Mechanism of serca modulation from rats with adjuvant arthritis

M. Strosova, J. Karlovska, C.M. Spickett, L. Horakova

Research output: Contribution to conferenceAbstract

Abstract

We studied the structural and functional alterations of SERCA in rats suffering from adjuvant arthritis (AA). AA was induced by intradermal administration of Mycobacterium butyricum (MB) to the base of the tail of Lewis rats. Injury of SERCA from skeletal muscles of AA rats was analyzed on days 7, 14, 21 and 28 after MB injection. Neither fragmentation, aggregation of SERCA protein, alterations in SH groups, nor oxidation of phosphatidylcholines and phosphatidylethanolamines in SR vesicles were observed in animals with AA. The only ROS/RNS modification was increased formation of nitrotyrosine. The
activity of SERCA from AA animals decreased on day 21 after MB injection and was associated with a significant increase of protein carbonyls in sarcoplasmic reticulum (SR). In contrast, on day 28 an increase of SERCA activity was observed and protein carbonyl level reversed to control level. Concerning kinetic parameters, maximum reaction velocity (Vmax) decrease and increase was observed with respect to both substrates (Ca, ATP) on days 21 and 28, respectively, suggesting possible conformational changes of the enzyme. These changes were not associated with alterations in nucleotide binding site situated in cytosol, but rather with tryptophan fluorescence intensity ratio (cytosol/membrane) related to the transmembrane domain of SERCA. Elevated SERCA activity on day 28 was caused by its higher expression. Acidic phospholipids (PA), probably present in SR of AA rats, may contribute to the elevation of Ca-ATPase activity, as PA administration in vitro increased this activity.
LanguageEnglish
Publication statusPublished - 2009
EventSFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention - Roma, Italy
Duration: 27 Sep 2009 → …

Conference

ConferenceSFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention
CountryItaly
CityRoma
Period27/09/09 → …

Fingerprint

Experimental Arthritis
Sarcoplasmic Reticulum
Mycobacterium
Cytosol
Lewis Bases
Phosphatidylethanolamines
Injections
Proteins
Phosphatidylcholines
Tryptophan
Adenosine Triphosphatases
Tail
Phospholipids
Skeletal Muscle
Nucleotides
Adenosine Triphosphate
Fluorescence
Binding Sites
Membranes
Wounds and Injuries

Bibliographical note

Abstract published online in Abstracts, Free Radical Research, 43(s1) p.S40.

Keywords

  • mechanism of serca modulation
  • rats
  • adjuvant arthritis
  • chemistry

Cite this

Strosova, M., Karlovska, J., Spickett, C. M., & Horakova, L. (2009). Mechanism of serca modulation from rats with adjuvant arthritis. Abstract from SFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention, Roma, Italy.
Strosova, M. ; Karlovska, J. ; Spickett, C.M. ; Horakova, L. / Mechanism of serca modulation from rats with adjuvant arthritis. Abstract from SFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention, Roma, Italy.
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Strosova, M, Karlovska, J, Spickett, CM & Horakova, L 2009, 'Mechanism of serca modulation from rats with adjuvant arthritis' SFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention, Roma, Italy, 27/09/09, .

Mechanism of serca modulation from rats with adjuvant arthritis. / Strosova, M.; Karlovska, J.; Spickett, C.M.; Horakova, L.

2009. Abstract from SFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention, Roma, Italy.

Research output: Contribution to conferenceAbstract

TY - CONF

T1 - Mechanism of serca modulation from rats with adjuvant arthritis

AU - Strosova, M.

AU - Karlovska, J.

AU - Spickett, C.M.

AU - Horakova, L.

N1 - Abstract published online in Abstracts, Free Radical Research, 43(s1) p.S40.

PY - 2009

Y1 - 2009

N2 - We studied the structural and functional alterations of SERCA in rats suffering from adjuvant arthritis (AA). AA was induced by intradermal administration of Mycobacterium butyricum (MB) to the base of the tail of Lewis rats. Injury of SERCA from skeletal muscles of AA rats was analyzed on days 7, 14, 21 and 28 after MB injection. Neither fragmentation, aggregation of SERCA protein, alterations in SH groups, nor oxidation of phosphatidylcholines and phosphatidylethanolamines in SR vesicles were observed in animals with AA. The only ROS/RNS modification was increased formation of nitrotyrosine. Theactivity of SERCA from AA animals decreased on day 21 after MB injection and was associated with a significant increase of protein carbonyls in sarcoplasmic reticulum (SR). In contrast, on day 28 an increase of SERCA activity was observed and protein carbonyl level reversed to control level. Concerning kinetic parameters, maximum reaction velocity (Vmax) decrease and increase was observed with respect to both substrates (Ca, ATP) on days 21 and 28, respectively, suggesting possible conformational changes of the enzyme. These changes were not associated with alterations in nucleotide binding site situated in cytosol, but rather with tryptophan fluorescence intensity ratio (cytosol/membrane) related to the transmembrane domain of SERCA. Elevated SERCA activity on day 28 was caused by its higher expression. Acidic phospholipids (PA), probably present in SR of AA rats, may contribute to the elevation of Ca-ATPase activity, as PA administration in vitro increased this activity.

AB - We studied the structural and functional alterations of SERCA in rats suffering from adjuvant arthritis (AA). AA was induced by intradermal administration of Mycobacterium butyricum (MB) to the base of the tail of Lewis rats. Injury of SERCA from skeletal muscles of AA rats was analyzed on days 7, 14, 21 and 28 after MB injection. Neither fragmentation, aggregation of SERCA protein, alterations in SH groups, nor oxidation of phosphatidylcholines and phosphatidylethanolamines in SR vesicles were observed in animals with AA. The only ROS/RNS modification was increased formation of nitrotyrosine. Theactivity of SERCA from AA animals decreased on day 21 after MB injection and was associated with a significant increase of protein carbonyls in sarcoplasmic reticulum (SR). In contrast, on day 28 an increase of SERCA activity was observed and protein carbonyl level reversed to control level. Concerning kinetic parameters, maximum reaction velocity (Vmax) decrease and increase was observed with respect to both substrates (Ca, ATP) on days 21 and 28, respectively, suggesting possible conformational changes of the enzyme. These changes were not associated with alterations in nucleotide binding site situated in cytosol, but rather with tryptophan fluorescence intensity ratio (cytosol/membrane) related to the transmembrane domain of SERCA. Elevated SERCA activity on day 28 was caused by its higher expression. Acidic phospholipids (PA), probably present in SR of AA rats, may contribute to the elevation of Ca-ATPase activity, as PA administration in vitro increased this activity.

KW - mechanism of serca modulation

KW - rats

KW - adjuvant arthritis

KW - chemistry

M3 - Abstract

ER -

Strosova M, Karlovska J, Spickett CM, Horakova L. Mechanism of serca modulation from rats with adjuvant arthritis. 2009. Abstract from SFRR Europe Meeting 2009 Free radicals, Health and Lifestyle: from cell signalling to disease prevention, Roma, Italy.