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Literature summary for 7.1.2.2 extracted from

  • Sakai, H.; Moriura, Y.; Notomi, T.; Kawawaki, J.; Ohnishi, K.; Kuno, M.
    Phospholipase C-dependent Ca2+-sensing pathways leading to endocytosis and inhibition of the plasma membrane vacuolar H+-ATPase in osteoclasts (2010), Am. J. Physiol. Cell Physiol., 299, C570-C578.
    View publication on PubMed
Search for more literature for 7.1.2.2

Inhibitors

Inhibitors Comment Organism Structure
bafilomycin A1
-
 Mus musculus
Ca2+ extracellular, inhibits the enzym ein osteoclast membranes, Ca2+ behaves as a negative feedback signal for osteoclast function Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane high enzyme content in the ruffled membrane facing the the bone surface Mus musculus 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Mus musculus
-
 ADP + phosphate + H+/out
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
osteoclast
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Mus musculus ADP + phosphate + H+/out
-
 ?

Synonyms

Synonyms Comment Organism
plasma membrane V-ATPase
-
 Mus musculus
plasma membrane vacuolar H+-ATPase
-
 Mus musculus

General Information

General Information Comment Organism
additional information Ca2+ facilitates a dynamin- and V-ATPase-dependent endocytosis in association with with an inhibition of the plasma membrane V-ATPase, overview Mus musculus
physiological function the protons secreted by the enzyme in osteoclast membrane into the closed extracellular compartment are essential for demineralization of calcified bone Mus musculus