Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2005-4-27
pubmed:databankReference
pubmed:abstractText
In many animal species including Xenopus, ovulated eggs possess an intrinsic apoptotic execution system. This program is inhibited for a limited time by some maternal apoptosis inhibitors, although their molecular properties remain uncharacterized. Baculovirus IAP repeat (BIR) family proteins contain evolutionarily conserved BIR domains and play important roles in apoptosis suppression, and are therefore good candidates as maternal apoptosis inhibitors. We identified four maternal BIR family proteins in Xenopus eggs and, using the biochemical advantages of egg extracts, examined their physiological functions. These molecules included two survivin-related proteins, xEIAP/XLX, and a possible ortholog of XIAP named xXIAP. The addition of recombinant xXIAP greatly delayed apoptotic execution, whereas the immunodepletion of endogenous xXIAP significantly accelerated the onset of apoptosis. In contrast, xEIAP/XLX was a poor apoptosis inhibitor, and neither of the survivin orthologs showed anti-apoptotic activity in our assay. Both xEIAP/XLX and xXIAP were degraded by activated caspases, and also by a novel proteolytic system that required the presence of C-terminal RING finger domain but was insensitive to proteasome inhibition. Our data suggest that the regulation of endogenous xXIAP concentration is important for the survival of Xenopus eggs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/BIRC5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Inhibitor of Apoptosis Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/X-Linked Inhibitor of Apoptosis..., http://linkedlifedata.com/resource/pubmed/chemical/XIAP protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1742-464X
pubmed:author
pubmed:issnType
Print
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2237-50
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:15853809-Amino Acid Sequence, pubmed-meshheading:15853809-Animals, pubmed-meshheading:15853809-Apoptosis, pubmed-meshheading:15853809-Female, pubmed-meshheading:15853809-Humans, pubmed-meshheading:15853809-Inhibitor of Apoptosis Proteins, pubmed-meshheading:15853809-Male, pubmed-meshheading:15853809-Microtubule-Associated Proteins, pubmed-meshheading:15853809-Mitogen-Activated Protein Kinases, pubmed-meshheading:15853809-Molecular Sequence Data, pubmed-meshheading:15853809-Neoplasm Proteins, pubmed-meshheading:15853809-Oocytes, pubmed-meshheading:15853809-Phosphoproteins, pubmed-meshheading:15853809-Protein Structure, Tertiary, pubmed-meshheading:15853809-Proteins, pubmed-meshheading:15853809-Recombinant Proteins, pubmed-meshheading:15853809-Sequence Alignment, pubmed-meshheading:15853809-X-Linked Inhibitor of Apoptosis Protein, pubmed-meshheading:15853809-Xenopus Proteins, pubmed-meshheading:15853809-Xenopus laevis
pubmed:year
2005
pubmed:articleTitle
Apoptosis-inhibiting activities of BIR family proteins in Xenopus egg extracts.
pubmed:affiliation
Department of Biochemistry, Toho University School of Medicine, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't