Scorpion venom phospholipases A2: A minireview. (September 2020)

• Record Type: Journal Article
• Authors: Krayem, Najeh; Gargouri, Youssef
• Is Part Of: Toxicon. Volume 184(2020)
• Page Start: 48
• Page End: 54
• Publication Date: 2020-09
• Subjects: Secreted phospholipases A2 -- Scorpion venom phospholipases A2 -- Biological activities -- Biochemical properties -- Structure-function relationships; CAM Chicken Chorioallantoic Membrane -- CC-PLA2 secreted PLA2 from Cerastes cerastes snake venom -- EBM Endothelial Basal Medium -- ECM Extra Cellular Matrix -- Fg Fibrinogen -- FGF-2 Fibroblast Growth Factors -- Fn Fibronectin -- HBMEC Human Brain Microvascular Endothelial Cells -- HfPLA2 Heterometrus fulvipes venom Phospholipase A2 -- HMEC-1 Human Microvascular Endothelial Cells -- HmTx Heteromtoxin from Heterometrus laoticus venom -- HPAECs Human Pulmonary Artery Endothelial Cells -- HUVEC Human Umbilical Vein Endothelial Cells -- IpTxi Imperatoxin I from Pandinus imperator venom -- MtPLA2 Mesobuthus tamulusvenom Secreted phospholipases A2, MVL-PLA2: secreted PLA2fromMacrovipera lebetinasnake venom -- P-BPB p-bromophenacyl bromide -- PIVL Kunitz-type serine protease inhibitor from Macrovipera lebetina venom -- PLA2 Phospholipase A2 -- rPLA2(+5) recombinant phospholipase A2 containing the long and Short chains linked by the penta-peptide. -- rPLA2(-5) recombinant phospholipase A2 in which the penta-peptide insert is deleted. -- RyRs Ryanodine Receptors -- SA Specific Activity -- Sm-PLGV phospholipase A2 purified from Scorpio maurus venom glands -- sPLA2 secreted phospholipases A2 -- SR Sarcoplasmic Reticulum -- U87 Human glioblastoma cells -- VEGF Vascular Endothelial Growth Factor -- vPLA2 venom PLA2; Toxins -- Periodicals; Venom -- Periodicals; 615.9
• DOI: 10.1016/j.toxicon.2020.05.020
• Languages: English
• ISSNs: 0041-0101

Abstract

Abstract: Many venomous species, including snakes, bees and scorpions, contain a variety of secreted phospholipases A2 (sPLA2 ) that contribute to prey digestion and venom toxicity. Based on their primary structures, the different venom sPLA2 have been classified into four groups I, II, III and IX. While the structure of sPLA2 groups II and I has been well characterized, only one crystal structure of group III sPLA2 from bee venom was described. Scorpion venom sPLA2 belong to group III with a particular heterodimeric structure composed of a long enzymatic chain linked by a disulfide bridge to a Short one after the release of five residues (penta-peptide) during the maturation processes. The function of the Short chain is still not clear. Its sequence varies in composition and in length between different scorpion species . Available studies of the structure-function relationships of scorpion venom sPLA2 are limited. Some biological activities of these enzymes such as neurotoxicity, myotoxicity, along with the hemolytic, anticoagulant, anti-tumoral and anti-angiogenic activities have been investigated. In this review, we tentatively summarize the last findings about the biochemical properties, the structure-function relation and the biological activities of scorpion venom phospholipases A2 . In addition to expanding the database of structures for these sPLA2 and understanding their properties and functions, this survey is intended to explore the molecular mechanisms and signaling pathways of the described biological activities.