Plasmalemmal vacuolar-type H+-ATPase in cancer biology

被引:129
|
作者
Sennoune, SR [1 ]
Luo, DF
Martinez-Zaguilán, R
机构
[1] Texas Tech Univ, Hlth Sci Ctr, Dept Physiol, Lubbock, TX 79430 USA
[2] Texas Tech Univ, Hlth Sci Ctr, SW Canc Ctr, Lubbock, TX 79430 USA
关键词
V-ATPase; F-ATPase; organelle; plasma membrane; tumor; invasion; metastasis; apoptosis;
D O I
10.1385/CBB:40:2:185
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
Vacuolar-type H+-adenosine triphosphatase (V-ATPase) is one of the most fundamental enzymes in nature. V ATPases are responsible for the regulation of proton concentration in the intracellular acidic compartments. It has similar structure with the mitochondrial F0F1-ATP synthase (F-ATPase).dagger The V ATPases are composed of multiple subunits and have various physiological functions, including membrane and organelle protein sorting, neurotransmitter uptake, cellular degradative processes, and cytosolic pH regulation. The V-ATPases have been involved in multidrug resistance. Recently, plasma membrane V-ATPases have been involved in regulation of extracellular acidity, essential for cellular invasiveness and proliferation in tumor metastasis. The current knowledge regarding the structure and function of V ATPase and its role in cancer biology is discussed.
引用
收藏
页码:185 / 206
页数:22
相关论文
共 50 条
  • [41] CHARACTERIZATION OF THE OSTEOCLAST VACUOLAR H+-ATPASE B-SUBUNIT
    BARTKIEWICZ, M
    HERNANDO, N
    REDDY, SV
    ROODMAN, GD
    BARON, R
    GENE, 1995, 160 (02) : 157 - 164
  • [42] Vacuolar H+-ATPase meets glycosylation in patients with cutis laxa
    Guillard, Mailys
    Dimopoulou, Aikaterini
    Fischer, Bjoern
    Morava, Eva
    Lefeber, Dirk J.
    Kornak, Uwe
    Wevers, Ron A.
    BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, 2009, 1792 (09): : 903 - 914
  • [43] New insight into the structure and regulation of the plant vacuolar H+-ATPase
    Kluge, C
    Lahr, J
    Hanitzsch, M
    Bolte, S
    Golldack, D
    Dietz, KJ
    JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 2003, 35 (04) : 377 - 388
  • [44] New Insight into the Structure and Regulation of the Plant Vacuolar H+-ATPase
    Christoph Kluge
    Joachim Lahr
    Miriam Hanitzsch
    Susanne Bolte
    Dortje Golldack
    Karl-Josef Dietz
    Journal of Bioenergetics and Biomembranes, 2003, 35 : 377 - 388
  • [45] Amino Acid Availability Modulates Vacuolar H+-ATPase Assembly
    Stransky, Laura A.
    Forgac, Michael
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2015, 290 (45) : 27360 - 27369
  • [46] Characterization and Localization of the Vacuolar-Type ATPase in the Midgut Cells of Silkworm (Bombyx mori)
    Yang, Huajun
    Chen, Huiqing
    Chen, Keping
    Yao, Qin
    Zhao, Guoli
    Wu, Chao
    Lv, Peng
    Wang, Lin
    ZEITSCHRIFT FUR NATURFORSCHUNG SECTION C-A JOURNAL OF BIOSCIENCES, 2009, 64 (11-12): : 899 - 905
  • [47] Vacuolar H+-ATPase (V-ATPase) Promotes Vacuolar Membrane Permeabilization and Nonapoptotic Death in Stressed Yeast
    Kim, Hyemin
    Kim, Adam
    Cunningham, Kyle W.
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (23) : 19029 - 19039
  • [48] Exploring the Link between Vacuolar-Type Proton ATPase and Epithelial Cell Polarity
    Sun-Wada, Ge-Hong
    Wada, Yoh
    BIOLOGICAL & PHARMACEUTICAL BULLETIN, 2022, 45 (10) : 1419 - 1425
  • [49] Phenotypic subunit composition of the tobacco (Nicotiana tabacum L.) vacuolar-type H+-translocating ATPase
    Drobny, M
    Schnölzer, M
    Fiedler, S
    Lüttge, U
    Fischer-Schliebs, E
    Christian, AL
    Ratajczak, R
    BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2002, 1564 (01): : 243 - 255
  • [50] Toosendanin, a novel potent vacuolar-type H plus -translocating ATPase inhibitor, sensitizes cancer cells to chemotherapy by blocking protective autophagy
    Dong, Yu
    Zhu, Guoyuan
    Wang, Sheng-Fang
    Keon, Kristine A.
    Rubinstein, John L.
    Zeng, Si-Xin
    Zhang, Shuang
    Chen, Qiu-Ling
    Fu, Jing
    Li, Min
    Shen, Han-Ming
    Lu, Jin-Jian
    Chen, Xiu-Ping
    Lu, Jia-Hong
    INTERNATIONAL JOURNAL OF BIOLOGICAL SCIENCES, 2022, 18 (07): : 2684 - 2702