2012
DOI: 10.1016/j.bbrc.2012.07.068
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Identification of ecdysone response elements (EcREs) in the Bombyx mori cathepsin D promoter

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Cited by 14 publications
(6 citation statements)
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“…It has been confirmed that Bombyx cathepsin B (BmCatB) is involved in the PCD of fat body, as inhibition of BmCatB and Bombyx cathepsin L (BmCatL)‐like (BmCatLL) activities blocks the histolysis of silk gland during Bombyx metamorphosis (Shiba et al ., ; Cai et al ., ). BmCatB and BmCatL are both ecdysone‐responsive, and ecdysone‐response elements (EcREs) exist in their respective promoters (Yu et al ., ; Cai et al ., ). Bombyx fibroinase (BmBcp), another BmCatL‐like protease, extracted from the silk gland, is confirmed to hydrolyse the fibroin molecule and the heavy chain of Bombyx fibroin by acquiring purification protein from silk glands, and its enzymatic properties have been analysed (Sumida et al ., ; Sutthikhum et al ., ; Watanabe et al ., ).…”
Section: Introductionmentioning
confidence: 98%
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“…It has been confirmed that Bombyx cathepsin B (BmCatB) is involved in the PCD of fat body, as inhibition of BmCatB and Bombyx cathepsin L (BmCatL)‐like (BmCatLL) activities blocks the histolysis of silk gland during Bombyx metamorphosis (Shiba et al ., ; Cai et al ., ). BmCatB and BmCatL are both ecdysone‐responsive, and ecdysone‐response elements (EcREs) exist in their respective promoters (Yu et al ., ; Cai et al ., ). Bombyx fibroinase (BmBcp), another BmCatL‐like protease, extracted from the silk gland, is confirmed to hydrolyse the fibroin molecule and the heavy chain of Bombyx fibroin by acquiring purification protein from silk glands, and its enzymatic properties have been analysed (Sumida et al ., ; Sutthikhum et al ., ; Watanabe et al ., ).…”
Section: Introductionmentioning
confidence: 98%
“…Cathepsin D and E are the main aspartic-type cathepsins, but only cathepsin D is reported in insects (Saikhedkar et al, 2015). Cathepsin D has physiological functions in PCD of the larval tissues in Bombyx, as well as in the hydrolysis of cysteine peptidase inhibitors in midguts in Dysdercus peruvianus (Wu et al, 2011;Yu et al, 2012;Pimentel et al, 2017). Additionally, cathepsin D is also involved in vitellogenin production and degradation in mosquitoes and fat body proteins histolysis in Ceratitis capitata and Bombyx (Cho & Raikhel, 1992;Rabossi et al, 2004;Gui et al, 2006).…”
Section: Introductionmentioning
confidence: 99%
“…For example, cathepsin L is a proteolytic processing enzyme for the production of active enkephalin (Yasothornsrikul et al, 2003). In silkworm, 20E was found to up-regulated transcript level of cathepsin D in the larval fat body (Gui et al, 2006), and the ecdysone response element (EcREs) was characterized and identified in the promoter region (Yu et al, 2012(Yu et al, , 2014. In the present study, BmCathepsin O was remarkably induced by 20E (Fig.…”
Section: Discussionmentioning
confidence: 50%
“…Several homologs and cDNA sequences of cathepsin B and D have been identified from silkworm genome, studies showed that cathepsin B was not only critical for normal development of silkworm, especially in fat body and posterior silk gland (Wang et al, 2008b), but also involved in the programmed cell death of the fat body during silkworm metamorphosis (Lee et al, 2009). Cathepsin D expression could be induced by 20-hydroxyecdysone (20E) (Yu et al, 2012), high temperature and H 2 O 2 , which suggested that cathepsin D also contributed to silkworm metamorphosis (Lee et al, 2009). In this study, a full-length cDNA of cathepsin O from B. mori was first cloned and characterized, and its temporal and spatial expression profiles were evaluated.…”
Section: Introductionmentioning
confidence: 99%
“…The ecdysteroid 20 hydroxyecdysone (20-OH-E) interacts with ecdysone responsive elements (EcREs) and induces the developmental stage specific expression of proteases (Ashburner, 1974;Thummel, 2002). Three different EcREs were identified in the region À109 to À99, À836 to À826 and À856 to À846 upstream of transcription start site of CathD promoter of B. mori (Yu et al, 2012).…”
Section: Indispensability and Functionality Of Cathepsins In Insect Dmentioning
confidence: 99%