Characterization of vacuolar-ATPase and selective inhibition of vacuolar-H(+)-ATPase in osteoclasts.
V-ATPase plays important roles in controlling the extra- and intra-cellular pH in eukaryotic cell, which is most crucial for cellular processes. V-ATPases are composed of a peripheral V(1) domain responsible for ATP hydrolysis and integral V(0) domain responsible for proton translocation. Osteoclasts are multinucleated cells responsible for bone resorption and relate to many common lytic bone disorders such as osteoporosis, bone aseptic loosening, and tumor-induced bone loss. This review summarizes the structure and function of V-ATPase and its subunit, the role of V-ATPase subunits in osteoclast function, V-ATPase inhibitors for osteoclast function, and highlights the importance of V-ATPase as a potential prime target for anti-resorptive agents.
Yao
GuanFeng
G
Department of Orthopedics, The Second Affiliated Hospital, ShanTou University Medical College, ShanTou, GuangDong 515041, China.
Feng
HaoTian
H
Cai
YanLing
Y
Qi
Weili
W
Kong
KangMei
K
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D010010:Osteoclasts / Q000378:metabolism* / Q000648:ultrastructure*; D015398:Signal Transduction / Q000502:physiology*; D014617:Vacuoles / Q000378:metabolism*
D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases