Increase of urinary extracellular-superoxide dismutase level correlated with cyclic adenosine monophosphate

被引:10
|
作者
Adachi, T
Yamada, H
Hara, H
Futenma, A
Kakumu, S
机构
[1] Gifu Pharmaceut Univ, Lab Clin Pharmaceut, Gifu 502, Japan
[2] Aichi Med Univ, Dept Internal Med 1, Nagakute, Aichi 48011, Japan
关键词
extracellular superoxide dismutase; cAMP; N-acetyl-beta-D-glucosaminidase; parathyroid hormone; renal tubule;
D O I
10.1016/S0014-5793(99)01185-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Extracellular superoxide dismutase (EC-SOD) is a secretory protein that is the major SOD isozyme in extracellular fluids. Plasma EC-SOD levels are distributed in two discrete groups vr with the rare group haring an enzyme with glycine instead of arginine-213, which causes a 10-fold higher serum level, Within the common phenotype group, the urinary EC-SOD level was significantly correlated with the urinary excretion of N-acetyl-beta-D-glucosaminidase (NAG), but not with serum EC-SOD, EC-SOD appears not to be leaked from the plasma by glomerular filtration, but rather to be secreted from the renal tubule or its surrounding tissues. The urinary EC-SOD level was also significantly correlated,with the urinary; cyclic adenosine monophosphate (cAMP) level, cAMP analogues and adenlate cyclase modulators significantly stimulated the expression of EC-SOD but not other SOD isozymes in cultured fibroblast cell lines. Moreover, injection of parathyroid hormone, in Ellsworth-Howard tests, increased urinary EC-SOD accompanied with the elevations of urinary cAMP and NAG. Together these observations suggest that factor(s) that stimulate the adenylate cyclase-cAMP sl stem regulate the urinary EC-SOD level. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:370 / 374
页数:5
相关论文
共 50 条
  • [31] Extracellular Superoxide Dismutase Attenuates Renal Oxidative Stress Through the Activation of Adenosine Monophosphate-Activated Protein Kinase in Diabetic Nephropathy
    Hong, Yu Ah
    Lim, Ji Hee
    Kim, Min Young
    Kim, Yaeni
    Park, Hoon Suk
    Kim, Hyung Wook
    Choi, Bum Soon
    Chang, Yoon Sik
    Kim, Hye Won
    Kim, Tae-Yoon
    Park, Cheol Whee
    ANTIOXIDANTS & REDOX SIGNALING, 2018, 28 (17) : 1543 - 1561
  • [32] Two variants of extracellular-superoxide dismutase: Relationship to cardiovascular risk factors in an unselected middle-aged population
    Marklund, SL
    Nilsson, P
    Israelsson, K
    Schampi, I
    Peltonen, M
    Asplund, K
    JOURNAL OF INTERNAL MEDICINE, 1997, 242 (01) : 5 - 14
  • [33] Extracellular vesicles: another compartment for the second messenger, cyclic adenosine monophosphate
    Sayner, Sarah L.
    Choi, Chung-Sik
    Maulucci, Marcy E.
    Ramila, K. C.
    Zhou, Chun
    Scruggs, April K.
    Yarbrough, Thomas
    Blair, Leslie A.
    King, Judy A.
    Seifert, Roland
    Kaever, Volkhard
    Bauer, Natalie N.
    AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY, 2019, 316 (04) : L691 - L700
  • [34] Neonatal Extracellular Superoxide Dismutase Knockout Mice Increase Total Superoxide Dismutase Activity and VEGF Expression after Chronic Hyperoxia
    Mathias, Maxwell
    Taylor, Joann
    Mendralla, Elizabeth
    Perez, Marta
    ANTIOXIDANTS, 2021, 10 (08)
  • [35] Decreased plasma extracellular superoxide dismutase level in patients with vasospastic angina
    Yamashita, Kazuhito
    Takahiro, Kubara
    Kamezaki, Fumihiko
    Adachi, Tetsuo
    Tasaki, Hiromi
    ATHEROSCLEROSIS, 2007, 191 (01) : 147 - 152
  • [36] An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases
    Adachi, T
    Morihara, N
    Yamazaki, N
    Yamada, H
    Futenma, A
    Kato, K
    Hirano, K
    JOURNAL OF BIOCHEMISTRY, 1996, 120 (01) : 184 - 188
  • [37] Oxidized low-density lipoprotein accelerates the destabilization of extracellular-superoxide dismutase mRNA during foam cell formation
    Makino, Junya
    Nii, Miyuki
    Kamiya, Tetsuro
    Hara, Hirokazu
    Adachi, Tetsuo
    ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2015, 575 : 54 - 60
  • [38] Extracellular Superoxide Dismutase Attenuates Hepatic Oxidative Stress in Nonalcoholic Fatty Liver Disease through the Adenosine Monophosphate-Activated Protein Kinase Activation
    Nam, Heechul
    Lim, Ji Hee
    Kim, Tae Woo
    Kim, Eun Nim
    Oum, Sae-Jong
    Bae, Si Hyun
    Park, Cheol Whee
    ANTIOXIDANTS, 2023, 12 (12)
  • [39] Urinary cyclic guanosine 3′,5′-monophosphate and cyclic adenosine 3′,5′-monophosphate changes in spontaneous and induced onset active labor
    Chen, DC
    Yuan, SSF
    Su, HY
    Lo, SC
    Ren, SS
    Wu, GJ
    ACTA OBSTETRICIA ET GYNECOLOGICA SCANDINAVICA, 2005, 84 (11) : 1081 - 1086
  • [40] ER stress inducer, thapsigargin, decreases extracellular-superoxide dismutase through MEK/ERK signalling cascades in COS7 cells
    Kamiya, Tetsuro
    Obara, Aya
    Hara, Hirokazu
    Inagaki, Naoki
    Adachi, Tetsuo
    FREE RADICAL RESEARCH, 2011, 45 (06) : 692 - 698