Isolation and characterization of insect PC2-like prohormone convertase cDNA
Endoproteolytic processing of large precursor molecules at basic amino acid residues plays an important role in the maturation of many hormones, neuropeptides and other regulatory proteins. Enzymes performing these reactions are designated as prohormone or proprotein convertases and belong to the su...
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Published in | Insect molecular biology Vol. 8; no. 3; pp. 305 - 310 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Oxford BSL
Blackwell Science Ltd
01.08.1999
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Subjects | |
Online Access | Get full text |
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Summary: | Endoproteolytic processing of large precursor molecules at basic amino acid residues plays an important role in the maturation of many hormones, neuropeptides and other regulatory proteins. Enzymes performing these reactions are designated as prohormone or proprotein convertases and belong to the subtilisin family of serine proteases. The screening of a larval cDNA library of the sheep blowfly Lucilia cuprina resulted in the isolation of two cDNAs encoding a PC2-like prohormone convertase. The predicted 675 amino acid preproprotein (LcuPC2) exhibits its highest identity to invertebrate and vertebrate prohormone convertase 2 homologues, and a noticeably lower identity to the so far known insect furin-like prohormone convertases of Drosophila melanogaster and Aedes aegypti. In Northern blot experiments a signal at 2.5 kb could be detected. |
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Bibliography: | ArticleID:IMB113 ark:/67375/WNG-6WXJD8CX-C istex:9877235CBDA362B3D64F3F8AD4071B840E6B05F5 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0962-1075 1365-2583 |
DOI: | 10.1046/j.1365-2583.1999.83113.x |