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Isolation and characterization of insect PC2‐like prohormone convertase cDNA
Author(s) -
Mentrup B.,
Londershausen M.,
Spindler K.D.,
Weidemann W.
Publication year - 1999
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.1999.83113.x
Subject(s) - prohormone convertase , prohormone , furin , biology , proprotein convertases , complementary dna , biochemistry , drosophila melanogaster , kexin , cdna library , serine , proteases , subtilisin , signal peptide , peptide sequence , microbiology and biotechnology , gene , enzyme , hormone , lipoprotein , ldl receptor , cholesterol
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.