Neurochemical pathology最新文献

{"title":"Enhanced synthesis of prostaglandins and hydroxyeicosatetraenoic acids in retina from a canine model of Batten's disease.","authors":"D L Birkle,&nbsp;T S Reddy,&nbsp;D Armstrong,&nbsp;N G Bazan","doi":"10.1007/BF03160187","DOIUrl":"https://doi.org/10.1007/BF03160187","url":null,"abstract":"<p><p>The metabolism of [1-14C]arachidonic acid (20:4, n-6) was studied in intact retina and retinal pigment epithelial cells from normal English setters and English setters affected with hereditary canine ceroid lipofuscinosis. Acylation of arachidonic acid into membrane glycerolipids and oxygenation by lipoxygenase and cyclooxygenase to eicosanoids were measured by radiochromatographic techniques. In addition, the histopathology of accumulated ceroid particles in retinal ganglion cells and pigment epithelial cells was studied by electron microscopy. Synthesis of prostaglandins and hydroxyeicosatetraenoic acids was increased in canine ceroid lipofuscinosis retina, but not in retinal pigment epithelium. Prostaglandin D2, the putative neuronal eicosanoid, was increased nearly eightfold, whereas other eicosanoids increased two- to threefold. Ultrastructural studies revealed accumulation of ceroid and deterioration of neuronal and pigment epithelial cell architecture. These experiments demonstrate that, although lipopigment accumulates in both tissues, alterations of eicosanoid synthesis are specific for the retina, a neuronal tissue. The specific increase in prostaglandin D2 and the specificity of changes for the retina indicate that enhanced eicosanoid synthesis may be a result of an impairment of the control of oxygenation of arachidonic acid in neurons.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"4 2","pages":"77-88"},"PeriodicalIF":0.0,"publicationDate":"1986-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF03160187","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14843555","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Neuron-specific gamma-enolase derived from human glioma.","authors":"M Kuramitsu,&nbsp;H Sawa,&nbsp;I Takeshita,&nbsp;T Iwaki,&nbsp;K Kato","doi":"10.1007/BF03160188","DOIUrl":"https://doi.org/10.1007/BF03160188","url":null,"abstract":"<p><p>Neuron-specific gamma-enolase in human neurogenic tumors, including gliomas, transplanted gliomas, and permanent human glioma cell lines, was studied quantitatively, using newly established enzyme immunoassay methods, together with immunostaining of the tissue and cell preparations. A significantly high level of gamma-enolase was found in some glioblastomas, astrocytomas and oligodendrogliomas as well as medulloblastomas. Glioblastomas transplanted into mice and cultured cell lines derived from the same origins, as well as the permanent human glioma cell lines, also contained gamma-enolase, although the contents were low compared with findings in the original tumor tissues. Immunohistochemically, gamma-enolase stained intensely in the glioblastomatous cells. Serum gamma-enolase concentrations in some patients with gliomas and those of all the transplanted mice were enhanced. The serum gamma-enolase levels in the mice correlated well with size of the transplanted tumor tissues. These results indicate that neuron-specific gamma-enolase is produced in some neurogenic tumors of nonneuronal origin, therefore, serum gamma-enolase may be a useful biomarker for monitoring the extent of disease in patients with gliomas.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"4 2","pages":"89-105"},"PeriodicalIF":0.0,"publicationDate":"1986-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF03160188","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14148293","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Severity of demyelination in vivo correlates with serum myelination inhibition activity in guinea pigs having a new form of experimental allergic encephalomyelitis.","authors":"D N Bourdette,&nbsp;B F Driscoll,&nbsp;F J Seil,&nbsp;M W Kies,&nbsp;E C Alvord","doi":"10.1007/BF02834294","DOIUrl":"https://doi.org/10.1007/BF02834294","url":null,"abstract":"<p><p>Guinea pigs received a suboptimal transfer of lymphocytes sensitized to myelin basic protein (BP) and were then immunized with guinea pig BP, BP plus chicken brain or chicken myelin, or chicken brain alone. Sera from these animals were tested for the presence of myelinotoxic antibodies, as detected by the myelination inhibition assay. Myelination inhibition activity correlated with the histologic severity of demyelination.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"4 1","pages":"1-9"},"PeriodicalIF":0.0,"publicationDate":"1986-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02834294","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13570830","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mitochondrial dysfunction and spinocerebellar degenerations.","authors":"J M Cedarbaum,&nbsp;J P Blass","doi":"10.1007/BF02834298","DOIUrl":"https://doi.org/10.1007/BF02834298","url":null,"abstract":"<p><p>A simplified classification of the spinocerebellar degenerations is proposed. Axonal ataxias include Friedreich's ataxia and other conditions involving, primarily, neurons with very long axons. Multiple system degenerations include the various olivopontocerebellar atrophies and related disorders. Ataxic encephalopathies are diffuse diseases of the nervous system in which ataxia is a prominent clinical feature. Several lines of data suggest that mitochondrial damage is a common mechanism in the spinocerebellar degenerations. Reasonable pathophysiological mechanisms can be invoked, linking mitochondrial damage to the observed pathologies (including the many cases of intermediate on variant forms).