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Differences in nonspecific esterase from normal and leukemic monocytes.

P D Cohn, P D Emanuel, M J Bozdech

|June 1, 1987

Summary

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Nonspecific esterase (NSE) isozymes in normal and leukemic monocytes were characterized. Leukemic cells showed two NSE isozyme families, while normal cells had only one, suggesting distinct roles in phagocyte function.

Area of Science:

Biochemistry
Cell Biology
Hematology

Background:

Nonspecific esterase (NSE) is crucial for cytochemical identification of mononuclear phagocytes, including leukemic cells.
NSE activity can be demonstrated through the hydrolysis of alpha-naphthyl acetate or butyrate.

Purpose of the Study:

To characterize and differentiate nonspecific esterase (NSE) isozymes from normal and leukemic human monocytes.
To investigate the biochemical properties and potential functional differences of these isozymes.

Main Methods:

Extraction of NSE from leukemic monocytes using various detergents.
Isoelectric focusing (IEF) to separate isozymes based on isoelectric point (pI).
Enzyme inhibition studies (sodium fluoride, PMSF), heat stability, and antigenic characterization.

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Main Results:

Two distinct pI categories of NSE isozymes were identified in leukemic monocytes (pI 5.7-6.3 and pI ≥6.6-7.6).
Normal monocytes exclusively exhibited the lower pI (5.7-6.3) isozymes.
While sharing some properties (inhibition by fluoride, Con-A binding, substrate preference), the two isozyme families differed in PMSF inhibition, heat resistance, and antigenic properties.

Conclusions:

Leukemic monocytes express at least two families of NSE isozymes, whereas normal monocytes express only one.
These isozymes are likely cell surface glycoproteins, resembling liver carboxyl or B-esterases.
The distinct properties suggest differential roles or regulation in normal versus malignant mononuclear phagocytes.