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atrophy/phosphatase

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The effect of nodularin on selective atrophy of left lobes in the liver was investigated in F344 rats. Nodularin was injected for 10 weeks from the third week of initiation with saline or N-nitrosodiethylamine (DEN), grouped as S/N and D/N, respectively. Nodularin significantly decreased weights of

Protein phosphatase 4 coordinates glial membrane recruitment and phagocytic clearance of degenerating axons in Drosophila.

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Neuronal damage induced by injury, stroke, or neurodegenerative disease elicits swift immune responses from glial cells, including altered gene expression, directed migration to injury sites, and glial clearance of damaged neurons through phagocytic engulfment. Collectively, these responses hinder

Degeneration and regeneration in denervated tonic and phasic skeletal muscle: morphology and acid phosphatase cytochemistry.

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Following denervation, ultrastructural alterations were observed in the tonic, anterior (ALD) and phasic posterior (PLD) latissimus dorsi muscles of the chicken. In the ALD muscle these changes were characteristic of both degeneration and regeneration, while in the PLD muscle, the changes were
Eight children with primary and secondary enteropathy were examined, in whom predominantly advanced partial atrophy and subtotal atrophy of the villous apparatus were established. Enzymic histochemical study of the activity of alkaline phosphatase showed correlation with the degree of villous

Dual-specificity phosphatase 4 is upregulated during skeletal muscle atrophy and modulates extracellular signal-regulated kinase activity.

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Skeletal muscle atrophy results from disparate physiological conditions, including denervation, corticosteroid treatment, and aging. The purpose of this study was to describe and characterize the function of dual-specificity phosphatase 4 (Dusp4) in skeletal muscle after it was found to be induced

Localization of non-specific esterase and acid phosphatase in human fibroblast from skeletal muscle atrophy.

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The intracellular localization of non-specific esterase and acid phosphatase was investigated in human fibroblast cells from skeletal muscle atrophy. Non-specific esterase and acid phosphatase positive sites were visualized ultrastructurally in the fibroblast. Electron microscopy for the
The Drosophila retinal degeneration C (rdgC) gene encodes an unusual protein serine/threonine phosphatase in that it contains at least two EF-hand motifs at its carboxy terminus. By a combination of large-scale sequencing of human retina cDNA clones and searches of expressed sequence tag and genomic
The survival of injured adult dopaminergic substantia nigra pars compacta neurons can be promoted by various neurotrophic factors. Most neurotrophic factor receptors are activated by intracellular tyrosine phosphorylation upon ligand binding and are subsequently inactivated or dephosphorylated by

Rapid assessment of protein-tyrosine phosphatase expression levels by RT-PCR with degenerate primers.

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Using degenerate oligodeoxynucleotide primers we previously obtained cDNA fragments from ten different murine protein-tyrosine phosphatases (PTPases). Employing this same primer set, a method was developed to assess the expression levels of these PTPase family members in a fast and simple way.
Skeletal muscle atrophy is caused by a decrease in muscle size and strength and results from a range of physiological conditions, including denervation, immobilization, corticosteroid exposure and aging. Newly named Dual Specificity Phosphatase 29 (Dusp29) has been identified as a novel neurogenic

MAP kinase phosphatase 1 is expressed and enhanced by FK506 in surviving mamillary, but not degenerating nigral neurons following axotomy.

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The MAP kinase phosphatase 1 (MKP-1), a dual serine-threonine phosphatase, inactivates the MAP kinases ERK and JNK/SAPK which are involved in neuronal survival and neuronal cell death following injury and degenerative stimuli. We have studied by immunocytochemistry whether regulation of MKP-1 is

Functional characterization of the three Drosophila retinal degeneration C (RDGC) protein phosphatase isoforms.

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Drosophila retinal degeneration C (RDGC) is the founding member of the PPEF family of protein phosphatases. RDGC mediates dephosphorylation of the visual pigment rhodopsin and the TRP ion channel. From the rdgC locus, three protein isoforms, termed RDGC-S, -M, and -L, with different N-termini are
Through our transcriptional mapping effort in the Xp22 region, we have isolated by exon trapping a new transcript highly homologous to the Drosophila retinal degeneration C (rdgC) gene. rdgC encodes a serine/threonine phosphatase protein and is required in Drosophila to prevent light-induced retinal

Cytochemical study of acid phosphatase activity in the functional and degenerating spinning gland cells of Pericallia ricinii (lepidoptera).

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A study of the presence, distribution and activity of acid phosphatase has been carried out in the cells of the spinning gland of moth pest Pericallia ricinii in sequential larval, prepupal and pupal stages. Acid phosphomonoesterase activity at first appears in the apical and basal regions of the

Drosophila retinal degeneration C (rdgC) encodes a novel serine/threonine protein phosphatase.

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The Drosophila retinal degeneration C (rdgC) gene is required to prevent light-induced retinal degeneration. Molecular analysis shows that the rdgC transcription unit encodes a novel serine/threonine protein phosphatase. Amino acids 153-393 define a domain that has 30% identity with the catalytic
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