</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"4 1","pages":"43-63"},"PeriodicalIF":0.0,"publicationDate":"1986-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02834298","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14644721","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Brain glutathione peroxidase in neurodegenerative disorders.","authors":"S J Kish,&nbsp;C L Morito,&nbsp;O Hornykiewicz","doi":"10.1007/BF02834296","DOIUrl":"https://doi.org/10.1007/BF02834296","url":null,"abstract":"<p><p>Glutathione peroxidase is an enzyme that couples the oxidation of reduced glutathione to the detoxification of peroxides. Alterations in the activity of this component of the glutathione oxygen scavenging system in brain have been reported in several conditions associated with oxidative challenge and/or cellular damage. We measured the activity of glutathione peroxidase in autopsied brain regions of neurologically normal adults and in brain of patients with primary degenerative disorder Alzheimer's type (AD/SDAT), as well as two other neurodegenerative disorders, namely Huntington's disease and striatonigral degeneration. No significant alterations in enzyme activity were observed in morphologically normal or abnormal brain regions. Our results suggest that in the three brain disorders studied, the neuronal cell loss is unlikely to result from reduced activity of brain glutathione peroxidase, and that a significant compensatory increase in this brain enzyme, consequent to the degenerative processes, does not occur.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"4 1","pages":"23-8"},"PeriodicalIF":0.0,"publicationDate":"1986-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02834296","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14075361","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biochemical and physicochemical determinations in a premyelin fraction obtained by zonal centrifugation in normal mouse and in dysmyelinating mutants (quaking, shiverer, and myelin-deficient).","authors":"J M Bourre,&nbsp;F Boiron,&nbsp;C Cassagne,&nbsp;O Dumont,&nbsp;F Leterrier,&nbsp;H Metzger,&nbsp;J Viret","doi":"10.1007/BF02834297","DOIUrl":"https://doi.org/10.1007/BF02834297","url":null,"abstract":"<p><p>Myelin and premyelin material denser than myelin were obtained from quaking (Qk), shiverer (Shi), and myelin-deficient (mld) mutant and control mice, using zonal centrifugation on zonal rotor. On these fractions, we performed biochemical analysis (lipids and fatty acid), and, in parallel, we determined the physical structure of membranes by the spin-label method. The hyperfine splitting constant (2 Tll) was used to determine the order of membranes and their rigidity, and frequency of rotation (Vc) was used to measure fluidity. In control mice, the premyelin material contained a lesser amount of sphingolipids than pure myelin, but the relative proportions between hydroxy- and nonhydroxy-cerebroside and sulfatides were similar in the premyelin material and in pure myelin. The premyelin material contained half the alkanes found in the pure myelin and much less very-long-chain fatty acids. The (2 Tll) was lower in the premyelin material, but the (Vc) was similar in myelin and premyelin material. In mutants, the amount of material recovered in the premyelin fraction was reduced in qk, and increased in both shi and mld. The relative amount of sphingolipids were normal in mld, but not in shi mutants, especially in cerebrosides formed with alpha-hydroxylated fatty acids and sulfatides formed with unsubstituted fatty acids. The absolute amounts of sphingolipids were nearly normal in both shi and mld. In the premyelin fraction from qk mutants, both relative and absolute amounts of sphingolipids were drastically altered. In percentage, cerebrosides and sulfatides formed with nonhydroxyfatty acids were dramatically reduced, and, conversely, cerebrosides and sulfatides formed with hydroxyfatty acids were increased. In terms of absolute amount, only cerebrosides and sulfatides formed with nonhydroxyfatty acids were dramatically reduced. In the premyelin fraction, polyunsaturated fatty acids were increased in shi and mld, but decreased in qk. In this mutant, lignoceric (24:0) and nervonic (24:1) acids were drastically reduced. The amount of alkanes in the premylin material from qk and mld was reduced by 50%. The shi fraction was nearly free of alkanes. The maximal apparent coupling constant (hyperfine splitting constant, 2 Tll) was not affected in the mld and qk mutant, but was reduced in the shi mutant premyelin fraction. The Vc was dramatically increased in the qk, slightly decreased in the shi, and close to control in the mld. This work provides additional data on premyelin material prepared in various neurological mutants using continuous gradients in zonal rotor.(ABSTRACT TRUNCATED AT 400 WORDS)</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"4 1","pages":"29-42"},"PeriodicalIF":0.0,"publicationDate":"1986-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02834297","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14145359","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mechanism of demyelination in the guinea pig. Separate sensitization with encephalitogenic myelin basic protein and nonencephalitogenic brain components.","authors":"B F Driscoll,&nbsp;J Kira,&nbsp;M W Kies,&nbsp;E C Alvord","doi":"10.1007/BF02834295","DOIUrl":"https://doi.org/10.1007/BF02834295","url":null,"abstract":"<p><p>Experimental allergic encephalomyelitis (EAE), accompanied by demyelinating central nervous system (CNS) lesions, can be induced in guinea pigs sensitized with whole guinea pig CNS tissue, but not in animals sensitized with purified myelin basic protein (BP). This type of chronic demyelinating EAE is presumably a result of a combination of a cell-mediated immune response to the encephalitogenic BP and a separate response to other nonencephalitogenic CNS antigens. We report here that demyelinating EAE can be induced when separate sensitizations are used to induce a cell-mediated response to BP and a second immune response to nonencephalitogenic CNS antigens. Animals sensitized in separate sites with guinea pig BP and whole chicken brain develop CNS demyelinating lesions. Animals sensitized only to BP or chicken brain do not develop demyelination.