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- W2075996894 abstract "It has become recognized that purinergic cell signaling is largely regulated by the extracellular-compartmentalized metabolome in specific organs and tissues. This regulation primarily involves membrane-bound and interstitial catabolic enzymes. Adenosine deaminase-1 (ADA), the encoding of which does not include a signal sequence, appears to be introduced into the interstitial compartment by a regulated mechanism. Recent evidence from various avenues of investigation now implicate ADA as an important regulator of adenosine signaling through both metabolomic influences and allosteric modulation of adenosine receptor actions. As a free enzyme, ADA can reduce adenosine concentrations to form inosine. ADA can also associate with membrane-bound proteins, including CD26 and adenosine receptors. It has been hypothesized that when bound to CD26 the enzymatic function of ADA is tightly localized, and may be important in the regulation of the cAMP-adenosine pathway. In contrast, recent evidence also suggests that ADA can be bound to adenosine receptors. Under the conditions investigated, the receptor affinity for adenosine increases. Kinetic analyses indicate that the probability of receptor binding and activation dominates over deamination under these conditions. These diverse, yet complimentary, roles can explain curious phenomena previously observed in the heart, and have important implications for cardiac responses to inflammatory challenges. Evidence from our laboratory demonstrates unique cytokine modulation by ADA that are consistent with both enzymatic and nonenzymatic roles for ADA in the heart and other tissues during inflammatory challenges and sepsis." @default.
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- W2075996894 date "2006-06-01" @default.
- W2075996894 modified "2023-09-29" @default.
- W2075996894 title "THE CARDIAC PURINE METABOLOME DURING SEPSIS" @default.
- W2075996894 doi "https://doi.org/10.1097/00024382-200606001-00048" @default.
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