Biochemical and Biophysical Research Communications
Regular ArticlecDNA Cloning and Characterization of Vascular Apoptosis-Inducing Protein 1☆,☆☆
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Cited by (53)
Snake Venom Metalloproteinases (SVMPs): A structure-function update
2020, Toxicon: XCitation Excerpt :There are copious reports of RGD variants such as KGD (lysine-glycine-aspartate), VGD (valine-glycine-aspartate), WGD (tryptophan-glycine-aspartate), MLD (methionine-leucine-aspartate), RTS (arginine-threonine-serine), KTS (lysine-threonine-serine) and so on (Calvete et al., 2005; Cesar et al., 2019; Rivas-Mercado and Garza-Ocañas, 2017). The RGD-motif is embedded in a flexible loop constituted by the oligopeptide chain of 13 aminoacyl residues, which interact significantly with the integrin αIIBβ3/GpIIb/IIIa inhibiting platelet aggregation (Chung et al., 1999; Masuda et al., 2000). In some P-II structures, additional intra-chain interaction culminate to structural reinforcement and stability, thus, preventing the proteolytic release of their disintegrins.
Bothrops erythromelas (Amaral, 1923) venom induces apoptosis on renal tubular epithelial cells
2016, ToxiconCitation Excerpt :Taken together, these results show that apoptosis is predominant. The major compound of BeV is metalloproteinases (Jorge et al., 2015), a class of apoptosis-inducing snake venom protein, such as described by Brenes et al. (2010), Masuda et al. (1998, 2000, 2001). Furthermore, the Bothropoides pauloensis venom, of which main compound is metalloproteinases (Rodrigues et al., 2012) was also described as an inductor of apoptosis (Marinho et al., 2015).
Purification and characterization of two high molecular mass snake venom metalloproteinases (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegans (Sakishima-habu)
2015, ToxiconCitation Excerpt :P-III SVMPs have been further divided into subclasses based on their distinct post-translation modifications, such as dimerization (P-IIIc) or proteolytic processing (P-IIIb). P-IIIc has been reported on HV1 from Protobothrops flavoviridis venom, VAP1 from Crotalus atrox venom, VLAIPs from Vipera lebetina venom, and TSV-DM from Protobothrops stejnegeri venom, and most these proteins were shown to induce apoptosis in vascular endothelial cells (Masuda et al., 2001, 2000, 1997; Samel et al., 2012; Trummal et al., 2005; Wan et al., 2006). The heterotrimeric subclass of SVMPs are now included in the P-III group as a subclass (P-IIId), which represents another post-translational modification of canonical P-IIIa SVMPs.
Vascular Apoptosis-Inducing Protein 1
2013, Handbook of Proteolytic EnzymesEffect of HUVEC apoptosis inducing proteinase from Vipera lebetina venom (VLAIP) on viability of cancer cells and on platelet aggregation
2012, ToxiconCitation Excerpt :However VLAIP is not able to induce apoptosis in HeLa, NIH3T3 (Trummal et al., 2005) and PC-3 cells. The disintegrin-like domain of VLAIP contains an ECD motif, which is similar to other P-III SVMPs such as VAP1 from Crotalus atrox (Masuda et al., 2000) and halysase from Gloydius halys (You et al., 2003). Halysase that contains ECD sequence in its disintegrin domain more strongly inhibits the endothelial cell adhesion to fibronectin (You et al., 2003).
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The sequence reported in this paper have been submitted to the DDBJ/EMBL/GenBank database (Accession No. AB042840).
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Abbreviations used: VAP, vascular apoptosis-inducing protein; MCS, multiple cloning site; VEC, vascular endothelial cells; FGF, fibroblast growth factor; LAO, -amino acid oxidase; PVDF, polyvinylidene difluoride; FBS, fetal bovine serum; PCR, polymerase chain reaction; PBS−, phosphate-buffered saline without magnesium and calcium; PMSF, phenylmethylsulfonyl fluoride.
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