Esterase-18 (ES-18) of the house mouse (Mus musculus): Biochemical characterization and genetics of an allozyme system linked to chromosome 19

Oh, von Deimling; Gaa, Andreas; Mm, Simon

doi:10.1007/bf02399606

Cited by 6 publications

(1 citation statement)

References 21 publications

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“…Many of the proteins that were significantly altered by 3 months of exercising were in pathways that govern energy regulation and cellular metabolism, including alterations in the phosphorylation state of NADH dehydrogenase, Enol Coenzyme A hydratase (Echs1), which is essential to the metabolism of fatty acids (Nagi et al, 1988), creatine kinase, which functions in the creation of energy reserves for rapid regeneration of ATP and is involved in maintaining structural integrity of mitochondria (Qin et al, 1998) and aldolase C, an enzyme in the glycolytic pathway (Villar-Palasi and Larner, 1970). We also noted changes in the phosphorylation state of proteins known to affect cellular metabolism including sepiapterin reductase, an enzyme required for tetrahydrobiopterin (BH4) biosynthesis (Levine et al, 1990) and glutamate oxaloacetate transaminase 1 (Got1) (Reshef et al, 2003; von Deimling et al, 1988). Changes in the phosphorylation state of the vesicle release and trafficking protein N-ethylmaleimide sensitive fusion attachment protein alpha (Andreeva et al, 2006) were also noted.…”

Section: Resultsmentioning

confidence: 98%

Exercise protects against MPTP-induced neurotoxicity in mice

et al. 2010

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Exercise has been shown to be potently neuroprotective in several neurodegenerative models, including 1-methyl-4 phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) model of Parkinson's disease (PD). In order to determine the critical duration of exercise necessary for DA neuroprotection, mice were allowed to run for either 1, 2 or 3 months prior to treatment with saline or MPTP. Quantification of DA neurons in the SNpc show that mice allowed to run unrestricted for 1 or 2 months lost significant numbers of neurons following MPTP administration as compared to saline treated mice; however, 3 months of exercise provided complete protection against MPTP-induced neurotoxicity. To determine the critical intensity of exercise for DA neuroprotection, mice were restricted in their running to either 1/3 or 2/3 that of the full running group for 3 months prior to treatment with saline or MPTP. Quantification of DA neurons in the SNpc show that mice whose running was restricted lost significant numbers of DA neurons due to MPTP toxicity; however, the 2/3 running group demonstrated partial protection. Neurochemical analyses of DA and its metabolites DOPAC and HVA show that exercise also functionally protects neurons from MPTP induced neurotoxicity. Proteomic analysis of SN and STR tissues indicates that 3 months of exercise induces changes in proteins related to energy regulation, cellular metabolism, the cytoskeleton, and intracellular signaling events. Taken together, these data indicate that exercise potently protects DA neurons from acute MPTP toxicity, suggesting that this simple lifestyle element may also confer significant protection against developing PD in humans.

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Section: Resultsmentioning

confidence: 98%

Exercise protects against MPTP-induced neurotoxicity in mice

et al. 2010

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Micro two‐dimensional gel electrophoresis of serum and testis esterases from different strains of mice

Abou-Haïla

1990

Electrophoresis

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Two-dimensional electrophoresis with time-dependent polyacrylamide gradient gel electrophoresis (PAGGE) in the second dimension was applied to the separation of native molecular forms of esterases from serum and testis of four strains of mice (C57BL/6J, Swiss OF1, F1 hybrid derived from these two populations and Tfm). In Phast System, a modified pH 3-9 gradient, a linear 8-25% gel gradient and a migration time corresponding to 300 Vh, were found to provide the best conditions for esterase analysis. About 70 esterase-active fractions could be separated with good reproducibility. The variants were characterized by their pI (3.9-7.35), their relative mobility and the visual estimation of their susceptibility towards neuraminidase and different esterase inhibitors. In the two tissues, the distribution of the esterase variants corresponded to a 50-500 kDa molecular mass range of calibration proteins, but most of the serum and testis-specific isoforms were confined to the 59-72 kDa range. All serum variants contained a terminal N-acetylneuraminic acid residue, whereas only the testicular esterases in common with those in serum appeared sensitive to neuraminidase. Cholinesterases with a low relative mobility and carboxylesterases with a high relative mobility were detected in serum, while carboxylesterases accounted for the greatest part in the testis which also contained cholinesterases and acetylesterases. Minor interspecies differences were found between C57BL/6J and Swiss OF1 esterases. The expression of two variants which differed between these two species seemed intermediate for the hybrid originating from these two populations. Two new spots were detected in the two-dimensional map of esterases from the strain bearing the Tfm mutation.

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Biochemical and physiological studies of soluble esterases fromDrosophila melanogaster

1991

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Twenty-two soluble esterases have been identified in D. melanogaster by combining the techniques of native polyacrylamide gel electrophoresis and isoelectric focusing. The sensitivity of each isozyme to three types of inhibitors (organophosphates, eserine sulfate, and sulfydryl reagents) identified 10 as carboxylesterases, 6 as cholinesterases, and 3 as acetylesterases. Three isozymes could not be classified and no arylesterases were identified. The carboxyl- and cholinesterases could each be further divided into two subclasses on the basis of inhibition by organophosphates and sulfhydryl reagents, respectively. Choline- and acetylesterases have characteristic substrate preferences but both subclasses of carboxylesterases are heterogeneous in substrate utilization. Subclass 2 carboxylesterases exhibit diverse temporal expression patterns, with subclass 1 carboxylesterases generally found in larvae and subclass 1 cholinesterases and acetylesterases more characteristic of pupae and adults. Tissues showing the greatest number of isozymes are larval body wall (eight) and digestive tract (six in larvae, six in adults). Carboxylesterases are distributed across a wide range of tissues, but subclass 1 cholinesterases are generally associated with neural or neurosecretory tissues and subclass 2 cholinesterases with digestive tissues.

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Esterase-18 (ES-18) of the house mouse (Mus musculus): Biochemical characterization and genetics of an allozyme system linked to chromosome 19

Cited by 6 publications

References 21 publications

Exercise protects against MPTP-induced neurotoxicity in mice

Exercise protects against MPTP-induced neurotoxicity in mice

Micro two‐dimensional gel electrophoresis of serum and testis esterases from different strains of mice

Biochemical and physiological studies of soluble esterases fromDrosophila melanogaster

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