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Anchalee Tassanakajon - One of the best experts on this subject based on the ideXlab platform.
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gene expression and characterization of a Serine Proteinase Inhibitor pmserpin8 from the black tiger shrimp penaeus monodon
Fish & Shellfish Immunology, 2012Co-Authors: Suphaphon Somnuk, Anchalee Tassanakajon, Vichien RimphanitchayakitAbstract:The ubiquitous SERPINs or Serine Proteinase Inhibitors are essential for controlling Proteinases in several biological processes in various organisms. A PmSERPIN8, one of eight SERPINs identified from the Penaeus monodon database, is studied and reported herein. The open reading frame of PmSERPIN8 gene derived from a genomic gene contains 5 exons of 320, 139, 244, 239 and 312 bp separated by 4 introns of 447, 657, 326 and 479 bp. The PmSERPIN8 gene is highly expressed at nauplius stage and gradually subsided as the shrimp grow through zoea, mysis and postlarva stages. At sub-adult stage, the PmSERPIN8 gene is expressed mainly in the hemocyte and epipodite. The expression in response to Vibrio harveyi and YHV injection is up-regulated, respectively, at 24 and 48 h post-injection. The number of PmSERPIN8-producing hemocytes, however, is observed highest at 48 h post V. harveyi injection. All three hemocyte cell types: hyaline, semigranular and granular hemocytes are able to produce PmSERPIN8. The recombinant mature PmSERPIN8 (rPmSERPIN8) with a predicted size of 45.5 kDa was over-produced in an Escherichia coli system, solubilized from the inclusion bodies, purified and tested for its activity. We have found that the rPmSERPIN8 is able to inhibit the growth of Gram-positive bacterium, Bacillus subtilis, but not Gram-negative bacterium, V. harveyi 639, and inhibit the shrimp prophenoloxidase system. The PmSERPIN8 is, thus, involved in the shrimp innate immunity.
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identification of genes expressed in response to yellow head virus infection in the black tiger shrimp penaeus monodon by suppression subtractive hybridization
Developmental and Comparative Immunology, 2010Co-Authors: Adisak Prapavorarat, Siriporn Pongsomboon, Anchalee TassanakajonAbstract:Abstract Suppression subtractive hybridization (SSH) was employed to identify yellow head virus (YHV)-responsive genes from the hemocytes of the black tiger shrimp, Penaeus monodon . Two SSH cDNA libraries were constructed to identify viral responsive genes in the early (24I) and late (48/72I) phases of YHV infection. From 240 randomly selected clones from each library, 155 and 30 non-redundant transcripts were obtained for the early and late libraries, respectively. From these clones, 72 and 16, respectively, corresponded to known genes ( E -values −4 ) that could be categorized according to their putative functions. The upregulated genes identified as likely to be associated with cell defense and homeostasis were found at a high proportion in the 24I SSH library, but not in 48/72I SSH library implying that these immune molecules participate in viral defense immunity in the early phase of YHV infection whereas their expressions were suppressed in the late phase of infection. Novel YHV-responsive genes were uncovered from these SSH libraries including caspases, histidine triad nucleotide-binding protein 2, Rab11, β-integrin, tetraspanin, prostaglandin E synthase, transglutaminase, Kazal-type Serine Proteinase Inhibitor and antimicrobial peptides. Among these YHV-responsive genes, several have been previously reported to participate in defense against white-spot syndrome virus (WSSV) implying that YHV infection in shrimp induces similar host immune responses as observed during WSSV infection. The expression of four apparently upregulated immune-related genes identified from the two SSH libraries, anti-lipopolysaccharide factor isoform 6 (ALF Pm 6), crustin isoform 1 (crustin Pm 1), transglutaminase and Kazal-type Serine Proteinase Inhibitor isoform 2 (SPI Pm 2), was evaluated by real-time RT-PCR to reveal differential expression in response to YHV infection at 6, 24, 48 and 72 h post-infection. The results confirmed their differential expression and upregulation, and thus verified the success of the SSHs and the likely involvement of these genes in shrimp antiviral mechanisms.
