The Experts below are selected from a list of 52617 Experts worldwide ranked by ideXlab platform
Ping Zhao - One of the best experts on this subject based on the ideXlab platform.
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a clip domain serine protease involved in Moulting in the silkworm bombyx mori cloning characterization expression patterns and functional analysis
Insect Molecular Biology, 2017Co-Authors: Handeng Liu, Luoling Wang, Z Meng, Xin Tang, Qingyou Xia, Ping ZhaoAbstract:Clip domain serine proteases (CLIPs), characterized by one or more conserved clip domains, are essential components of extracellular signalling cascades in various biological processes, especially in innate immunity and the embryonic development of insects. Additionally, CLIPs may have additional non-immune functions in insect development. In the present study, the clip domain serine protease gene Bombyx mori serine protease 95 (BmSP95), which encodes a 527-residue protein, was cloned from the integument of B. mori. Bioinformatics analysis indicated that BmSP95 is a typical CLIP of the subfamily D and possesses a clip domain at the N terminus, a trypsin-like serine protease (tryp_spc) domain at the C terminus and a conserved proline-rich motif between these two domains. At the transcriptional level, BmSP95 is expressed in the integument during Moulting and metamorphosis, and the expression pattern is consistent with the fluctuating 20-hydroxyecdysone (20E) titre in B. mori. At the translational level, BmSP95 protein is synthesized in the epidermal cells, secreted as a zymogen and activated in the Moulting fluid. Immunofluorescence revealed that BmSP95 is distributed into the old endocuticle in the Moulting stage. The expression of BmSP95 was upregulated by 20E. Moreover, expression of BmSP95 was downregulated by pathogen infection. RNA interference-mediated silencing of BmSP95 led to delayed Moulting from pupa to moth. These results suggest that BmSP95 is involved in integument remodelling during Moulting and metamorphosis.
Handeng Liu - One of the best experts on this subject based on the ideXlab platform.
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a clip domain serine protease involved in Moulting in the silkworm bombyx mori cloning characterization expression patterns and functional analysis
Insect Molecular Biology, 2017Co-Authors: Handeng Liu, Luoling Wang, Z Meng, Xin Tang, Qingyou Xia, Ping ZhaoAbstract:Clip domain serine proteases (CLIPs), characterized by one or more conserved clip domains, are essential components of extracellular signalling cascades in various biological processes, especially in innate immunity and the embryonic development of insects. Additionally, CLIPs may have additional non-immune functions in insect development. In the present study, the clip domain serine protease gene Bombyx mori serine protease 95 (BmSP95), which encodes a 527-residue protein, was cloned from the integument of B. mori. Bioinformatics analysis indicated that BmSP95 is a typical CLIP of the subfamily D and possesses a clip domain at the N terminus, a trypsin-like serine protease (tryp_spc) domain at the C terminus and a conserved proline-rich motif between these two domains. At the transcriptional level, BmSP95 is expressed in the integument during Moulting and metamorphosis, and the expression pattern is consistent with the fluctuating 20-hydroxyecdysone (20E) titre in B. mori. At the translational level, BmSP95 protein is synthesized in the epidermal cells, secreted as a zymogen and activated in the Moulting fluid. Immunofluorescence revealed that BmSP95 is distributed into the old endocuticle in the Moulting stage. The expression of BmSP95 was upregulated by 20E. Moreover, expression of BmSP95 was downregulated by pathogen infection. RNA interference-mediated silencing of BmSP95 led to delayed Moulting from pupa to moth. These results suggest that BmSP95 is involved in integument remodelling during Moulting and metamorphosis.
Dwayne D. Hegedus - One of the best experts on this subject based on the ideXlab platform.
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Insect intestinal mucins and serine proteases associated with the peritrophic matrix from feeding, starved and Moulting Mamestra configurata larvae.
