Molecular cloning and characterisation of peroxinectin, a cell adhesion molecule, from the giant freshwater prawn Macrobrachium rosenbergii

Hsu, Pei-I.; Liu, Chun-Hung; Tseng, Deng-Yu; Lee, Pai-Po; Cheng, Winton

doi:10.1016/j.fsi.2005.08.010

Cited by 30 publications

(20 citation statements)

References 29 publications

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“…Temporal expression analysis indicated that mRNA expression of Fi-Pxn could be changed by bacteria challenge and similar results were reported by various authors (Dong et al, 2009;Sritunyalucksana et al, 2001;Liu et al, 2005, 2010, Hsu et al, 2006 which suggested that peroxinectin might be involved in immune response to bacterial infection. In invertebrates, peroxinectin genes can be upregulated by lipopolysaccharides (LPSs)or other microbial compounds, while a peroxinectin-like gene is expressed during oogenesis and early embryogenesis of Drosophila melanogaster (V á zquez et al, 2002).…”

Section: Discussionsupporting

confidence: 85%

“…Full length sequence of peroxinectin has been isolated from several other crustacean species such as Fenneropenaeus chinensis (Dong et al, 2009) , Litopenaeus vannamei (Liu et al, 2004(Liu et al, , 2005 , Scylla serrata (Lin et al, 2010) , Macrobrachium rosenbergii (Hsu et al, 2006) , Penaeus monodon (Sritunyalucksana et al, 2001) and in tunicate such as Ciona intestinalis (Vizzini et al, 2013) . However, the molecular mechanism behind the peroxinectin gene and its involvement in prophenoloxidase activating system is still unresolved.…”

Section: Introductionmentioning

confidence: 99%

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Molecular Cloning of Peroxinectin Gene and Its Expression in Response to Peptidoglycan andVibrio Harveyiin Indian White ShrimpFenneropenaeus Indicus

Shanthi

Manju

Rajakumaran

et al. 2014

Cell Communication & Adhesion

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The cDNA sequence of peroxinectin was obtained from the haemocytes of Indian white shrimp Fenneropenaeus indicus using RT-PCR and RACE. Fenneropenaeus indicus peroxinectin (Fi-Pxn) sequence has an open reading frame (ORF) of 2415 bp encoding a protein of 804 amino acids with 21 residues signal sequence. The mature protein has molecular mass of 89.8 kDa with an estimated pI of 8.6. Two putative integrin-binding motifs, RGD and KGD, were observed at the basic N-terminal and C-terminal part of the mature aminoacid sequence. Fi-Pxn nucleotide sequence comparison showed high homology to mud crab Scylla serrata (89%) and to various vertebrate and invertebrate species. qRT-PCR showed peroxinectin mRNA transcript in haemocytes of F. indicus increased at 6 h post injection of peptidoglycan and Vibrio harveyi. The Fi-Pxn was mainly expressed in the tissues of haemocytes and the heart. The moulting stage responses showed Fi-Pxn expression in premoult stages D 0/1 and D 0/2 .

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Section: Discussionsupporting

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Molecular Cloning of Peroxinectin Gene and Its Expression in Response to Peptidoglycan andVibrio Harveyiin Indian White ShrimpFenneropenaeus Indicus

Shanthi

Manju

Rajakumaran

et al. 2014

Cell Communication & Adhesion

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“…Both the cell adhesion and peroxidase functions can be activated in the presence of LPS or beta-1,3-glucans (Johansson and Söderhäll, 1988;Liu et al, 2005Liu et al, , 2007Hsu et al, 2006). Peroxinectin also binds Cu-Zn-superoxide dismutase (CuZnSOD) at the surface of circulating hemocytes, and this interaction, facilitated by the close localization, may modulate both the enzyme activities.…”

