Literature summary for 3.4.23.5 extracted from

Gui, Z.Z.; Lee, K.S.; Kim, B.Y.; Choi, Y.S.; Wei, Y.D.; Choo, Y.M.; Kang, P.D.; Yoon, H.J.; Kim, I.; Je, Y.H.; Seo, S.J.; Lee, S.M.; Guo, X.; Sohn, H.D.; Jin, B.R.
Functional role of aspartic proteinase cathepsin D in insect metamorphosis (2006), BMC Dev. Biol., 6, 49.

Search for more literature for 3.4.23.5

Application

Application	Comment	Organism
medicine	it is shown that BmCatD is critically involved in the programmed cell death of the larval fat body and larval gut in silkworm metamorphosis	Bombyx mori

Cloned(Commentary)

Cloned (Comment)	Organism
baculovirus expression vector system, using the Autographa californica nucleopolyhedrovirus (AcNPV) and insect cell line Sf9, is employed for the production of recombinant BmCatD protein	Bombyx mori

Protein Variants

Protein Variants	Comment	Organism
additional information	RNA interference-mediated BmCatD knock-down inhibits programmed cell death of the larval fat body, resulting in the arrest of larval-pupal transformation. BmCatD RNA interference also inhibits the programmed cell death of larval gut during pupal stage	Bombyx mori

Organism

Organism	UniProt	Comment	Textmining
Bombyx mori	Q7Z1E4	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
larval integument	cathepsin D of the silkworm Bombyx mori (BmCatD) is ecdysone-induced, differentially and spatially expressed in the larval fat body of the final instar and in the larval gut of pupal stage, and its expression leads to programmed cell death. Furthermore, BmCatD is highly induced in the fat body of baculovirus-infected Bombyx mori larvae	Bombyx mori	-

Synonyms

Synonyms	Comment	Organism
BmCatD	-	Bombyx mori
cathepsin D	-	Bombyx mori

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Release 2023.1 (January 2023)