title: Modulation of sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase activity and oxidative modification during the development of adjuvant arthritis.
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 Ca(2+)-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 Ca(2+) level through conformational alterations of SERCA, and decreasing levels of calsequestrin in SR may also play regulatory role in SERCA activity and expression.
authors.affiliation: Institute of Experimental Pharmacology and Toxicology, Slovak Academy of Sciences, Bratislava, Slovakia.
authors.forename: Miriam K
authors.initials: MK
authors.lastname: Strosova
authors.forename: Janka
authors.initials: J
authors.lastname: Karlovska
authors.forename: Petronela
authors.initials: P
authors.lastname: Zizkova
authors.forename: Magdalena
authors.initials: M
authors.lastname: Kwolek-Mirek
authors.forename: Silvester
authors.initials: S
authors.lastname: Ponist
authors.forename: Corinne M
authors.initials: CM
authors.lastname: Spickett
authors.forename: Lubica
authors.initials: L
authors.lastname: Horakova
mesh_terms: D000818:Animals; D001169:Arthritis, Experimental / Q000209:etiology / Q000378:metabolism*; D002135:Calcium-Binding Proteins; D002155:Calsequestrin; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D008560:Membrane Fluidity; D018482:Muscle, Skeletal / Q000187:drug effects / Q000378:metabolism; D018384:Oxidative Stress; D010712:Phosphatidic Acids / Q000494:pharmacology; D050050:Protein Carbonylation; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D051381:Rats; D011917:Rats, Inbred Lew; D012519:Sarcoplasmic Reticulum / Q000378:metabolism; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases / Q000737:chemistry / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000737:chemistry
chemical_list: D002135:Calcium-Binding Proteins; D002155:Calsequestrin; D002352:Carrier Proteins; D010712:Phosphatidic Acids; D013438:Sulfhydryl Compounds; C057137:Casq1 protein, rat; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases