onr:"swepub:oai:DiVA.org:gih-6581"
Search: onr:"swepub:oai:DiVA.org:gih-6581" > Role of nitration i...
- 1 of 1
- Previous record
- Next record
- To hitlist
Role of nitration in control of phosphorylase and glycogenolysis in mouse skeletal muscle.
-
- Blackwood, Sarah J (author)
- Karolinska Institutet,Gymnastik- och idrottshögskolan,Institutionen för fysiologi, nutrition och biomekanik
-
- Jude, Baptiste (author)
- Karolinska Institutet, Sweden.
-
- Mader, Theresa (author)
- Karolinska Institutet
- show more...
- show less...
- (creator_code:org_t)
- American Physiological Society, 2021
- 2021
- English.
- In: American Journal of Physiology. Endocrinology and Metabolism. - : American Physiological Society. - 0193-1849 .- 1522-1555. ; 320:4, s. E691-E701
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- Phosphorylase is one of the most carefully studied proteins in history, but knowledge of its regulation during intense muscle contraction is incomplete. Tyrosine nitration of purified preparations of skeletal muscle phosphorylase results in inactivation of the enzyme and this is prevented by antioxidants. Whether an altered redox state affects phosphorylase activity and glycogenolysis in contracting muscle is not known. Here, we investigate the role of redox state in control of phosphorylase and glycogenolysis in isolated mouse fast-twitch (extensor digitorum longus, EDL) and slow-twitch (soleus) muscle preparations during repeated contractions. Exposure of crude muscle extracts to H2O2 had little effect on phosphorylase activity. However, exposure of extracts to peroxynitrite (ONOO-), a nitrating/oxidizing agent, resulted in complete inactivation of phosphorylase (half maximal inhibition at ~200 µM ONOO-), which was fully reversed by the presence of an ONOO-scavanger, dithiothreitol (DTT). Incubation of isolated muscles with ONOO- resulted in nitration of phosphorylase and marked inhibition of glycogenolysis during repeated contractions. ONOO- also resulted in large decreases in high-energy phosphates (ATP and phosphocreatine) in the rested state and following repeated contractions. These metabolic changes were associated with decreased force production during repeated contractions (to ~60% of control). In contrast, repeated contractions did not result in nitration of phosphorylase, nor did DTT or the general antioxidant N-acetylcysteine alter glycogenolysis during repeated contractions. These findings demonstrate that ONOO- inhibits phosphorylase and glycogenolysis in living muscle under extreme conditions. However, nitration does not play a significant role in control of phosphorylase and glycogenolysis during repeated contractions.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Fysiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Physiology (hsv//eng)
Keyword
- antioxidants
- contraction
- glycogen
- phosphorylase
- skeletal muscle
- Medicin/Teknik
- Medicine/Technology
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
- American Journal of Physiology. Endocrinology and Metabolism (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Blackwood, Sarah ...
- Jude, Baptiste
- Mader, Theresa
- Lanner, Johanna ...
- Katz, Abram
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
- MEDICAL AND HEAL ...
- and Basic Medicine
- and Physiology
- Articles in the publication
- American Journal ...
- By the university
- The Swedish School of Sport and Health Sciences
- Karolinska Institutet
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
