title: Mechanisms of apoptosis in Crustacea: What conditions induce versus suppress cell death?
abstract: Arthropoda is the largest of all animal phyla and includes about 90% of extant species. Our knowledge about regulation of apoptosis in this phylum is largely based on findings for the fruit fly Drosophila melanogaster. Recent work with crustaceans shows that apoptotic proteins, and presumably mechanisms of cell death regulation, are more diverse in arthropods than appreciated based solely on the excellent work with fruit flies. Crustacean homologs exist for many major proteins in the apoptotic networks of mammals and D. melanogaster, but integration of these proteins into the physiology and pathophysiology of crustaceans is far from complete. Whether apoptosis in crustaceans is mainly transcriptionally regulated as in D. melanogaster (e.g., RHG 'killer' proteins), or rather is controlled by pro- and anti-apoptotic Bcl-2 family proteins as in vertebrates needs to be clarified. Some phenomena like the calcium-induced opening of the mitochondrial permeability transition pore (MPTP) are apparently lacking in crustaceans and may represent a vertebrate invention. We speculate that differences in regulation of the intrinsic pathway of crustacean apoptosis might represent a prerequisite for some species to survive harsh environmental insults. Pro-apoptotic stimuli described for crustaceans include UV radiation, environmental toxins, and a diatom-produced chemical that promotes apoptosis in offspring of a copepod. Mechanisms that serve to depress apoptosis include the inhibition of caspase activity by high potassium in energetically healthy cells, alterations in nucleotide abundance during energy-limited states like diapause and anoxia, resistance to opening of the calcium-induced MPTP, and viral accommodation during persistent viral infection. Characterization of the players, pathways, and their significance in the core machinery of crustacean apoptosis is revealing new insights for the field of cell death.
authors.affiliation: Department of Biological Sciences, Louisiana State University, Baton Rouge, 70803, USA. menze@lsu.edu
authors.forename: Michael A
authors.initials: MA
authors.lastname: Menze
authors.forename: Grady
authors.initials: G
authors.lastname: Fortner
authors.forename: Suman
authors.initials: S
authors.lastname: Nag
authors.forename: Steven C
authors.initials: SC
authors.lastname: Hand
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D051017:Apoptosis Regulatory Proteins / Q000737:chemistry / Q000378:metabolism; D020169:Caspases / Q000378:metabolism; D003445:Crustacea / Q000166:cytology* / Q000201:enzymology; D008928:Mitochondria / Q000378:metabolism; D008969:Molecular Sequence Data; D010539:Permeability
chemical_list: D051017:Apoptosis Regulatory Proteins; D020169:Caspases