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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2002-9-4
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/GRASP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Grip1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA,
http://linkedlifedata.com/resource/pubmed/chemical/ras Guanine Nucleotide Exchange...
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pubmed:status |
MEDLINE
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pubmed:issn |
0306-4522
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2002 IBRO
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pubmed:issnType |
Print
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pubmed:volume |
114
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
217-27
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12207967-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12207967-Animals,
pubmed-meshheading:12207967-Animals, Newborn,
pubmed-meshheading:12207967-Antibody Specificity,
pubmed-meshheading:12207967-Brain,
pubmed-meshheading:12207967-Brain Ischemia,
pubmed-meshheading:12207967-Carrier Proteins,
pubmed-meshheading:12207967-Caspase 3,
pubmed-meshheading:12207967-Caspases,
pubmed-meshheading:12207967-Catalytic Domain,
pubmed-meshheading:12207967-Cell Death,
pubmed-meshheading:12207967-Cells, Cultured,
pubmed-meshheading:12207967-Functional Laterality,
pubmed-meshheading:12207967-Immunohistochemistry,
pubmed-meshheading:12207967-Infarction, Middle Cerebral Artery,
pubmed-meshheading:12207967-Membrane Proteins,
pubmed-meshheading:12207967-Mice,
pubmed-meshheading:12207967-Neostriatum,
pubmed-meshheading:12207967-Nerve Tissue Proteins,
pubmed-meshheading:12207967-Neurons,
pubmed-meshheading:12207967-Protein Structure, Tertiary,
pubmed-meshheading:12207967-Receptors, AMPA,
pubmed-meshheading:12207967-ras Guanine Nucleotide Exchange Factors
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pubmed:year |
2002
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pubmed:articleTitle |
Physiological and pathological caspase cleavage of the neuronal RasGEF GRASP-1 as detected using a cleavage site-specific antibody.
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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.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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