Clinical significance of esterases in XXXX .

@entity1 @entity4521 @entity5940 @entity12880 @entity2697 @entity117 @entity8162 @entity5012 @entity13507 @entity2900 @entity1339
Esterases, hydrolases which split @entity13507 bonds, hydrolyse a number of compounds used as drugs in @entity1 . The enzymes involved are classified broadly as cholinesterases (including acetylcholinesterase), carboxylesterases, and arylesterases, but apart from acetylcholinesterase, their biological function is unknown. The acetylcholinesterase present in nerve endings involved in neurotransmission is inhibited by anticholinesterase drugs, e.g. @entity1339 , and by organophosphorous compounds (mainly insecticides). Cholinesterases are primarily involved in drug hydrolysis in the plasma, arylesterases in the plasma and red blood cells, and carboxylesterases in the liver, gut and other tissues. The esterases exhibit specificities for certain substrates and inhibitors but a drug is often hydrolysed by more than one esterase at different sites. @entity117 ( @entity117 ), for example, is hydrolysed to @entity2697 by carboxylesterases in the liver during the first-pass. Only 60% of an oral dose reaches the systemic circulation where it is hydrolysed by plasma cholinesterases and albumin and red blood cell arylesterases. Thus, the concentration of @entity117 relative to @entity2697 in the circulation may be affected by individual variation in esterase levels and the relative roles of the different esterases, and this may influence the overall pharmacological effect. Other drugs have been less extensively investigated than @entity117 and these include @entity4521 ( @entity4521 ), @entity2900 ( @entity2900 ), @entity12880 , @entity5012 , @entity8162 and other local anaesthetics. Ester prodrugs are widely used to improve absorption of drugs and in depot preparations. The active drug is released by hydrolysis by tissue carboxylesterases. Individual differences in esterase activity may be genetically determined, as is the case with atypical cholinesterases and the polymorphic distribution of serum paraoxonase and red blood cell @entity5940 . Disease states may also alter esterase activity.