Insect Molecular Biology, 2010Co-Authors: Umut Toprak, Martin A. Erlandson, Cedric Gillott, Doug Baldwin, Dwayne D. HegedusAbstract:Insect intestinal mucins (McIIM2-4) expressed in the midgut of feeding, starved and Moulting Mamestra configurata larvae were identified. McIIM2 and McIIM4 were associated with the peritrophic matrix (PM). PMs from feeding and starved larvae were translucent and contained organized chitin bundles perpendicular to their long axis, whereas PM from Moulting larvae consisted of an inner opaque mass surrounded by an outer translucent sleeve. Serine protease genes (McSP1, McSP2, McSP25 and McSP29) were also expressed in these larvae and several serine proteases were associated with the PM. Serine protease activity was also detected in the midgut of feeding, starved and Moulting larvae.
Luoling Wang - One of the best experts on this subject based on the ideXlab platform.
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a clip domain serine protease involved in Moulting in the silkworm bombyx mori cloning characterization expression patterns and functional analysis
Insect Molecular Biology, 2017Co-Authors: Handeng Liu, Luoling Wang, Z Meng, Xin Tang, Qingyou Xia, Ping ZhaoAbstract:Clip domain serine proteases (CLIPs), characterized by one or more conserved clip domains, are essential components of extracellular signalling cascades in various biological processes, especially in innate immunity and the embryonic development of insects. Additionally, CLIPs may have additional non-immune functions in insect development. In the present study, the clip domain serine protease gene Bombyx mori serine protease 95 (BmSP95), which encodes a 527-residue protein, was cloned from the integument of B. mori. Bioinformatics analysis indicated that BmSP95 is a typical CLIP of the subfamily D and possesses a clip domain at the N terminus, a trypsin-like serine protease (tryp_spc) domain at the C terminus and a conserved proline-rich motif between these two domains. At the transcriptional level, BmSP95 is expressed in the integument during Moulting and metamorphosis, and the expression pattern is consistent with the fluctuating 20-hydroxyecdysone (20E) titre in B. mori. At the translational level, BmSP95 protein is synthesized in the epidermal cells, secreted as a zymogen and activated in the Moulting fluid. Immunofluorescence revealed that BmSP95 is distributed into the old endocuticle in the Moulting stage. The expression of BmSP95 was upregulated by 20E. Moreover, expression of BmSP95 was downregulated by pathogen infection. RNA interference-mediated silencing of BmSP95 led to delayed Moulting from pupa to moth. These results suggest that BmSP95 is involved in integument remodelling during Moulting and metamorphosis.
Qingyou Xia - One of the best experts on this subject based on the ideXlab platform.
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a clip domain serine protease involved in Moulting in the silkworm bombyx mori cloning characterization expression patterns and functional analysis
Insect Molecular Biology, 2017Co-Authors: Handeng Liu, Luoling Wang, Z Meng, Xin Tang, Qingyou Xia, Ping ZhaoAbstract:Clip domain serine proteases (CLIPs), characterized by one or more conserved clip domains, are essential components of extracellular signalling cascades in various biological processes, especially in innate immunity and the embryonic development of insects. Additionally, CLIPs may have additional non-immune functions in insect development. In the present study, the clip domain serine protease gene Bombyx mori serine protease 95 (BmSP95), which encodes a 527-residue protein, was cloned from the integument of B. mori. Bioinformatics analysis indicated that BmSP95 is a typical CLIP of the subfamily D and possesses a clip domain at the N terminus, a trypsin-like serine protease (tryp_spc) domain at the C terminus and a conserved proline-rich motif between these two domains. At the transcriptional level, BmSP95 is expressed in the integument during Moulting and metamorphosis, and the expression pattern is consistent with the fluctuating 20-hydroxyecdysone (20E) titre in B. mori. At the translational level, BmSP95 protein is synthesized in the epidermal cells, secreted as a zymogen and activated in the Moulting fluid. Immunofluorescence revealed that BmSP95 is distributed into the old endocuticle in the Moulting stage. The expression of BmSP95 was upregulated by 20E. Moreover, expression of BmSP95 was downregulated by pathogen infection. RNA interference-mediated silencing of BmSP95 led to delayed Moulting from pupa to moth. These results suggest that BmSP95 is involved in integument remodelling during Moulting and metamorphosis.
