Modulation of sarcoplasmic/endoplasmic reticulum Ca2+-ATPase activity and oxidative modification during the development of adjuvant arthritis

M. K. Strosova, J. Karlovska, P. Zizkova, M. Kwolek-Mirek, S. Ponist, C. M. Spickett, L. Horakova

Research output: Contribution to journalArticle

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Abstract

Adjuvant arthritis (AA) was induced by intradermal administration of Mycobacterium butyricum to the tail of Lewis rats. In sarcoplasmic reticulum (SR) of skeletal muscles, we investigated the development of AA.

SR Ca2+-ATPase (SERCA) activity decreased on day 21, suggesting possible conformational changes in the transmembrane part of the enzyme, especially at the site of the calcium binding transmembrane part. These events were associated with an increased level of protein carbonyls, a decrease in cysteine SH groups, and alterations in SR membrane fluidity. There was no alteration in the nucleotide binding site at any time point of AA, as detected by a FITC fluorescence marker. Some changes observed on day 21 appeared to be reversible, as indicated by SERCA activity, cysteine SH groups, SR membrane fluidity, protein carbonyl content and fluorescence of an NCD-4 marker specific for the calcium binding site.

The reversibility may represent adaptive mechanisms of AA, induced by higher relative expression of SERCA, oxidation of cysteine, nitration of tyrosine and presence of acidic phospholipids such as phosphatidic acid. Nitric oxide may regulate cytoplasmic Ca2+ level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.
LanguageEnglish
Pages40-47
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume511
Issue number1-2
DOIs
Publication statusPublished - Jul 2011

Fingerprint

Experimental Arthritis
Calcium-Transporting ATPases
Sarcoplasmic Reticulum
Endoplasmic Reticulum
Cysteine
Fluidity
Modulation
Fluorescence
Calsequestrin
Binding Sites
Membrane Fluidity
Calcium
Nitration
Phosphatidic Acids
Fluorescein-5-isothiocyanate
Tyrosine
Muscle
Rats
Phospholipids
Nitric Oxide

Keywords

  • sarcoplasmic reticulum
  • nitric-oxide synthase
  • nitrotyrosine
  • free radicals
  • calsequestrin
  • adjuvant arthritis
  • SERCA
  • rheumatoid-arthritis
  • skeletal-muscle
  • oxidative modification
  • ATPASE
  • free-radicals
  • collagen-induced arthritis
  • adenosine-triphosphatase
  • s-glutathiolation
  • modulation
  • sarcoplasmic/endoplasmic
  • adjuvant arthritis

Cite this

Strosova, M. K. ; Karlovska, J. ; Zizkova, P. ; Kwolek-Mirek, M. ; Ponist, S. ; Spickett, C. M. ; Horakova, L. / Modulation of sarcoplasmic/endoplasmic reticulum Ca2+-ATPase activity and oxidative modification during the development of adjuvant arthritis. In: Archives of Biochemistry and Biophysics. 2011 ; Vol. 511, No. 1-2. pp. 40-47.
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abstract = "Adjuvant arthritis (AA) was induced by intradermal administration of Mycobacterium butyricum to the tail of Lewis rats. In sarcoplasmic reticulum (SR) of skeletal muscles, we investigated the development of AA. SR Ca2+-ATPase (SERCA) activity decreased on day 21, suggesting possible conformational changes in the transmembrane part of the enzyme, especially at the site of the calcium binding transmembrane part. These events were associated with an increased level of protein carbonyls, a decrease in cysteine SH groups, and alterations in SR membrane fluidity. There was no alteration in the nucleotide binding site at any time point of AA, as detected by a FITC fluorescence marker. Some changes observed on day 21 appeared to be reversible, as indicated by SERCA activity, cysteine SH groups, SR membrane fluidity, protein carbonyl content and fluorescence of an NCD-4 marker specific for the calcium binding site. The reversibility may represent adaptive mechanisms of AA, induced by higher relative expression of SERCA, oxidation of cysteine, nitration of tyrosine and presence of acidic phospholipids such as phosphatidic acid. Nitric oxide may regulate cytoplasmic Ca2+ level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.",
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Modulation of sarcoplasmic/endoplasmic reticulum Ca2+-ATPase activity and oxidative modification during the development of adjuvant arthritis. / Strosova, M. K.; Karlovska, J.; Zizkova, P.; Kwolek-Mirek, M.; Ponist, S.; Spickett, C. M.; Horakova, L.

In: Archives of Biochemistry and Biophysics, Vol. 511, No. 1-2, 07.2011, p. 40-47.

Research output: Contribution to journalArticle

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T1 - Modulation of sarcoplasmic/endoplasmic reticulum Ca2+-ATPase activity and oxidative modification during the development of adjuvant arthritis

AU - Strosova, M. K.

AU - Karlovska, J.

AU - Zizkova, P.

AU - Kwolek-Mirek, M.

AU - Ponist, S.

AU - Spickett, C. M.

AU - Horakova, L.

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N2 - Adjuvant arthritis (AA) was induced by intradermal administration of Mycobacterium butyricum to the tail of Lewis rats. In sarcoplasmic reticulum (SR) of skeletal muscles, we investigated the development of AA. SR Ca2+-ATPase (SERCA) activity decreased on day 21, suggesting possible conformational changes in the transmembrane part of the enzyme, especially at the site of the calcium binding transmembrane part. These events were associated with an increased level of protein carbonyls, a decrease in cysteine SH groups, and alterations in SR membrane fluidity. There was no alteration in the nucleotide binding site at any time point of AA, as detected by a FITC fluorescence marker. Some changes observed on day 21 appeared to be reversible, as indicated by SERCA activity, cysteine SH groups, SR membrane fluidity, protein carbonyl content and fluorescence of an NCD-4 marker specific for the calcium binding site. The reversibility may represent adaptive mechanisms of AA, induced by higher relative expression of SERCA, oxidation of cysteine, nitration of tyrosine and presence of acidic phospholipids such as phosphatidic acid. Nitric oxide may regulate cytoplasmic Ca2+ level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.

AB - Adjuvant arthritis (AA) was induced by intradermal administration of Mycobacterium butyricum to the tail of Lewis rats. In sarcoplasmic reticulum (SR) of skeletal muscles, we investigated the development of AA. SR Ca2+-ATPase (SERCA) activity decreased on day 21, suggesting possible conformational changes in the transmembrane part of the enzyme, especially at the site of the calcium binding transmembrane part. These events were associated with an increased level of protein carbonyls, a decrease in cysteine SH groups, and alterations in SR membrane fluidity. There was no alteration in the nucleotide binding site at any time point of AA, as detected by a FITC fluorescence marker. Some changes observed on day 21 appeared to be reversible, as indicated by SERCA activity, cysteine SH groups, SR membrane fluidity, protein carbonyl content and fluorescence of an NCD-4 marker specific for the calcium binding site. The reversibility may represent adaptive mechanisms of AA, induced by higher relative expression of SERCA, oxidation of cysteine, nitration of tyrosine and presence of acidic phospholipids such as phosphatidic acid. Nitric oxide may regulate cytoplasmic Ca2+ level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.

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