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identification of genes expressed in response to yellow head virus infection in the black tiger shrimp penaeus monodon by suppression subtractive hybridization
Developmental and Comparative Immunology, 2010Co-Authors: Adisak Prapavorarat, Siriporn Pongsomboon, Anchalee TassanakajonAbstract:Suppression subtractive hybridization (SSH) was employed to identify yellow head virus (YHV)-responsive genes from the hemocytes of the black tiger shrimp, Penaeus monodon. Two SSH cDNA libraries were constructed to identify viral responsive genes in the early (24I) and late (48/72I) phases of YHV infection. From 240 randomly selected clones from each library, 155 and 30 non-redundant transcripts were obtained for the early and late libraries, respectively. From these clones, 72 and 16, respectively, corresponded to known genes (E-values < 1 x 10(-4)) that could be categorized according to their putative functions. The upregulated genes identified as likely to be associated with cell defense and homeostasis were found at a high proportion in the 24I SSH library, but not in 48/72I SSH library implying that these immune molecules participate in viral defense immunity in the early phase of YHV infection whereas their expressions were suppressed in the late phase of infection. Novel YHV-responsive genes were uncovered from these SSH libraries including caspases, histidine triad nucleotide-binding protein 2, Rab11, beta-integrin, tetraspanin, prostaglandin E synthase, transglutaminase, Kazal-type Serine Proteinase Inhibitor and antimicrobial peptides. Among these YHV-responsive genes, several have been previously reported to participate in defense against white-spot syndrome virus (WSSV) implying that YHV infection in shrimp induces similar host immune responses as observed during WSSV infection. The expression of four apparently upregulated immune-related genes identified from the two SSH libraries, anti-lipopolysaccharide factor isoform 6 (ALFPm6), crustin isoform 1 (crustinPm1), transglutaminase and Kazal-type Serine Proteinase Inhibitor isoform 2 (SPIPm2), was evaluated by real-time RT-PCR to reveal differential expression in response to YHV infection at 6, 24, 48 and 72 h post-infection. The results confirmed their differential expression and upregulation, and thus verified the success of the SSHs and the likely involvement of these genes in shrimp antiviral mechanisms.
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a five domain kazal type Serine Proteinase Inhibitor from black tiger shrimp penaeus monodon and its Inhibitory activities
Developmental and Comparative Immunology, 2006Co-Authors: Nawarat Somprasong, Vichien Rimphanitchayakit, Anchalee TassanakajonAbstract:A novel five-domain Kazal-type Serine Proteinase Inhibitor, SPIPm2, identified from the hemocyte cDNA library of black tiger shrimp Penaeus monodon was successfully expressed in the Escherichia coli expression system. The expressed recombinant SPIPm2 (rSPIPm2) as inclusion bodies was solubilized with a sodium carbonate buffer, pH10, and purified by gel filtration chromatography. The molecular mass of rSPIPm2 was determined using MALDI-TOF mass spectrometry to be 29.065 kDa. The Inhibitory activities of rSPIPm2 were tested against trypsin, a-chymotrypsin, subtilisin and elastase. The Inhibitor exhibited potent Inhibitory activities against subtilisin and elastase, weak Inhibitory activity against trypsin, and did not inhibit chymotrypsin. Tight-binding inhibition assay suggested that the molar ratios of SPIPm2 to subtilisin and elastase were 1:2 and 1:1, respectively. The inhibition against subtilisin and elastase was a competitive type with inhibition constants (Ki) of 0.52 and 3.27 nM, respectively. The Inhibitory activity of SPIPm2 against subtilisin implies that, in shrimp, it may function as a defense component against Proteinases from pathogenic bacteria but the elastase Inhibitory function is not known. r 2006 Elsevier Ltd. All rights reserved.
Sandro Palmieri - One of the best experts on this subject based on the ideXlab platform.
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purification Inhibitory properties amino acid sequence and identification of the reactive site of a new Serine Proteinase Inhibitor from oil rape itbrassica napus seed
FEBS Letters, 1994Co-Authors: Fabrizio Ceciliani, Enea Menegatti, Paolo Ascenzi, Severino Ronchi, Fabrizio Bortolotti, Sandro PalmieriAbstract:Abstract A new Serine Proteinase Inhibitor, rapeseed trypsin Inhibitor (RTI), has been isolated from rapeseed (Brassica napus var. oleifera) seed. The protein inhibits the catalytic activity of bovine β-trypsin and bovine α-chymotrypsin with apparent dissociation constants of 3.0 × 10−10 M and 4.1 × 10−7 M, at pH 8.0 and 21°C, respectively. The stoichiometry of both Proteinase-Inhibitor complexes is 1:1. The amino acid sequence of RTI consists of 60 amino acid residues, corresponding to an Mr, of about 6.7 kDa. The p1-pi, reactive site bond has been tentatively identified at position Arg20-Ile21. RTI shows no similarity to other Serine Proteinase Inhibitors except the low molecular weight mustard trypsin Inhibitor (MTI-2). RTI and MTI-2 could be members of a new class of plant Serine Proteinase Inhibitors.
