High impact information on Cp1

• We have exploited this observation to isolate clones from a Drosophila embryo cDNA library that block DCP-1 caspase-dependent yeast cell death [1].
• We have sequenced the cDNA of a novel Ca(2+)-activated cysteine proteinase (calpain) from the fruit fly, Drosophila melanogaster [2].
• We show that the shrimp cathepsin L (CatL) gene MeCatL has lost all of its five introns [3].
• Immunofluorescence shows that CP1 is localized in small granules, probably lysosomes, in mbn-2 cells [4].
• Cysteine proteinase 1 (CP1), a cathepsin L-like enzyme expressed in the Drosophila melanogaster haemocyte cell line mbn-2 [4].

Biological context of Cp1

• The complete structure of the cysteine proteinase (CP1) gene reveals two large 5' introns as well as a small third intron [5].
• Drosophila cysteine proteinase-1 showed 67% similarity in its amino acid sequence to a lobster cysteine proteinase-3 contained in the digestive juice [6].
• One clone of 1229 bp, with an open reading frame of 1014 bp, was sequenced and found to contain 50-65% amino acid sequence identity with several members of the cathepsin L subfamily of cysteine proteases [7].
• In the present study we used primers designed based on the consensus amino acid motifs flanking the conserved active sites C25 and N175 present in all papain-like cysteine proteinases to amplify by polymerase chain reaction, sequence and characterize two Haemaphysalis longicornis tick cysteine proteinase genes [8].
• A similar phenotype has been reported when one of the effector caspases of Drosophila, Dcp-1, is ectopically expressed during mid-oogenesis with the same Gal4 driver [9].

Associations of Cp1 with chemical compounds

• One of these systems may be based on the occurrence of phytocystatins, cysteine proteinase inhibitors of plant origin, that probably inhibit insect cysteine proteinases involved in digestive functions [6].

Analytical, diagnostic and therapeutic context of Cp1

• In situ hybridization studies for the embryo showed that the mRNA for Drosophila cysteine proteinase-1 was predominantly expressed in the midgut [6].
• Ultrastructural (possession of megasomes), biochemical (cysteine proteinase activity and gelatin SDS-PAGE banding pattern) and infectivity (in vivo) data are presented which show the close similarity of the cultured forms to lesion amastigotes [10].
• Molecular cloning of two Haemaphysalis longicornis cathepsin L-like cysteine proteinase genes [8].

References