Molecular and chemical neuropathology最新文献_第2页

The impact of diabetes on CNS. Role of bioenergetic defects. 糖尿病对中枢神经系统的影响生物能量缺陷的作用。

Molecular and chemical neuropathology Pub Date : 1998-08-01 DOI: 10.1007/BF02815119

G Kaur, S K Bhardwaj

引用次数: 18

Localization of GTPase-activating protein-(GAP) like immunoreactivity in mouse cerebral regions. 小鼠脑区gtpase激活蛋白(GAP)样免疫反应的定位。

Molecular and chemical neuropathology Pub Date : 1998-08-01 DOI: 10.1007/BF02815122

M Namima, K Takeuchi, Y Watanabe, M Yamano, M Saito, H Sasa, K Okamoto

引用次数: 3

Molecular and chemical neuropathology Pub Date : 1998-08-01 DOI: 10.1007/BF02815113

K A Skau, C G Triplett

引用次数: 8

Expression and regulation of complement C1q by human THP-1-derived macrophages. 人thp -1源性巨噬细胞对补体C1q的表达和调控。

Molecular and chemical neuropathology Pub Date : 1998-06-01 DOI: 10.1007/BF02815080

D G Walker

引用次数: 35

Dephosphorylation of tau during transient forebrain ischemia in the rat. 大鼠短暂性前脑缺血过程中tau蛋白的去磷酸化。

Molecular and chemical neuropathology Pub Date : 1998-06-01 DOI: 10.1007/BF02815073

D A Shackelford, R Y Yeh

{"title":"Dephosphorylation of tau during transient forebrain ischemia in the rat.","authors":"D A Shackelford, R Y Yeh","doi":"10.1007/BF02815073","DOIUrl":"https://doi.org/10.1007/BF02815073","url":null,"abstract":"The effect of transient cerebral ischemia on phosphorylation of the microtubule-associated protein (MAP) tau was investigated using the rat four-vessel occlusion model. Phosphorylation of tau is proposed to regulate its binding to microtubules, influencing the dynamics of microtubule assembly necessary for axonal growth and neurite plasticity. In this study, tau was rapidly dephosphorylated during ischemia in the hippocampus, neocortex, and striatum. Dephosphorylation of tau was observed within 5 min of occlusion and increased after 15 min in all three brain regions, regardless of their relative vulnerability to the insult. Thus, dephosphorylation of tau is an early marker of ischemia and precedes the occlusion time required to cause extensive neuronal cell death in this model. On restoration of blood flow for a little as 15 min, tau was phosphorylated at a site(s) that causes a reduction in its electrophoretic mobility. The dephosphorylation/phosphorylation of tau may alter its distribution between axon and cell body, and affect its susceptibility to proteolysis. These changes would be expected to influence microtubule stability, possibly contributing to disruption of axonal transport, but also allowing neurite remodeling in a regenerative response.","PeriodicalId":18736,"journal":{"name":"Molecular and chemical neuropathology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02815073","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21197201","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}

引用次数: 40

Determination of ammonia in cerebrospinal fluid using the indophenol direct method. 吲哚酚直接法测定脑脊液中氨。

Molecular and chemical neuropathology Pub Date : 1998-06-01 DOI: 10.1007/BF02815078

J R Huizenga, A W Teelken, A Tangerman, A E de Jager, C H Gips, P L Jansen

引用次数: 12

Aluminum but not iron treatment induces pro-oxidant events in the rat brain. 铝处理而不是铁处理在大鼠大脑中诱导促氧化事件。

Molecular and chemical neuropathology Pub Date : 1998-06-01 DOI: 10.1007/BF02815081

S C Bondy, S F Ali, S Guo-Ross

{"title":"Aluminum but not iron treatment induces pro-oxidant events in the rat brain.","authors":"S C Bondy, S F Ali, S Guo-Ross","doi":"10.1007/BF02815081","DOIUrl":"https://doi.org/10.1007/BF02815081","url":null,"abstract":"In an attempt to delineate the capacity of aluminum (Al) to promote pro-oxidant events, several indices of oxidative stress have been determined in brains and livers of rats exposed to an Al salt, either alone or in combination with an iron (Fe) compound. Treatment with Al over a 3-wk period increased both cortical levels of glutathione (GSH) and the rates of generation of reactive oxygen species (ROS). Dosing with an Fe compound resulted in no parallel changes, and concurrent exposure to Fe together with Al prevented these elevations. Both Fe and Al dosing elevated glutamine synthetase activity in the cortex. Levels of creatine kinase, another enzyme susceptible to oxidative stress, were also elevated in cortices of Al-treated rats. These data are in contrast to the changes found in liver fractions where exposure to Fe greatly enhanced hepatic pro-oxidant events as judged by changes in all three of the test indices used. Concurrent treatment with Al did not potentiate the pro-oxidant effects of Fe in liver. Al treatment had very minor effects on hepatic parameters of oxidative events. The results suggest that the presence of Al may exert deleterious pro-oxidant changes within the brain, which may be related to induction of oxidant species. These changes are tissue-specific and appear to be independent of any promotion of pro-oxidant status induced by exogenous Fe.","PeriodicalId":18736,"journal":{"name":"Molecular and chemical neuropathology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02815081","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21197163","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}

引用次数: 52

Decreased serotonin2A receptors in Brodmann's area 9 from schizophrenic subjects. A pathological or pharmacological phenomenon? 精神分裂症患者布罗德曼9区血清素2a受体减少。是病理现象还是药理现象?

