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Polyisoprenylated Methylated Protein Methyl Esterase in various animal tissues: Implications for organophosphorus compound‐induced neuropathy
Author(s) -
Aguilar Byron J,
Amissah Felix,
AyukTakem Lambert,
Duverna Randolph,
Lamango Nazarius S
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.721.1
PMPMEase is a ubiquitous enzyme initially identified as carboxylesterase 1. It is a serine esterase and as such is susceptible to organophosphorus compounds (OPs) and sulfonyl fluorides. PMPMEase activities in the tissues of bovine, chicken, human, porcine, mouse, rat and sheep were determined. Enzymatic activities ranging between 1 and 124 nmol/min/g of protein were observed in the brain, heart, intestine, kidney, liver, lung and spleen. The liver exhibited the highest specific activity for all the species, 3–124 nmol/min/g of protein. The kidney and lung also showed good specific activity 2–61 and 2–84 nmol/min/g of protein, respectively. PMPMEase activities of 18 and 70 nmol/min/g of protein were detected in the blood of mice and rats, respectively. No activity was detected in human, bovine, porcine, sheep and chicken blood. Rodents have been reported to be resistant to non‐cholinergic OPs poisoning. The presence of circulating PMPMEase activity in rodents and not the other species may suggest that the blood activities may act as a shield, neutralizing the OPs before it reaches organs such as the brain where they may cause neuropathy. Supported by NIH/NIGMS/SCORE (GM 08111‐35) & NIH/NCRR (G12 RR0 3020).