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"4 1","pages":"11-22"},"PeriodicalIF":0.0,"publicationDate":"1986-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02834295","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13570831","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The effects of ischemia and CDPamines on Na+, K+-ATPase and acetylcholinesterase activities in rat brain.","authors":"W J Goldberg,&nbsp;R V Dorman,&nbsp;Z Dabrowiecki,&nbsp;L A Horrocks","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cerebral ischemia produced a decrease in Na+, K+-ATPase activity in striatum and cortex; acetylcholinesterase activity was not affected in either region. Pretreatment of the animals with CDPcholine and CDPethanolamine did not prevent the decline in ATPase activity, suggesting that the accumulation of free fatty acids associated with ischemia is not responsible for these changes. Addition of exogenous diacylglycerols to the ATPase assay mixture produced an inhibition of the enzyme similar in magnitude to that observed in tissue samples from ischemic brain. These results support our hypothesis that the local accumulation of diacylglycerols following ischemia is involved in the observed changes in enzymatic activity.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"3 4","pages":"237-48"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14141233","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Arachidonic acid and other long-chain fatty acids in canine ceroid lipofuscinosis. Distribution in glycerolipids, metabolism, and pathophysiological correlations.","authors":"T S Reddy,&nbsp;D Armstrong,&nbsp;N G Bazan","doi":"10.1007/BF02834282","DOIUrl":"https://doi.org/10.1007/BF02834282","url":null,"abstract":"<p><p>Dogs with canine ceroid lipofuscinosis (CCL)+ show an abnormal EEG as early as 5 mo of age and exhibited either severe disorganization or very low amplitudes by 24 mo. Ceroid particles accumulate with age and, within neurons, have a unique characteristic appearance consisting of lamellar patterns enclosed by a single unit membrane. Although the etiology of their formation has not been fully elucidated, isolated particles are enriched in phospholipids. Our present studies have examined microsomal enzymes involved in phospholipid synthesis and turnover and demonstrate that the acyl group composition of cerebral lipids from animals with CCL is similar to that from controls. However, the activation of palmitic, linoleic, arachidonic, and docosahexaenoic acids into their Coenzyme A thiol ester forms was significantly lower in cerebral and cerebellar microsomes of the diseased dogs than in those of the controls. In addition, the incorporation of arachidonic acid into phospholipids was significantly decreased in affected animals. These results suggest that the metabolism of arachidonic acid plays an important role in the pathogenesis of ceroid lipofuscinosis.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"3 2","pages":"83-97"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02834282","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15160842","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Axonal transport of cytoskeletal proteins in aluminum toxicity. Aluminum toxicity and axonal transport.","authors":"K S Kosik,&nbsp;A H McCluskey,&nbsp;F X Walsh,&nbsp;D J Selkoe","doi":"10.1007/BF02834283","DOIUrl":"https://doi.org/10.1007/BF02834283","url":null,"abstract":"<p><p>Aluminum administration in certain species results in the accumulation of neurofilament bundles within the neuronal perikaryon and the proximal neuronal processes. The study presented here was designed to investigate how aluminum exerts its effects on the neuronal cytoskeleton. Microinjections of AlCl3 were administered directly to the rabbit lumbar spinal cord; the injections resulted in the accumulation of neurofilament bundles in upwards of 80% of the anterior horn cells. Approximately 7 d later, [35S]methionine was administered to the same region, and exactly 14 d after the radioactive pulse the animals were sacrificed. Sequential 3-mm segments of the sciatic nerves beginning at the root exit zone were processed for gel electrophoresis and fluorography. The counts incorporated into gel bands representing actin, tubulin, and the neurofilament (NF) subunits were determined for each segment, and a distribution curve for the pooled control and pooled aluminum-treated rabbits was constructed. The distribution curves for the two groups, separately analyzed for each cytoskeletal protein, did not significantly differ using an analysis of variance. We conclude that an interruption of slow axonal transport does not occur in this model of aluminum-induced lumbar myelopathy.</p>","PeriodicalId":77753,"journal":{"name":"Neurochemical pathology","volume":"3 2","pages":"99-108"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02834283","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13559607","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}