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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
1992-1-9
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M79452,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M80723,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M80724,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81660,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81661,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81662,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81664,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81665,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81666,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S68023,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S68027
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pubmed:abstractText |
We report a phenomenon previously unknown for oviparous animals; in Aedes aegypti mosquitoes a serine carboxypeptidase is synthesized extraovarially and then internalized by oocytes. The cDNA encoding mosquito vitellogenic carboxypeptidase (VCP) was cloned and sequenced. The VCP cDNA hybridizes to a 1.5-kilobase mRNA present only in the fat body of vitellogenic females. The deduced amino acid sequence of VCP shares significant homology with members of the serine carboxypeptidase family. Binding assays using a serine protease inhibitor, [3H]diisopropyl fluorophosphate, showed that VCP is activated in eggs at the onset of embryonic development. Activation of VCP is associated with the reduction in its size from 53 kDa (inactive proenzyme) to 48 kDa (active enzyme). The active, 48-kDa, form of VCP is maximally present at the middle of embryonic development and disappears by the end.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-1311540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-2106523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-2226439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-2308160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-2351682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-2454229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-2583514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-2820978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-2983426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3028649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3072724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3132106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3136930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3275655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3301004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3342240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3344434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3415699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-3733735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-4587122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-6852022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-7048999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1961751-7108955
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10821-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1961751-Aedes,
pubmed-meshheading:1961751-Amino Acid Sequence,
pubmed-meshheading:1961751-Animals,
pubmed-meshheading:1961751-Base Sequence,
pubmed-meshheading:1961751-Carboxypeptidases,
pubmed-meshheading:1961751-Cloning, Molecular,
pubmed-meshheading:1961751-Embryo, Nonmammalian,
pubmed-meshheading:1961751-Female,
pubmed-meshheading:1961751-Insect Proteins,
pubmed-meshheading:1961751-Isoflurophate,
pubmed-meshheading:1961751-Molecular Sequence Data,
pubmed-meshheading:1961751-Oocytes,
pubmed-meshheading:1961751-Ovary,
pubmed-meshheading:1961751-Polymerase Chain Reaction,
pubmed-meshheading:1961751-Sequence Homology, Nucleic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
An extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos.
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pubmed:affiliation |
Graduate Program in Genetics, Michigan State University, East Lansing 48824.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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