Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.3.5.1 (succinate dehydrogenase)
 8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cochlear microphonics and succinic dehydrogenase (SDH) activity of the hair cells during anoxia were studied in guinea pigs. After injection of the glucose-glucose oxidase mixture into the cerebellomedullary cistern, the deprivation of the oxygen tension in CSF and perilymph was measured in different time courses. In CSF, oxygen tension was reduced to zero within 60 min while in perilymph the maximal reduction was about a half the original level. The cochlear microphonics responded well to the oxygen tension deprivation in the perilymph. SDH activity, particularly in the outer hair cells was quite parallel to the oxygen tension in perilymph and also to the behavior of the cochlear microphonics. The present results indicate a close relationship between the electrophysiological and histochemical findings and that cochlear microphonics represent the function of the outer hair cells only.
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PMID:Cochlear microphonics and SDH activity in the hair cells under anoxia. 98 31

The mouse granular convoluted tubules of submandibular gland of laboratory mouse are releasing a range of biologically active peptides (renin, neural growth factor and others) into both the saliva and blood circulation, the males producing it in a larger extent than females. Recently, several from respective peptides were identified to be endogenous ones and brain-related. The present work was aimed to utilise submandibular gland/SMG auto- and isotransplants regenerating in murine brain as a possibly local source of peptides. Experimentally, the newborn and juvenile matured white A breeded mice of both sexes were used. Glandular grafts were grafted into brain parenchyma or CSF spaces. Laboratory animals have then been perished during the first 6 weeks after transplantation, and the transplants so acquired evaluated as serial frontal sections embedded in paraffin and H.E. stained by light microscopy. Also cryocate sections were incubated in order to detect the presence of alkaline phosphatase (AP) and succinic dehydrogenase/(SDH). It was stated experimentally that both mentioned SMG grafts underwent the survival and development intracerebrally. Some first regressive changes were gradually replaced by glandular proliferation and lobular neomorphogenesis having been more pronounced in osotransplants. The proliferative period was characterized by cellular mitoses, multiplication of duct-like and terminal tubulous structures of newly formed glandular lobules. Partially, the isotransplants display the transformation of proliferation stage into that of cellular cytodifferentiation followed by gradual appearance of striated ducts, acini and even granular convoluted tubules on the 5th week after transplantation. Also the reoccurrence of enzyme activities in the transplant parenchyma after their initially total disappearance is testifying of both proliferation and cytodifferentiation developed gradually. During the first days of implantation, the revascularization of grafts occurs, those being high in AP endothelial activity of vessels newly formed. This is to conclude that higher proliferative intensity of isotransplants and their exclusive cytodifferentiation demonstrate that an undifferentiated murine SMG which can develop itself ontogenetically is more effective graft than a SMG differentiated fully. On the next stage, the development of glandular grafts will be studied with more delay after transplantations. Also the enzyme implementation of new parenchymatous components is to be elucidated. Further experimentation is planified as to influencing intracerebral SMG graft development with administration of hormones and isoproterenol to laboratory animals.
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PMID:[Regeneration of auto- and isografts of submandibular glands in the brain of laboratory mice. I. Morphologic evaluation of the healed graft using light microscopy]. 264 Mar 57

An Argentine male child died at 4.5 years of age of a lethal mitochondrial disease associated with a MELAS mutation and a Barth syndrome-like presentation. The child had severe failure to thrive from the early months and for approximately two years thereafter. In addition, the patient had severely delayed gross motor milestones, marked muscle weakness, and dilated cardiomyopathy that progressed to congestive heart failure. He also had persistently elevated urinary levels of 3-methylglutaconic and 2-ethylhydracrylic acids and low blood levels of cholesterol. Detailed histopathologic evaluation of the skeletal muscle biopsy showed high activity of succinate dehydrogenase, a generalized decrease of COX activity, and abundant ragged-red fibers. Electron microscopic studies revealed multiple mitochondrial abnormalities in lymphocytes and monocytes, in the striated muscle, and in the postmortem samples (muscle, heart, liver, and brain). Biochemical analysis showed a pronounced and constant lactic acidosis, and abnormal urinary organic acid excretion (unchanged in the fasting and postprandial states). In addition, in CSF there was a marked increase of lactate and beta-hydroxybutyrate (beta-HOB) and also a high systemic ratio beta-HOB/acetoacetate. Enzymatic assay of the respiratory chain in biopsied muscle showed 10% of complex I activity and 24% of complex IV activity compared with controls. Molecular studies of the mitochondrial genome revealed an A to G mutation at nucleotide pair 3243 in mitochondrial DNA, a well-known pathogenetic mutation (MELAS mutation) in all the patient's tissues and also in the blood specimens of the probands mother and sibs (4 of 5). The diagnosis of MELAS mutation was reinforced by the absence of an identifiable mutation in the X-linked G4.5 gene of the propositus. The present observation gives additional evidence of the variable clinical expression of mtDNA mutations in humans and demonstrates that all clinical variants deserve adequate investigation to establish a primary defect. It also suggests adding Barth-like syndrome to the list of phenotypes with the MELAS mutation.
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PMID:Barth's syndrome-like disorder: a new phenotype with a maternally inherited A3243G substitution of mitochondrial DNA (MELAS mutation). 1124 64

