메뉴 건너뛰기




Volumn 374, Issue 2, 2003, Pages 315-319

The requirement of cytosolic phospholipase A2 for the PMA activation of proton efflux through the N-terminal 230-amino-acid fragment of gp91phox

Author keywords

Arachidonic acid; gp91phox; NADPH oxidase; Phospholipase A 2; Proton channel

Indexed keywords

CELLS; CYTOLOGY; PHYSIOLOGY; PROTONS;

EID: 0041829126     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030495     Document Type: Article
Times cited : (14)

References (26)
  • 1
    • 0020573287 scopus 로고
    • Unsaturated fatty acids as second messengers of superoxide generation by macrophages
    • Bromberg, Y. and Pick, E. (1983) Unsaturated fatty acids as second messengers of superoxide generation by macrophages. Cell. Immunol. 79, 240-252
    • (1983) Cell. Immunol. , vol.79 , pp. 240-252
    • Bromberg, Y.1    Pick, E.2
  • 3
    • 0028181632 scopus 로고
    • 2 for activation of the assembled NADPH oxidase in human neutrophils
    • 2 for activation of the assembled NADPH oxidase in human neutrophils. Biochem. J. 297, 217-223
    • (1994) Biochem. J. , vol.297 , pp. 217-223
    • Dana, R.1    Malech, H.L.2    Levy, R.3
  • 5
    • 0027395762 scopus 로고
    • The immediate activator of the NADPH oxidase is arachidonate not phosphorylation
    • Henderson, L. M., Moule, S. K. and Chappell, J. B. (1993) The immediate activator of the NADPH oxidase is arachidonate not phosphorylation. Eur. J. Biochem. 211, 157-162
    • (1993) Eur. J. Biochem. , vol.211 , pp. 157-162
    • Henderson, L.M.1    Moule, S.K.2    Chappell, J.B.3
  • 10
    • 0033618397 scopus 로고    scopus 로고
    • + channel in phagocyte-like cells
    • + channel in phagocyte-like cells. J. Biol. Chem. 274, 21603-21608
    • (1999) J. Biol. Chem. , vol.274 , pp. 21603-21608
    • Lowenthal, A.1    Levy, R.2
  • 12
    • 0031026632 scopus 로고    scopus 로고
    • 2 in activated human monocytes: Regulation of superoxide anion production and low density lipoprotein oxidation
    • 2 in activated human monocytes: regulation of superoxide anion production and low density lipoprotein oxidation. J. Biol. Chem. 272, 2404-2411
    • (1997) J. Biol. Chem. , vol.272 , pp. 2404-2411
    • Li, Q.1    Cathcart, M.K.2
  • 16
    • 0035448083 scopus 로고    scopus 로고
    • + channel by DEPC, a histidine modifying agent: Evidence for at least two target sites
    • + channel by DEPC, a histidine modifying agent: evidence for at least two target sites. Biochem. J. 358, 315-324
    • (2001) Biochem. J. , vol.358 , pp. 315-324
    • Mankelow, T.J.1    Henderson, L.M.2
  • 17
    • 0018764575 scopus 로고
    • Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ
    • Thomas, J. A., Buchsbaum, R. N., Zimniak, A. and Racker, E. (1979) Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ. Biochemistry 18, 2210-2218
    • (1979) Biochemistry , vol.18 , pp. 2210-2218
    • Thomas, J.A.1    Buchsbaum, R.N.2    Zimniak, A.3    Racker, E.4
  • 20
    • 0036898073 scopus 로고    scopus 로고
    • phox component of NADPH oxidase is not a voltage-gated proton channel
    • phox component of NADPH oxidase is not a voltage-gated proton channel. J. Gen. Physiol. 120, 773-779
    • (2002) J. Gen. Physiol. , vol.120 , pp. 773-779
    • DeCoursey, T.E.1    Morgan, D.2    Cherny, V.V.3
  • 21
    • 0036900969 scopus 로고    scopus 로고
    • Voltage-gated proton "channels": A spectator's viewpoint
    • Touret, N. and Grinstein, S. (2002) Voltage-gated proton "channels": a spectator's viewpoint. J. Gen. Physiol. 120, 767-771
    • (2002) J. Gen. Physiol. , vol.120 , pp. 767-771
    • Touret, N.1    Grinstein, S.2
  • 22
    • 1842845132 scopus 로고    scopus 로고
    • NOX family NADPH oxidases: Do they have built-in proton channels?
    • Maturana, A., Krause, K. H. and Demaurex, N. (2002) NOX family NADPH oxidases: do they have built-in proton channels? J. Gen. Physiol. 120, 781-786
    • (2002) J. Gen. Physiol. , vol.120 , pp. 781-786
    • Maturana, A.1    Krause, K.H.2    Demaurex, N.3
  • 24
    • 0028271116 scopus 로고
    • Arachidonic acid metabolism by nuclei of a retinoic acid - Or vitamin D3-differentiated human leukemia cell line HL-60
    • Matsumoto, K., Morita, I. and Murota, S. (1994) Arachidonic acid metabolism by nuclei of a retinoic acid - or vitamin D3-differentiated human leukemia cell line HL-60. Prostaglandins Leukotrienes Essent. Fatty Acids 51, 51-55
    • (1994) Prostaglandins Leukotrienes Essent. Fatty Acids , vol.51 , pp. 51-55
    • Matsumoto, K.1    Morita, I.2    Murota, S.3
  • 25
    • 0022486975 scopus 로고
    • Lipoxygenation of arachidonic acid by differentiated and undifferentiated human promyelocytic HL-60 cells
    • Ziboh, V. A., Wong, T., Wu, M. C. and Yunis, A. A. (1986) Lipoxygenation of arachidonic acid by differentiated and undifferentiated human promyelocytic HL-60 cells. J. Lab. Clin. Med. 108, 161-166
    • (1986) J. Lab. Clin. Med. , vol.108 , pp. 161-166
    • Ziboh, V.A.1    Wong, T.2    Wu, M.C.3    Yunis, A.A.4
  • 26
    • 0029822371 scopus 로고    scopus 로고
    • - superoxide generating flavocytochrome b of neutrophils. Evidence for a transition from a low-spin state to a high-spin state of the heme iron component
    • - superoxide generating flavocytochrome b of neutrophils. Evidence for a transition from a low-spin state to a high-spin state of the heme iron component. Biochemistry 35, 13400-13410
    • (1996) Biochemistry , vol.35 , pp. 13400-13410
    • Doussiere, J.1    Gaillard, J.2    Vignais, P.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.