Alterations in Properties and Isoenzyme Patterns of Esterases in Developing Rat Brain*

Bernsohn, Joseph; Barron, Kevin D.; Hess, Adeline R.; Hedrick, Marjorie T.

doi:10.1111/j.1471-4159.1963.tb11903.x

Cited by 32 publications

(4 citation statements)

References 35 publications

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“…fraction of the total tissue nonspecific esterase activity recovered in the supernatant of aqueous homogenates (BERNSOHN et al, 1963). The bound esterase is only extractable in aqueous media by the use of surfactants (BERNSOHN, BARRON and NORGELLO, 1964; BERNSOHN, BARRON, DOOLIN, HESS and HEDRICK, 1966). In addition to data on nonspecific esterase, limited qualitative ontogenetic observations on cholinesterases will be described.…”

mentioning

confidence: 99%

Esterases of Developing Human Brain*

Barron

Bernsohn

1968

Journal of Neurochemistry

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The free and bound nonspecific esterases occurring in, respectively, the saline and triton X‐100 extracts of adult and developing human brain were studied by starch gel electrophoresis (zymograms). Zymograms of the free esterase fraction visualized with NA as substrate were qualitatively similar at 5‐12 days of age to the electrophoretic patterns observed in adult material. In both adult and developing brain, zymograms of bound esterase resembled those of the free enzyme, the major difference being the presence in the former of a slow, broad, anodic zone of diethyl‐p‐nitrophenyl phosphate‐inhibited enzyme. Esterases characteristic of adult white matter and having preferential affinity for alpha‐naphthylpropionate, alpha‐naphthyl butyrate and alpha‐naphthyl valerate were not identified in infant brain until about 4 months postnatal age. A far‐moving, anodic enzyme was distinctly evident in zymograms of brains of less than 1 month of age. This enzyme hydrolysed NP, NB, and NV more actively than alpha‐naphthyl acetate. It was present in the adult brain but, in contrast to the infant, was no longer electrophoretically‐separable from another enzyme which had greater affinity for NA and had previously been designated the A10 band. Quantitative assays demonstrated that the bound esterase increased in cerebral and cerebellar cortex during development. In contrast, the proportion of free to bound esterase showed little change in white matter. Acetylcholinesterase and butyrylcholinesterase zymograms became identical to adult patterns from 1 to 4 months of age. Thiolacetic acid esterase was present at 38 weeks gestation. Some functional and anatomical correlations were attempted in explanation of the biochemical observations.

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confidence: 99%

Esterases of Developing Human Brain*

Barron

Bernsohn

1968

Journal of Neurochemistry

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“…On the other hand, the membranebound AChE activated postnatally (PD 15-30) displays the characteristic excess sub strate inhibition. Alterations in esterase isoenzymes have been reported in the rat brain during normal maturation of the ner vous system using a-naphthyl esters as sub strate, and a starch gel electrophoretic sys tem [Bernsohn et al, 1963]. With this separa tion system, the number of isoenzymes in creased from 4 to 5 at PD l to 141 month after birth.…”

Section: Discussionmentioning

confidence: 89%

Membrane-Bound Form of Acetylcholinesterase Activated during Postnatal Development of the Rat Somatosensory Cortex

Inestrosa¹,

Ruiz²

1985

Dev Neurosci

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We are interested in the expression of synapse-specific macromolecules and its correlation with the appearance of neuronal types and synaptogenesis during development of the mammalian brain. We report here studies showing that the appearance of acetylcholinesterase (AChE) at layer IV of the rat somatosensory cortex is correlated with the expression of a membrane-bound AChE. Both its electrophoretic mobility and its sedimentation coefficient remain unaltered during maturation; however, its kinetics parameters, the heat and fixative sensitivities and the substrate inhibition changed through development. Our results suggest that an adult form of membrane-bound AChE is expressed postnatally.

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“…Chemically, heroin is a diacetylmorphine, characterized by the presence of two ester groups and therefore susceptible to hydrolysis to morphine by esterase enzymes. Therefore, it has been suggested that in vivo metabolism of heroin depends on the action of cholinesterase that seems to have partial affinity for such substrate, or of various aryl esterases already demonstrated to be present in the rat brain [6][7][8][9]. Based on this suggestion, and to define an eventual distribution specificity of such type enzymes active on heroin, the spinal cord and the remaining five large regions of the rat brain were prepared i.e., telencephalon, mesencephalon, diencephalon, cerebellum and medulla oblongata.…”

Section: Introductionmentioning

confidence: 99%

Titrimetric and parallel voltammetric sensitivity to heroin metabolism in brain

Crespi¹

2017

Brain Nerves

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A titrimetric technique has been successfully employed to measure esterase activities in different tissues. We have applied this tech nique to investigate the distribution of the esterase enzymes in spinal cord and five different brain areas of the rat (telencephalon, mesencephalon, diencephalon, cerebellum and medulla oblongata). The presence of non-specific esterase activity has been determined using alpha-napthyl acetate, a widely employed substrate for these en zymes, whereby the possible existence of "heroin-esterases" has been tested. Our results suggest that the activity of cerebral esterase's on heroin can be studied selectively at pH 8.5, showing quantitative differences in the distribution of these so-called " heroin-es terases" in spinal cord and in the five brain areas studied.In parallel, the efficacy of such "heroin-esterases" has been verified using voltammetric analysis of the influence of the brain enzymes upon the substrate heroin resulting in the evidence of an oxidation signal due to the selective oxidation of uprising morphine.Furthermore, the localization of these enzymes seems to overlap the distribution of brain morphine receptors, suggesting a possible role for these "heroin-esterase" in the metabolism and subsequent ly in the pharmacological activity of heroin, i.e., by converting this drug into morphine.

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Alterations in Properties and Isoenzyme Patterns of Esterases in Developing Rat Brain*

Cited by 32 publications

References 35 publications

Esterases of Developing Human Brain*

Esterases of Developing Human Brain*

Membrane-Bound Form of Acetylcholinesterase Activated during Postnatal Development of the Rat Somatosensory Cortex

Titrimetric and parallel voltammetric sensitivity to heroin metabolism in brain

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