Molecular and chemical neuropathology Pub Date : 1998-06-01 DOI: 10.1007/BF02815075

B Dean, W Hayes, C Hill, D Copolov

引用次数: 39

Effect of starvation and insulin-induced hypoglycemia on oxidative stress scavenger system and electron transport chain complexes from rat brain, liver, and kidney. 饥饿和胰岛素诱导的低血糖对大鼠脑、肝、肾氧化应激清除系统和电子传递链复合物的影响。

Molecular and chemical neuropathology Pub Date : 1998-06-01 DOI: 10.1007/BF02815077

S K Bhardwaj, M L Sharma, G Gulati, A Chhabra, R Kaushik, P Sharma, G Kaur

{"title":"Effect of starvation and insulin-induced hypoglycemia on oxidative stress scavenger system and electron transport chain complexes from rat brain, liver, and kidney.","authors":"S K Bhardwaj, M L Sharma, G Gulati, A Chhabra, R Kaushik, P Sharma, G Kaur","doi":"10.1007/BF02815077","DOIUrl":"https://doi.org/10.1007/BF02815077","url":null,"abstract":"Considerable evidence suggests that oxidative stress plays an important role in tissue damage associated with hypoglycemia and other metabolic disorders. The altered brain neurotransmitters metabolism, cerebral electrolyte contents, and impaired blood-brain barrier function may contribute to CNS dysfunction in hypoglycemia. The present study elucidates the effect of starvation and insulin-induced hypoglycemia on the free radical scavanger system--reduced glutathione (GSH) content, glutathione S-transferase (GST), glutathione peroxidase (GPx), glutathione reductase (GR), gamma-glutamyl transpeptidase (gamma-GTP), gamma-glutamyl cystein synthetase (gamma-GCS), catalase and superoxide dismutase (SOD), and mitochondrial electron transport chain (ETC) complexes I-IV from three different regions of rat brain, namely cerebral hemispheres (CH), cerebellum (CB), and brainstem (BS). Peripheral organs, such as liver and kidney, were also studied. Significant changes in these enzymic activities were observed. The analysis of such alterations is important in ultimately determining the basis of neuronal dysfunction during metabolic stress conditions, such as hypoglycemia, and also defining the nature of these changes may help to develop therapeutic means to cure metabolically stressed tissues.","PeriodicalId":18736,"journal":{"name":"Molecular and chemical neuropathology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02815077","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21197204","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}

引用次数: 33

Weak binding and removal of extrinsic proteinase activities of myelin membranes. 髓鞘膜外蛋白酶活性的弱结合和去除。

Molecular and chemical neuropathology Pub Date : 1998-06-01 DOI: 10.1007/BF02815079

U Haas, H H Berlet

{"title":"Weak binding and removal of extrinsic proteinase activities of myelin membranes.","authors":"U Haas, H H Berlet","doi":"10.1007/BF02815079","DOIUrl":"https://doi.org/10.1007/BF02815079","url":null,"abstract":"The concurrent release of myelin basic protein (MBP) and extrinsic proteinases from isolated myelin membranes by aqueous solvents of high ionic strength is considered circumstantial evidence of a presumptive mutual interaction in situ. The joint release of proteins and proteinases from myelin membranes of bovine brain, depending on the ionic strength of aqueous solvents, was therefore examined; 25 mM Tris buffer released an average 1.4% of total myelin protein. It was attributable to about 25 different electrophoretic bands, but no apparent MBP. However, the extract potently mediated the limited proteolysis of added MBP at pH 4.0, 5.6, and 9.0. Because of the pH and the effects of specific inhibitors, proteolysis appears to be owing to activities of cathepsin B and D, and an alkaline metalloproteinase. The subsequent extraction of myelin membranes with buffered 300 mM NaCl released an additional 20% of total myelin protein, mainly MBP. The extracts, unlike those of untreated myelin membranes, no longer cleaved MBP at pH 5.6 and 9.0, and did so only slightly at pH 4.0. The results indicate that the bulk of soluble myelin-associated proteinases is much less tightly bound than MBP. The weak binding of the former and the prevalence of lysosomal cathepsin B- and D-like activities suggest that during their isolation, myelin membranes may adsorb soluble cellular proteins of tissue homogenates. At any rate the washing of myelin membranes with dilute buffer was found to largely remove soluble proteinase activities that are otherwise associated with salt-soluble MBP of myelin.","PeriodicalId":18736,"journal":{"name":"Molecular and chemical neuropathology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02815079","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21197158","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}

引用次数: 1