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purification Inhibitory properties and amino acid sequence of a new Serine Proteinase Inhibitor from white mustard sinapis alba l seed
FEBS Letters, 1992Co-Authors: Enea Menegatti, Martino Bolognesi, Paolo Ascenzi, Gabriella Tedeschi, Severino Ronchi, Fabrizio Bortolotti, Richard M Thomas, Sandro PalmieriAbstract:Abstract A new Serine Proteinase Inhibitor, mustard trypsin Inhibitor 2 (MTI-2), has been isolated from white mustard ( Sinapis alba L.) seed by affinity chromatography and reverse phase HPLC. The protein inhibits the catalytic activity of bovine β-trypsin and bovine α-chymotrypsin, with dissociation constants ( K d ) of 1.6 × 10 −10 M and 5.0 × 10 −7 M, respectively, at pH 8.0 and 21°C, the stiochiometry of both Proteinase-Inhibitor complexes being 1:1. The amino acid sequence of MTI-2, which was determined following S -pyridylethylation, is comprised of 63 residues, corresponding to a molecular weight of about 7 kDa, and shows only extremely limited homology to other Serine Proteinase Inhibitors.
Colin Macaulay - One of the best experts on this subject based on the ideXlab platform.
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suppression of collagen induced arthritis with a Serine Proteinase Inhibitor serpin derived from myxoma virus
Clinical Immunology, 2014Co-Authors: Ernest Brahn, Grant Mcfadden, Alexandra Lucas, Sarah Lee, Colin MacaulayAbstract:Many viruses encode virulence factors to facilitate their own survival by modulating a host's inflammatory response. One of these factors, secreted from cells infected with myxoma virus, is the Serine Proteinase Inhibitor (serpin) Serp-1. Because Serp-1 had demonstrated anti-inflammatory properties in arterial injury models and viral infections, it was cloned and evaluated for therapeutic efficacy in collagen-induced arthritis (CIA). Clinical severity was significantly lower in the Serp-1 protocols (p<0.0001) and blinded radiographs indicated that the Serp-1 group had significantly less erosions than the controls (p<0.01). Delayed-type hypersensitivity was lower in the Serp-1 group but antibody titers to type II collagen were not significantly altered. Recipients had minimal histopathologic synovial changes and did not develop neutralizing antibodies to Serp-1. These results indicate that Serp-1 impedes the pathogenesis of CIA and suggests that the therapeutic potential of Serine Proteinase Inhibitors in inflammatory joint diseases, such as rheumatoid arthritis, should be investigated further.
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suppression of collagen induced arthritis with a Serine Proteinase Inhibitor serpin derived from myxoma virus
Clinical Immunology, 2014Co-Authors: Ernest Brahn, Grant Mcfadden, Alexandra Lucas, Sarah Lee, Colin MacaulayAbstract:Abstract Many viruses encode virulence factors to facilitate their own survival by modulating a host's inflammatory response. One of these factors, secreted from cells infected with myxoma virus, is the Serine Proteinase Inhibitor (serpin) Serp-1. Because Serp-1 had demonstrated anti-inflammatory properties in arterial injury models and viral infections, it was cloned and evaluated for therapeutic efficacy in collagen-induced arthritis (CIA). Clinical severity was significantly lower in the Serp-1 protocols (p
Alexandra Lucas - One of the best experts on this subject based on the ideXlab platform.
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suppression of collagen induced arthritis with a Serine Proteinase Inhibitor serpin derived from myxoma virus
Clinical Immunology, 2014Co-Authors: Ernest Brahn, Grant Mcfadden, Alexandra Lucas, Sarah Lee, Colin MacaulayAbstract:Abstract Many viruses encode virulence factors to facilitate their own survival by modulating a host's inflammatory response. One of these factors, secreted from cells infected with myxoma virus, is the Serine Proteinase Inhibitor (serpin) Serp-1. Because Serp-1 had demonstrated anti-inflammatory properties in arterial injury models and viral infections, it was cloned and evaluated for therapeutic efficacy in collagen-induced arthritis (CIA). Clinical severity was significantly lower in the Serp-1 protocols (p
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suppression of collagen induced arthritis with a Serine Proteinase Inhibitor serpin derived from myxoma virus
Clinical Immunology, 2014Co-Authors: Ernest Brahn, Grant Mcfadden, Alexandra Lucas, Sarah Lee, Colin MacaulayAbstract:Many viruses encode virulence factors to facilitate their own survival by modulating a host's inflammatory response. One of these factors, secreted from cells infected with myxoma virus, is the Serine Proteinase Inhibitor (serpin) Serp-1. Because Serp-1 had demonstrated anti-inflammatory properties in arterial injury models and viral infections, it was cloned and evaluated for therapeutic efficacy in collagen-induced arthritis (CIA). Clinical severity was significantly lower in the Serp-1 protocols (p<0.0001) and blinded radiographs indicated that the Serp-1 group had significantly less erosions than the controls (p<0.01). Delayed-type hypersensitivity was lower in the Serp-1 group but antibody titers to type II collagen were not significantly altered. Recipients had minimal histopathologic synovial changes and did not develop neutralizing antibodies to Serp-1. These results indicate that Serp-1 impedes the pathogenesis of CIA and suggests that the therapeutic potential of Serine Proteinase Inhibitors in inflammatory joint diseases, such as rheumatoid arthritis, should be investigated further.
