Details

Autor(en) / Beteiligte

• Ackermann, M
• Kubitza, M
• Hauska, G
• Piña, A. L

Titel

vertebrate homologue of sulfide-quinone reductase in mammalian mitochondria

Ist Teil von

• Cell and tissue research, 2014-12, Vol.358 (3), p.779-792

Ort / Verlag

Berlin/Heidelberg: Springer-Verlag

Erscheinungsjahr

2014

Quelle

MEDLINE

Beschreibungen/Notizen

• Hydrogen sulfide (H₂S) is the first inorganic compound identified as both a substrate for mitochondrial oxidative phosphorylation and a transmitter in mammalian cells. H₂S seems to mediate effects that are correlated with those of nitric oxide (NO) by a reciprocal regulation. Moreover, H₂S is consumed by mitochondrial oxidation mediated by sulfide-quinone reductase-like protein (SQRDL)—the vertebrate homolog of sulfide-quinone oxidoreductase (SQR). There is evidence that SQR plays an essential role in regulating H₂S levels in fission yeast. To start understanding the role of SQRDL in the mammalian metabolism of H₂S, we examine rat tissues. Our results show that SQRDL protein is present in all tissues tested, albeit restricted to specific mitochondrial populations at the cellular level. We demonstrate a developmental regulation of Sqrdl transcription in the kidney, where SQRDL protein is detectable in glomerular podocytes and in tubular cells of the renal medulla. We also show that Sqrdl transcription in T cells is responsive to external H₂S. Taken together, our results suggest that Sqrdl transcription is adaptively regulated, probably to meet the need of H₂S oxidation. Thus far, SQRDL has only been studied in a limited set of tissues. The present report demonstrates the presence and specific localization of SQRDL in various mammalian tissues.