| pubmed-article:12207967 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C0521390 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C1425725 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C1521733 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C0205463 | lld:lifeskim |
| pubmed-article:12207967 | lifeskim:mentions | umls-concept:C0442726 | lld:lifeskim |
| pubmed-article:12207967 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:12207967 | pubmed:dateCreated | 2002-9-4 | lld:pubmed |
| pubmed-article:12207967 | pubmed:abstractText | Caspases are proteases involved in various physiological and pathological processes in the nervous system, including development and pathogenesis. GRASP-1 is a recently identified neuronal substrate of caspase-3-subfamily caspases. It is a Ras-guanine nucleotide exchange factor (RasGEF) that interacts with the glutamate receptor interacting protein (GRIP). This alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor/GRIP protein complex has been proposed to be involved in AMPA receptor synaptic targeting. The caspase-3 cleavage of GRASP-1 separates the N-terminal RasGEF catalytic domain from the C-terminal GRIP-interacting region, potentially disrupting regulation of the RasGEF activity by GRIP. To examine the regulation and regional distribution of the caspase-3 cleavage of GRASP-1 in vivo, we generated a cleavage site-specific antibody, termed CGP, against the cleaved N-terminal fragment of GRASP-1. Using this antibody, we have examined the caspase cleavage of GRASP-1 during postnatal development and following ischemia in mice. We found that caspase cleavage of GRASP-1 occurs in specific brain regions in a time-dependent manner during development and ischemia. This data provides an important account of the brain areas that might require caspase-3 activity in postnatal development and ischemic damage, which has not been documented. It also demonstrates that the CGP antibody is a powerful tool for studying neuronal activity of the caspase-3-subfamily caspases in vivo. | lld:pubmed |
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| pubmed-article:12207967 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12207967 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12207967 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12207967 | pubmed:issn | 0306-4522 | lld:pubmed |
| pubmed-article:12207967 | pubmed:author | pubmed-author:YuRR | lld:pubmed |
| pubmed-article:12207967 | pubmed:author | pubmed-author:HuganirR LRL | lld:pubmed |
| pubmed-article:12207967 | pubmed:author | pubmed-author:HurnP DPD | lld:pubmed |
| pubmed-article:12207967 | pubmed:author | pubmed-author:SAULG BGB2nd | lld:pubmed |
| pubmed-article:12207967 | pubmed:copyrightInfo | Copyright 2002 IBRO | lld:pubmed |
| pubmed-article:12207967 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12207967 | pubmed:volume | 114 | lld:pubmed |
| pubmed-article:12207967 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12207967 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12207967 | pubmed:pagination | 217-27 | lld:pubmed |
| pubmed-article:12207967 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12207967 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12207967 | pubmed:articleTitle | Physiological and pathological caspase cleavage of the neuronal RasGEF GRASP-1 as detected using a cleavage site-specific antibody. | lld:pubmed |
| pubmed-article:12207967 | pubmed:affiliation | Department of Neuroscience, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, 904A PCTB, 725 N. Wolfe Street, Baltimore, MD 21205, USA. | lld:pubmed |
| pubmed-article:12207967 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12207967 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12207967 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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