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virus encoded Serine Proteinase Inhibitor serp 1 inhibits atherosclerotic plaque development after balloon angioplasty
Circulation, 1996Co-Authors: Joanne L. Macen, Alexandra Lucas, Li Ying Liu, Piers Nash, Erbin Dai, Michael W Stewart, Kathryn Graham, Wai S Etches, Lynn K BoshkovAbstract:Background Recurrent atherosclerotic plaque growth, restenosis, is a significant clinical problem after interventional procedures. Initiation of restenosis involves activation of inflammatory and thrombotic cascades, which are regulated by Serine Proteinase enzymes and Inhibitors. We have investigated the use of a viral Serine Proteinase Inhibitor, SERP-1, to reduce plaque development after primary balloon angioplasty. This is the first experimental report of the use of a viral anti-inflammatory protein for the prevention of atherosclerosis. Methods and Results Seventy-four cholesterol-fed rabbits were treated with either local or systemic infusions of SERP-1 protein (or control solutions) after balloon-mediated injury. Sites of SERP-1 infusion in rabbits had dramatically reduced plaque compared with control infusions at the 4-week follow-up. At low-dose infusions (30 to 300 pg), only the primary infusion site had a demonstrable decrease in plaque, whereas at higher-dose infusions (>3000 pg), a generalize...
Vichien Rimphanitchayakit - One of the best experts on this subject based on the ideXlab platform.
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gene expression and characterization of a Serine Proteinase Inhibitor pmserpin8 from the black tiger shrimp penaeus monodon
Fish & Shellfish Immunology, 2012Co-Authors: Suphaphon Somnuk, Anchalee Tassanakajon, Vichien RimphanitchayakitAbstract:The ubiquitous SERPINs or Serine Proteinase Inhibitors are essential for controlling Proteinases in several biological processes in various organisms. A PmSERPIN8, one of eight SERPINs identified from the Penaeus monodon database, is studied and reported herein. The open reading frame of PmSERPIN8 gene derived from a genomic gene contains 5 exons of 320, 139, 244, 239 and 312 bp separated by 4 introns of 447, 657, 326 and 479 bp. The PmSERPIN8 gene is highly expressed at nauplius stage and gradually subsided as the shrimp grow through zoea, mysis and postlarva stages. At sub-adult stage, the PmSERPIN8 gene is expressed mainly in the hemocyte and epipodite. The expression in response to Vibrio harveyi and YHV injection is up-regulated, respectively, at 24 and 48 h post-injection. The number of PmSERPIN8-producing hemocytes, however, is observed highest at 48 h post V. harveyi injection. All three hemocyte cell types: hyaline, semigranular and granular hemocytes are able to produce PmSERPIN8. The recombinant mature PmSERPIN8 (rPmSERPIN8) with a predicted size of 45.5 kDa was over-produced in an Escherichia coli system, solubilized from the inclusion bodies, purified and tested for its activity. We have found that the rPmSERPIN8 is able to inhibit the growth of Gram-positive bacterium, Bacillus subtilis, but not Gram-negative bacterium, V. harveyi 639, and inhibit the shrimp prophenoloxidase system. The PmSERPIN8 is, thus, involved in the shrimp innate immunity.
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a five domain kazal type Serine Proteinase Inhibitor from black tiger shrimp penaeus monodon and its Inhibitory activities
Developmental and Comparative Immunology, 2006Co-Authors: Nawarat Somprasong, Vichien Rimphanitchayakit, Anchalee TassanakajonAbstract:A novel five-domain Kazal-type Serine Proteinase Inhibitor, SPIPm2, identified from the hemocyte cDNA library of black tiger shrimp Penaeus monodon was successfully expressed in the Escherichia coli expression system. The expressed recombinant SPIPm2 (rSPIPm2) as inclusion bodies was solubilized with a sodium carbonate buffer, pH10, and purified by gel filtration chromatography. The molecular mass of rSPIPm2 was determined using MALDI-TOF mass spectrometry to be 29.065 kDa. The Inhibitory activities of rSPIPm2 were tested against trypsin, a-chymotrypsin, subtilisin and elastase. The Inhibitor exhibited potent Inhibitory activities against subtilisin and elastase, weak Inhibitory activity against trypsin, and did not inhibit chymotrypsin. Tight-binding inhibition assay suggested that the molar ratios of SPIPm2 to subtilisin and elastase were 1:2 and 1:1, respectively. The inhibition against subtilisin and elastase was a competitive type with inhibition constants (Ki) of 0.52 and 3.27 nM, respectively. The Inhibitory activity of SPIPm2 against subtilisin implies that, in shrimp, it may function as a defense component against Proteinases from pathogenic bacteria but the elastase Inhibitory function is not known. r 2006 Elsevier Ltd. All rights reserved.
