| pubmed-article:19364322 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19364322 | lifeskim:mentions | umls-concept:C0596208 | lld:lifeskim |
| pubmed-article:19364322 | lifeskim:mentions | umls-concept:C0699919 | lld:lifeskim |
| pubmed-article:19364322 | lifeskim:mentions | umls-concept:C0007585 | lld:lifeskim |
| pubmed-article:19364322 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
| pubmed-article:19364322 | lifeskim:mentions | umls-concept:C0728725 | lld:lifeskim |
| pubmed-article:19364322 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:19364322 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:19364322 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:19364322 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:19364322 | pubmed:dateCreated | 2009-4-14 | lld:pubmed |
| pubmed-article:19364322 | pubmed:abstractText | The cysteine proteases caspase-3 and cathepsins are involved in both neuronal plasticity and neuropathology. Using primary neuroglial and glial cerebellar cultures, the pH dependence of cleavage of a synthetic caspase-3 substrate, Ac-DEVD-AMC, was studied. At acidic pH, cathepsin B cleaved Ac-DEVD, this activity being significantly higher than that of caspase-3 at pH 7.4. This activity is blocked by peptide inhibitors of both caspase-3 and cathepsin B. Substitution of culture medium for balanced salt solution stimulated cathepsin B secretion in both types of cultures. Ischemia (oxygen-glucose deprivation) significantly decreased secretion of cathepsin B activities into the culture medium. | lld:pubmed |
| pubmed-article:19364322 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19364322 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19364322 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19364322 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19364322 | pubmed:issn | 1608-3040 | lld:pubmed |
| pubmed-article:19364322 | pubmed:author | pubmed-author:KhaspekovL... | lld:pubmed |
| pubmed-article:19364322 | pubmed:author | pubmed-author:OnufrievM VMV | lld:pubmed |
| pubmed-article:19364322 | pubmed:author | pubmed-author:YakovlevA AAA | lld:pubmed |
| pubmed-article:19364322 | pubmed:author | pubmed-author:GulyaevaN VNV | lld:pubmed |
| pubmed-article:19364322 | pubmed:author | pubmed-author:LyzhinA AAA | lld:pubmed |
| pubmed-article:19364322 | pubmed:author | pubmed-author:StepanichevM... | lld:pubmed |
| pubmed-article:19364322 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19364322 | pubmed:volume | 74 | lld:pubmed |
| pubmed-article:19364322 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19364322 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19364322 | pubmed:pagination | 281-7 | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:meshHeading | pubmed-meshheading:19364322... | lld:pubmed |
| pubmed-article:19364322 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19364322 | pubmed:articleTitle | A secreted caspase-3-substrate-cleaving activity at low pH belongs to cathepsin B: a study on primary brain cell cultures. | lld:pubmed |
| pubmed-article:19364322 | pubmed:affiliation | Institute of Higher Nervous Activity and Neurophysiology, Russian Academy of Sciences, 117485 Moscow, Russia. | lld:pubmed |
| pubmed-article:19364322 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19364322 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
