Cathepsin L participates in the remodeling of the midgut through dissociation of midgut cells and activation of apoptosis via caspase-1

Yang, Cui; Lin, Xian-Wu; Xu, Wei‐Hua

doi:10.1016/j.ibmb.2017.01.010

Cited by 22 publications

(18 citation statements)

References 42 publications

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“…20E is the primary hormone in the architecture of insects’ moulting and metamorphosis, which is confirmed to regulate the PCD, including apoptosis, autophagy and histolysis of midgut (Rabossi et al ., ; Tian et al ., ; Yang et al ., ). BmCatB and BmCatD are previously reported to be induced by 20E in Bombyx fat body (Gui et al ., ; Lee et al ., ); however, other tissue‐destruction‐related proteases are rarely checked.…”

Section: Resultsmentioning

confidence: 99%

“…During the larval-pupal metamorphosis, larval tissues undergo fierce histolysis and PCD (Tian et al, 2012(Tian et al, , 2014Yang et al, 2017). Previous microarray data reveal that some predicated Bombyx cysteine-type cathepsins, including BmCatF and -O, are highly expressed in fat body at day 3 of fifth instar (5L-3) feeding stage (Li et al, 2015); we further checked the expression of BmCatB, BmCatD, BmCatLL-1, BmCatLL-2, BmBcp, BmMmp, BmAdamTS-1, BmAdamTS L and Bmbcpi in fat body, testis, ovary, midgut, silk gland (posterior silk gland) and Malpighian tubule both at day 2 of prepupal (PP2) and day 4 of fifth instar (5L-4) feeding stages ( Fig.…”

Section: Tissue Distribution Of Destruction-related Proteases In Bombyxmentioning

confidence: 99%

“…through the ligand-receptor complex 20E-EcR-USP (Riddiford et al, 2000;Thummel & Chory, 2002). In holometabolous insects, the obsolete larval tissues or organs undergo a remodelling process to recycle intracellular components for pupal-adult organs formation during larval-pupal metamorphosis, when the 20E titre is at its peak (Li et al, 2015;Yang et al, 2017). Fat body, which acts as the centre for nutrient storage and metabolism, is characterized by the destruction of intact fat body into individual cells as well as the simultaneously severe programmed cell death (PCD) regulated by 20E combined with the AMPK-TOR pathway (Tian et al, 2012(Tian et al, , 2014Jia et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…The destruction-related proteases in insects, categorized by the amino acids present in their active centres mainly involve cysteine-type cathepsins, aspartic-type cathepsins and metzincins (Berti & Storer, 1995;Stoka et al, 2016;Yang et al, 2017). Cathepsins have been previously shown to take part in the digestion of tissues, embryonic degradation, fat body histolysis and protein degradation, playing critical roles in insect development or metamorphosis (Cristofoletti et al, 2005;Zhao et al, 2005;Yang et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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20‐Hydroxyecdysone‐upregulated proteases involved in Bombyx larval fat body destruction

Guo

et al. 2018

Insect Molecular Biology

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During insect larval-pupal metamorphosis, the obsolete larval organs and tissues undergo histolysis and programmed cell death to recycle cellular materials. It has been demonstrated that some cathepsins are essential for histolysis in larval tissues, but the process of tissue destruction is not well documented. Fat body, the homologous organ to mammalian liver and adipose tissue, goes through a distinct destruction process during larval-pupal transition. Herein, we found that most of the Bombyx proteases - including Bombyx cathepsin B (BmCatB) (BmCatLL-2), Bombyx cathepsin D (BmCatD), Bombyx cathepsin L like-1 (BmCatLL-1) and -2(BmCatLL-2), Bombyx fibroinase (BmBcp), Bombyx matrix metalloprotease (BmMmp), Bombyx A disintegrin and metalloproteinase with thrombospondin motifs 1 (BmAdamTS-1), Bombyx A disintegrin and metalloproteinase with thrombospondin motifs like (BmAdamTS L) and Bombyx cysteine protease inhibitor (Bmbcpi)- were expressed highly in fat body during feeding and metamorphosis, with a peak occurring during the nonfeeding moulting or prepupal stage, as well as being responsive to 20-hydroxyecdysone (20E). The aforementioned protease genes expression was upregulated by injection of 20E into the feeding larvae, while blocking 20E signalling transduction led to downregulation. Western blotting and immunofluorescent staining of BmCatB and BmBcp confirmed the coincident variation of their messenger RNA (mRNA) and protein level during the development and after the treatments. Moreover, BmCatB, BmBcp, BmMmp and BmAdamTS-1 RNA interference all led to blockage of larval fat body destruction. Taken together, we conclude that 20E regulates larval fat body destruction by upregulating related protease gene expression and protein levels during larval-pupal transition.

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Section: Resultsmentioning

confidence: 99%

Section: Tissue Distribution Of Destruction-related Proteases In Bombyxmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

20‐Hydroxyecdysone‐upregulated proteases involved in Bombyx larval fat body destruction

Guo

et al. 2018

Insect Molecular Biology

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“…For instance, some cathepsins can become activated (Baumgartner et al., ), released into the cytosol (Chwieralski, Welte, & Bühling, ), and degrade antiapoptotic proteins (Repnik et al., ). Other cathepsins process granzyme B molecules that enter and destroy target cells (Repnik et al., ) or cleave procaspase, increasing activity of the mature form (Yang, Yin, & Xu, ). Yet other cathepsins are secreted out of a cell and help digest extracellular matrices (Fonović & Turk, ).…”

Section: Introductionmentioning

confidence: 99%

Involvement of a host Cathepsin L in symbiont‐induced cell death

2018

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The cathepsin L gene of the host squid, Euprymna scolopes, is upregulated during the first hours of colonization by the symbiont Vibrio fischeri. At this time, the symbiotic organ begins cell death‐mediated morphogenesis in tissues functional only at the onset of symbiosis. The goal of this study was to determine whether Cathepsin L, a cysteine protease associated with apoptosis in other animals, plays a critical role in symbiont‐induced cell death in the host squid. Sequence analysis and biochemical characterization demonstrated that the protein has key residues and domains essential for Cathepsin L function and that it is active within the pH range typical of these proteases. With in situ hybridization and immunocytochemistry, we localized the transcript and protein, respectively, to cells interacting with V. fischeri. Activity of the protein occurred along the path of symbiont colonization. A specific Cathepsin L, nonspecific cysteine protease, and caspase inhibitor each independently attenuated activity and cell death to varying degrees. In addition, a specific antibody decreased cell death by ~50%. Together these data provide evidence that Cathepsin L is a critical component in the symbiont‐induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association.

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Caspase gene silencing affects the growth and development of Tuta absoluta

Rahmani

Bandani

2021

Biocatalysis and Agricultural Biotechnology

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Cathepsin L participates in the remodeling of the midgut through dissociation of midgut cells and activation of apoptosis via caspase-1

Cited by 22 publications

References 42 publications

20‐Hydroxyecdysone‐upregulated proteases involved in Bombyx larval fat body destruction

20‐Hydroxyecdysone‐upregulated proteases involved in Bombyx larval fat body destruction

Involvement of a host Cathepsin L in symbiont‐induced cell death

Caspase gene silencing affects the growth and development of Tuta absoluta

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