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Tartrate-resistant acid phosphatase : ウィキペディア英語版
Tartrate-resistant acid phosphatase

Tartrate-resistant acid phosphatase (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5), is a glycosylated monomeric metalloprotein enzyme expressed in mammals. It has a molecular weight of approximately 35kDa, a basic isoelectric point (7.6-9.5), and optimal activity in acidic conditions. TRAP is synthesized as latent proenzyme and activated by proteolytic cleavage and reduction. It is differentiated from other mammalian acid phosphatases by its resistance to inhibition by tartrate, molecular weight and characteristic purple colour.
The mechanism of phosphate ester hydrolysis by TRAP is through a nucleophilic attack mechanism, whereby, catalysis occurs with the binding of a phosphate-substrate to the Fe2+ in the active site of TRAP. This is then followed by a nucleophilic attack by a hydroxide ligand on the bound phosphorus atom, resulting in cleavage of the phosphate ester bond and production of an alcohol. The exact identity and mechanism of the hydroxide ligand is unclear, but it is thought to be either a hydroxide that bridges the metal ions within the active site or a terminal hydroxide bound to Fe3+, with conflicting reports for both mechanisms.
==TRAP expression and cell localization==

Under normal circumstances, TRAP is highly expressed by osteoclasts, activated macrophages, neurons, and by the porcine endometrium during pregnancy. In newborn rats, TRAP is also detectable in the spleen, thymus, liver, kidneys, skin, lung, and heart at low levels. TRAP expression is increased in certain pathological conditions. These include leukaemic reticuloendotheliosis (hairy cell leukaemia), Gaucher’s disease, HIV-induced encephalopathy, osteoclastoma and osteoporosis, and metabolic bone diseases.
In osteoclasts, TRAP is localized within the ruffled border area, the lysosomes, the Golgi cisternae and vesicles.〔

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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