Understanding the Molecular Mechanism and Structure-Function Relationship of the Toxicity of PLA2 and K49 Homologs in Snake Venom
1Department of Biochemistry, Institute of Biology, State University of Campinas (UNICAMP), CP 6109, 13083-970 Campinas, SP, Brazil
2Facultad de Ciencias Exactas y Naturales y Agrimensura, Universidad Nacional del Nordeste, Corrientes, Argentina
3Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas, Campinas, SP, Brazil
Understanding the Molecular Mechanism and Structure-Function Relationship of the Toxicity of PLA2 and K49 Homologs in Snake Venom
Description
Animal venoms are a rich and complex mixture of toxic and pharmacologically active proteins and peptides. Due to this broad range of biological functions, these biomolecules have been the subject of hundreds of scientific articles in different research fields, including biochemistry, biophysics, pharmacology, toxicology, and medicine.
Venoms from snakes of the family Viperidae contain class II PLA2s, which share structural features with secretory PLA2s of the class II-A present in inflammatory exudates in mammals. A number of venom PLA2s have been shown to induce a variety of pharmacological effects although comprehensive studies of the actions of venom PLA2s on the various events of toxicity are scarce. A particularly interesting subgroup of venom PLA2s includes homologs having a number of amino acid substitutions at the calcium-binding loop, especially lysine substituting aspartate at position 49, resulting in the inability of these enzymes to bind calcium and, consequently, in the abrogation of their catalytic activity. Thus, these PLA2s homologs exert their activities independently of enzymatic phospholipids degradation; the ability to induce pharmacological effects with higher potencies underscores the importance of PLA2 enzymes in snake venom toxicity.
Today, despite a series of investigations in different areas, the mechanisms of action for both variants (D49 and K49 PLA2 homologs) are not fully elucidated. We invite researchers to contribute original research articles and review articles and to encourage continued efforts to better understand the role of the catalytic activity and its absence in the homolog K49, in triggering drug events. Potential topics include, but are not limited to:
- Phospholipases A2 and K49 homolog from snake venoms, emphasizing their biological activities in vivo and in vitro
- Studying calcium independence of snake venom phospholipases A2 homologs (K49) pharmacologically based on the effects of synthetic peptides that identify a C-terminal region as being responsible for myotoxicity
- Studying the snake venom phospholipases A2 as an antitumoral agent
- Perspective of snake venom PLA2s, highlighting the variety of pharmacological activities associated with these enzymes and discussing the molecular regions involved in recognition of tissue targets
- Reviewing the use of chemical modifications in the study of venom PLA2 and K49 homolog structure-function relationships
Before submission authors should carefully read over the journal's Author Guidelines, which are located at http://www.hindawi.com/journals/jbb/guidelines/. Prospective authors should submit an electronic copy of their complete manuscript through the journal Manuscript Tracking System at http://mts.hindawi.com/ according to the following timetable: