Susceptibility of weakly ouabain-sensitive Na, K-ATPase isoform in ischemic and reperfused rat retinas

被引:4
|
作者
Kuboki, J [1 ]
Ishiguro, S [1 ]
Tamai, M [1 ]
机构
[1] Tohoku Univ, Sch Med, Dept Ophthalmol, Aoba Ku, Sendai, Miyagi 9808574, Japan
关键词
Na; K-ATPase; alpha isoform; ischemia; oxidative stress;
D O I
10.1620/tjem.187.353
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
It is possible that Na, K-ATPase may play some roles in ischemic damage of nervous tissue. To determine whether Na, K-ATPase is affected in ischemic and reperfused retina, we measured enzyme activities. Retinal ischemia was induced by clamping the optic nerve of female adult Sprague-Dawley (SD) rats for 90 minutes. At 0.5, 2 and 24 hours after reperfusion, rat eyes were enucleated, and the retinas were removed. In addition to unseparated, total ouabain-sensitive Na, K-ATPase activity, we measured weakly ouabain-sensitive (alpha) and highly ouabain-sensitive (alpha[+]) isoform activities separately by ATP hydrolysis. Total ouabain-sensitive Na, K-ATPase activity, alpha and alpha(+) isoform activities showed no significant difference from sham-operated contralateral eyes at 0.5 and 2 hours of reperfusion. After 24 hours of reperfusion, total ouabain-sensitive Na, K-ATPase activity decreased to 63% of the control. The activities of alpha and alpha(+) isoforms were 47% and 72%, respectively. The ratios of the alpha and alpha(+) isoform activities (alpha/alpha [+]) significantly decreased at 2 and 24 hours of reperfusion. Activity in a isoform decreased markedly in reperfused rat retinas. This response may be beneficial for reducting the oxidative stress in reperfused retinas.
引用
收藏
页码:353 / 361
页数:9
相关论文
共 50 条
  • [41] Sex differences in human lymphocyte Na,K-ATPase as studied by labeled ouabain binding
    Scarrone, S.
    Balestrino, M.
    Frassoni, F.
    Pozzi, S.
    Gandolfo, C.
    Podesta, M.
    Cupello, A.
    INTERNATIONAL JOURNAL OF NEUROSCIENCE, 2007, 117 (02) : 275 - 285
  • [42] Regulation of renal Na+,K+-ATPase and ouabain-sensitive H+,K+-ATPase by the cyclic AMP-protein kinase A signal transduction pathway
    Beltowski, J
    Marciniak, A
    Wójcicka, G
    Górny, D
    ACTA BIOCHIMICA POLONICA, 2003, 50 (01) : 103 - 114
  • [43] Isoform-specific up-regulation by ouabain of Na+,K+-ATPase in cultured rat astrocytes
    Hosoi, R
    Matsuda, T
    Asano, S
    Nakamura, H
    Hashimoto, H
    Takuma, K
    Baba, A
    JOURNAL OF NEUROCHEMISTRY, 1997, 69 (05) : 2189 - 2196
  • [44] NA,K-ATPASE AND THE DEVELOPMENT OF NA+ TRANSPORT IN RAT DISTAL COLON
    PACHA, J
    TEISINGER, J
    POPP, M
    CAPEK, K
    JOURNAL OF MEMBRANE BIOLOGY, 1991, 120 (03) : 201 - 210
  • [45] The α1 Na,K-ATPase gene is a susceptibility hypertension gene in the Dahl salt-sensitiveHSD rat
    Herrera, VLM
    Xie, HX
    Lopez, LV
    Schork, NJ
    Ruiz-Opazo, N
    JOURNAL OF CLINICAL INVESTIGATION, 1998, 102 (06) : 1102 - 1111
  • [46] Neuronal function and ALPHA3 isoform of the Na/K-ATPase
    Dobretsov, M
    Stimers, JR
    FRONTIERS IN BIOSCIENCE-LANDMARK, 2005, 10 : 2373 - 2396
  • [47] OUABAIN-SENSITIVE AND CA-2+-SENSITIVE ATPASE ACTIVITY OF CHIMERIC NA-PUMP AND CA-PUMP MOLECULES
    LUCKIE, DB
    BOYD, KL
    TAKEYASU, K
    FEBS LETTERS, 1991, 281 (1-2): : 231 - 234
  • [48] Apical ouabain-sensitive K+-activated-ATPase activity in colon and caecum of the chick
    Calonge, ML
    DelaHorra, C
    Cano, M
    SanchezAguayo, I
    Ilundain, AA
    PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 1997, 433 (03): : 330 - 335
  • [49] Oligodendrocytes in brain and optic nerve express the β3 subunit isoform of Na,K-ATPase
    Martín-Vasallo, P
    Wetzel, RK
    García-Segura, LM
    Molina-Holgado, E
    Arystarkhova, E
    Sweadner, KJ
    GLIA, 2000, 31 (03) : 206 - 218
  • [50] Isoform-Specific Na,K-ATPase Alterations Precede Disuse-Induced Atrophy of Rat Soleus Muscle
    Kravtsova, Violetta V.
    Matchkov, Vladimir V.
    Bouzinova, Elena V.
    Vasiliev, Alexander N.
    Razgovorova, Irina A.
    Heiny, Judith A.
    Krivoi, Igor I.
    BIOMED RESEARCH INTERNATIONAL, 2015, 2015