Section: Discussionmentioning

confidence: 99%

“…Because PXN has peroxidase activity, this protein might produce hypohalic acid near to the bound pathogen (Cerenius et al, 2008;Johansson, 1999). In invertebrates, peroxinectin genes can be upregulated by LPS or other microbial compounds (Dong et al, 2009;Hsu et al, 2006;Liu et al, 2005), while a peroxinectin-like gene is expressed during oogenesis and early embryogenesis of D. melanogaster (Vázquez et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…Several reports suggest that peroxinectin can be essential in cellular defense reaction and resembles the functions of mammalian leukocyte peroxidases (Johansson et al, 1995;Sritunyalucksana et al, 2001;Söderhäll, 1999;Hsu et al, 2006). In crustaceans, they are synthesized and released by semigranular and granular hemocytes in response to foreign stimuli.…”

Section: Discussionmentioning

confidence: 99%

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Ciona intestinalis peroxinectin is a novel component of the peroxidase–cyclooxygenase gene superfamily upregulated by LPS

Vizzini

Parrinello

Sanfratello

et al. 2013

Developmental & Comparative Immunology

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a b s t r a c tPeroxinectins function as hemoperoxidase and cell adhesion factor involved in invertebrate immune reaction. In this study, the ascidian (Ciona intestinalis) peroxinectin gene (CiPxt) and its expression during the inflammatory response have been examined. CiPxt is a new member of the peroxidase-cyclooxygenase gene superfamily that contains both the peroxidase domain and the integrin KGD (Lys-Gly-Asp) binding motif. A phylogenetic tree showed that CiPxt is very close to the chordate group and appears to be the outgroup of mammalian MPO, EPO and TPO clades. The CiPxt molecular structure model resulted superimposable to the human myeloperoxidase. The CiPxt mRNA expression is upregulated by LPS inoculation suggesting it is involved in C. intestinalis inflammatory response. The CiPxt was expressed in hemocytes (compartment/morula cells), vessel epithelium, and unilocular refractile granulocytes populating the inflamed tunic matrix and in the zones 7, 8 and 9 of the endostyle, a special pharynx organs homolog to the vertebrate thyroid gland.

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In vitroandin silicostudies on cell adhesion protein peroxinectin fromFenneropenaeus indicusand screening of heme blockers against activity

2015

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In invertebrates, the prophenoloxidase (proPO) pathway is involved in the phenol-like antioxidant production against invading pathogens. Overproduction of melanin and phenolic substances leads to the disruption of hemocytes (own host cells); therefore, there is a prerequisite to regulate the antioxidant production, which is performed by the proteases and proPO-associated cell adhesion protein peroxinectin (PX). PX is a macromolecular structure consisting of protein involved in the proPO pathway, which is a potential target in the regulatory mechanism in crustaceans. In the proPO cascade, pattern recognition proteins initiate the proPO cascade by the consequent reaction, and PX is involved in the key step in the regulatory mechanism of phenoloxidase enzyme synthesis. In the present study, Indian white shrimp Fenneropenaeus indicus PX (Fein-PX) gene sequence was used. Upregulation of Fein-PX was determined using immunostimulants β-glucan (agonists) and examined its expression by quantitative RT-PCR. To find the downregulation or negative regulation of Fein-PX, inhibitors were screened, and its 3D model provides molecular insights into the rationale inhibitor design for developing an effective molecule against Fein-PX.

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Molecular cloning and characterisation of peroxinectin, a cell adhesion molecule, from the giant freshwater prawn Macrobrachium rosenbergii

Cited by 30 publications

References 29 publications

Molecular Cloning of Peroxinectin Gene and Its Expression in Response to Peptidoglycan andVibrio Harveyiin Indian White ShrimpFenneropenaeus Indicus

Molecular Cloning of Peroxinectin Gene and Its Expression in Response to Peptidoglycan andVibrio Harveyiin Indian White ShrimpFenneropenaeus Indicus

Ciona intestinalis peroxinectin is a novel component of the peroxidase–cyclooxygenase gene superfamily upregulated by LPS

In vitroandin silicostudies on cell adhesion protein peroxinectin fromFenneropenaeus indicusand screening of heme blockers against activity

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