ArticleJournal of muscle research and cell motility2009
Regulation of fast skeletal muscle activity by SERCA1 vicinal-cysteines.
Article in Journal of muscle research and cell motility, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 7 citations in OpenAlex.
- Purification and characterization of ZmRIP1, a novel reductant-inhibited protein tyrosine phosphatase from maize.Plant physiology · 2012Article
- Altered calcium pump and secondary deficiency of gamma-sarcoglycan and microspan in sarcoplasmic reticulum membranes isolated from delta-sarcoglycan knockout mice.Cell calcium · 2010Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
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Abstract
During prolonged skeletal muscle contractions free radicals are produced that may lead to fatigue. Vicinal cysteines, known as a Vicinal-thiol groups react preferentially among them depending on redox potential. Therefore, we examined the role of VT groups on the activity and conformational changes of sarcoplasmic reticulum (SR) Ca(2+)-ATPase (SERCA1) from rabbit skeletal muscle isolated SR, by selective oxidation-reduction of VT-groups. After Ca(2+) is released from the SR to start contraction, SERCA1 pumps this cytosolic Ca(2+) back to the SR leading to muscle relaxation. Phenylarsine oxide (PAO) reacts selectively with VT-proteins forming dithioarsines, which are stable but exchanges rapidly with 2,3-dimercaptopropanol (BAL). When 0.1 mM PAO is added to isolated SR, 60 and 67% inhibition of SERCA1 hydrolytic and Ca(2+) uptake activities, respectively is observed. ATPase activity was fully reversible with 1 mM BAL. The SERCA1 thermal inactivation determined from isolated SR from muscle at rest showed a single transition for inactivation (T(i)) at 49 +/- 1.12 degrees C. In the presence of 0.1 mM PAO, SERCA1 shows two transitions at T(i) 34 +/-0.9 degrees C and at 27 +/-1.2 degrees C. The thermal denaturation profile of SERCA1 from muscle at rest, showed two transitions at T(m) = 51.5 +/-1.3 degrees C and 63 +/-1.02 degrees C related to nucleotide and Ca(2+) binding domains, respectively. Whereas isolated SR obtained after a protocol of tetanic stimulation to produce muscle fatigue, showed three transitions in the SERCA1 denaturation profile similar to the effect of PAO, addition of 1 mM BAL reverted the effect of fatigue on SERCA1 denaturation profile. These results indicate a mechanism relating VT group's oxidation to muscle fatigue.
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