Huntington's disease (HD) has a mitochondrial dysfunction causing the vulnerability to the excitotoxicity and activations of multiple cell death pathways. Recent evidences suggest that the hematopoietic cytokine, granulocyte-colony stimulating factor (G-CSF), exerts pleiotropic neuroprotection in acute neural injury with activating various survival pathways. Thus, we investigated whether G-CSF can modulate neurodegeneration in an HD animal model induced by 3-nitropropionic acid (3NP), which inhibits mitochondrial succinate dehydrogenase complex II. Either G-CSF (50 microg/kg/day) or saline (as vehicle) was administered intraperitoneally for 5 days with 3NP (63 mg/kg/day) continuous osmotic pump infusion into male Lewis rats. We measured motor scales (0-8) daily and sacrificed rats at 5 days. We observed that G-CSF receptors were expressed in 3NP-induced degenerating striatum. Rats treated with G-CSF showed less degree of neurologic deficits. In the G-CSF-treated rats, the striatal lesion volume measured by Nissl staining, TUNEL+ apoptotic cells, Fluorojade C+ degenerating neurons, and c-Jun+ cells were all decreased. In western blotting, G-CSF activated survival pathways including p-ERK, p-eNOS, p-STAT3, and p-Akt. In summary, G-CSF was found to have neuroprotective effects and save striatal cells through activations of survival pathways in the 3NP-induced striatal degeneration model for HD.
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PMID:Granulocyte-colony stimulating factor attenuates striatal degeneration with activating survival pathways in 3-nitropropionic acid model of Huntington's disease. 1816 68

Mitochondrial quality control, which is crucial for maintaining cellular homeostasis, has been considered to be achieved exclusively through mitophagy. Here we report an alternative mitochondrial quality control pathway mediated by extracellular mitochondria release. By performing time-lapse confocal imaging on a stable cell line with fluorescent-labeled mitochondria, we observed release of mitochondria from cells into the extracellular space. Correlative light-electron microscopy revealed that majority of the extracellular mitochondria are in free form and, on rare occasions, some are enclosed in membrane-surrounded vesicles. Rotenone- and carbonyl cyanide m-chlorophenylhydrazone-induced mitochondrial quality impairment promotes the extracellular release of depolarized mitochondria. Overexpression of PRKN (parkin RBR E3 ubiquitin protein ligase), which has a pivotal role in mitophagy regulation, suppresses the extracellular mitochondria release under basal and stress condition, whereas its knockdown exacerbates it. Correspondingly, overexpression of PRKN-independent mitophagy regulators, BNIP3 (BCL2 interacting protein 3) and BNIP3L/NIX (BCL2 interacting protein 3 like), suppress extracellular mitochondria release. Autophagy-deficient cell lines show elevated extracellular mitochondria release. These results imply that perturbation of mitophagy pathway prompts mitochondria expulsion. Presence of mitochondrial protein can also be detected in mouse sera. Sera of PRKN-deficient mice contain higher level of mitochondrial protein compared to that of wild-type mice. More importantly, fibroblasts and cerebrospinal fluid samples from Parkinson disease patients carrying loss-of-function PRKN mutations show increased extracellular mitochondria compared to control subjects, providing evidence in a clinical context. Taken together, our findings suggest that extracellular mitochondria release is a comparable yet distinct quality control pathway from conventional mitophagy. Abbreviations: ACTB: actin beta; ANXA5: annexin A5; ATP5F1A/ATP5A: ATP synthase F1 subunit alpha; ATG: autophagy related; BNIP3: BCL2 interacting protein 3; BNIP3L/NIX: BCL2 interacting protein 3 like; CCCP: carbonyl cyanide m-chlorophenylhydrazone; CM: conditioned media; CSF: cerebrospinal fluid; DMSO: dimethyl sulfoxide; EM: electron microscopy; HSPD1/Hsp60: heat shock protein family D (Hsp60) member 1; KD: knockdown; KO: knockout; MAP1LC3A/LC3: microtubule associated protein 1 light chain 3 alpha; MT-CO1: mitochondrially encoded cytochrome c oxidase I; NDUFB8: NADH:ubiquinone oxidoreductase subunit B8; OE: overexpression; OPA1: OPA1 mitochondrial dynamin like GTPase; OXPHOS: oxidative phosphorylation; PBS: phosphate-buffered saline; PB: phosphate buffer; PD: Parkinson disease; PINK1: PTEN induced kinase 1; PRKN: parkin RBR E3 ubiquitin protein ligase; RB1CC1/FIP200: RB1 inducible coiled-coil 1; SDHB: succinate dehydrogenase complex iron sulfur subunit B; TOMM20: translocase of outer mitochondrial membrane 20; TOMM40: translocase of outer mitochondrial membrane 40; UQCRC2: ubiquinol-cytochrome c reductase core protein 2; WT: wild-type.
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PMID:Alternative mitochondrial quality control mediated by extracellular release. 3321 72