Disease relevance of Ppa1

• The causative agent of tuberculosis, Mycobacterium tuberculosis, contains a well conserved copy of PPase [1].

High impact information on Ppa1

• The inhibitor was identified as pyrophosphate on the basis of the calcification induced in aortas cultured with inorganic pyrophosphatase, the inhibition of calcification in injured aortas by pyrophosphate, and the production of inhibitory levels of pyrophosphate by normal aortas [2].
• In this study, we present evidence suggesting that both genistein and the serine/threonine protein phosphatase (PPase) inhibitor calyculin A activate the CFTR by inhibiting PPase activity [3].
• The data suggest that genistein and calyculin A inhibit different PPase activities, allowing CFTR phosphorylation and partial stimulation, by a basal PKA activity [3].
• Circadian rhythmometric analysis of hepatic phosphohydrolases with special reference to glucose-6-phosphatase and inorganic pyrophosphatase [4].
• Glucose-6-P phosphohydrolase shows a similar behavior with [glucose-6-P] less than or equal to 0.10 mM, but inorganic pyrophosphatase activity does not even at the 0.05 or 0.02 mM level [5].

Biological context of Ppa1

• Statistically significant circadian rhythm was detected in glucose-6-phosphatase (G6Pase) and inorganic pyrophosphatase (InPPase) activity expressed on fresh weight and protein basis [4].

References