Renal Vacuolar H+-ATPase
Vacuolar H+-ATPases are ubiquitous multisubunit complexes mediating the ATP-dependent
transport of protons. In addition to their role in acidifying the lumen of various intracellular …
transport of protons. In addition to their role in acidifying the lumen of various intracellular …
Regulation of luminal acidification by the V-ATPase
Specialized cells in the body express high levels of V-ATPase in their plasma membrane
and respond to hormonal and nonhormonal cues to regulate extracellular acidification …
and respond to hormonal and nonhormonal cues to regulate extracellular acidification …
V-ATPases in osteoclasts: structure, function and potential inhibitors of bone resorption
The vacuolar-type H+-ATPase (V-ATPase) proton pump is a macromolecular complex
composed of at least 14 subunits organized into two functional domains, V1 and V0. The …
composed of at least 14 subunits organized into two functional domains, V1 and V0. The …
Osteoclastic acidification pathways during bone resorption
AV Rousselle, D Heymann - Bone, 2002 - Elsevier
Osteoclasts resorb bone by attaching to the surface and then secreting protons into an
extracellular compartment formed between osteoclast and bone surface. This secretion is …
extracellular compartment formed between osteoclast and bone surface. This secretion is …
How the osteoclast degrades bone
HC Blair - Bioessays, 1998 - Wiley Online Library
Osteoclasts are multinucleated monocyte‐macrophage derivatives that degrade bone. Their
specialized role is central to a process that continuously removes and replaces segments of …
specialized role is central to a process that continuously removes and replaces segments of …
Three subunit a isoforms of mouse vacuolar H+-ATPase: preferential expression of the a3 isoform during osteoclast differentiation
T Toyomura, T Oka, C Yamaguchi, Y Wada… - Journal of biological …, 2000 - ASBMB
Vacuolar H+-ATPase (V-ATPase) is a multi-subunit enzyme with a membrane peripheral
catalytic (V 1) and an intrinsic (V o) sector. We have identified three cDNA clones coding for …
catalytic (V 1) and an intrinsic (V o) sector. We have identified three cDNA clones coding for …
Distinct expression patterns of different subunit isoforms of the V-ATPase in the rat epididymis
C Pietrement, GH Sun-Wada, N Da Silva… - Biology of …, 2006 - academic.oup.com
In the epididymis and vas deferens, the vacuolar H+ ATPase (V-ATPase), located in the
apical pole of narrow and clear cells, is required to establish an acidic luminal pH. Low pH is …
apical pole of narrow and clear cells, is required to establish an acidic luminal pH. Low pH is …
Differentiation and functions of osteoclasts and odontoclasts in mineralized tissue resorption
T Sasaki - Microscopy research and technique, 2003 - Wiley Online Library
The differentiation and functions of osteoclasts (OC) are regulated by osteoblast‐derived
factors such as receptor activator of NFKB ligand (RANKL) that stimulates OC formation, and …
factors such as receptor activator of NFKB ligand (RANKL) that stimulates OC formation, and …
Regulation of the V-ATPase in kidney epithelial cells: dual role in acid–base homeostasis and vesicle trafficking
The proton-pumping V-ATPase is a complex, multi-subunit enzyme that is highly expressed
in the plasma membranes of some epithelial cells in the kidney, including collecting duct …
in the plasma membranes of some epithelial cells in the kidney, including collecting duct …
The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site
LS Holliday, M Lu, BS Lee, RD Nelson… - Journal of Biological …, 2000 - ASBMB
Vacuolar H+-ATPase (V-ATPase) binds actin filaments with high affinity (K d= 55 nm; Lee,
BS, Gluck, SL, and Holliday, LS (1999) J. Biol. Chem. 274, 29164–29171). We have …
BS, Gluck, SL, and Holliday, LS (1999) J. Biol. Chem. 274, 29164–29171). We have …