inhibition by H2O2"],"prefix":"10.3390","volume":"10","author":[{"given":"Juhyun","family":"Sim","sequence":"first","affiliation":[{"name":"National Forensic Service, 10 Ipchun-ro, Wonju 26460, Korea"},{"name":"College of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul 120-750, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1846-2652","authenticated-orcid":false,"given":"Jiyoung","family":"Park","sequence":"additional","affiliation":[{"name":"College of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul 120-750, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyun Ae","family":"Woo","sequence":"additional","affiliation":[{"name":"College of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul 120-750, Korea"},{"name":"College of Pharmacy, Graduate School of Applied Science and Technology for Skin Health and Aesthetics, Ewha Womans University, Seoul 120-750, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sue Goo","family":"Rhee","sequence":"additional","affiliation":[{"name":"Yonsei Biomedical Research Institute, Yonsei University College of Medicine, Seoul 120-752, Korea"},{"name":"Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,2,25]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1089\/ars.2010.3393","article-title":"Multiple functions of peroxiredoxins: Peroxidases, sensors and regulators of the intracellular messenger H2O2, and protein chaperones","volume":"15","author":"Rhee","year":"2011","journal-title":"Antioxid. 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