Identification of caspases and apoptosis in the simple metazoan Hydra.
Apoptosis is a normal process by which cells die and are eliminated from tissue by phagocytosis [1]. It is involved in regulating cell numbers in adult tissues and in eliminating 'excess' cells during embryogenesis and development. Apoptosis is mediated by activation of caspases, which then cleave a variety of cellular substrates and thereby cause the characteristic morphology of apoptotic cells (rounded cells, condensed chromatin, susceptibility to phagocytosis) [2]. Although apoptosis has been well documented in nematodes, insects and mammals, it is not yet clear how early in evolution apoptosis or its component enzymes arose. In the simple metazoan Hydra vulgaris, cell death regulates cell numbers [3] [4] [5]. In starved animals, for example, epithelial cell proliferation continues at a nearly normal rate although the tissue does not increase in size; the excess cells produced are eliminated by phagocytosis. Cell death can also be induced in wild-type hydra by treatment with colchicine [6] or in a mutant strain (sf-1) by temperature shock [7]. Here, we show that cell death in hydra is morphologically indistinguishable from apoptosis in higher animals, that hydra polyps express two genes with strong homology to members of the caspase 3 family, and that caspase-3-specific enzyme activity accompanies apoptosis in hydra. The occurrence of apoptosis and caspases in a member of the ancient metazoan phylum Cnidaria supports the idea that the invention of apoptosis was an essential feature of the evolution of multicellular animals.
Cikala
M
M
Zoologisches Institut, Universität München, Luisenstrasse 14, München, 80333, Germany.
Wilm
B
B
Hobmayer
E
E
Böttger
A
A
David
C N
CN
D000818:Animals; D017209:Apoptosis / Q000187:drug effects / Q000502:physiology*; D001665:Binding Sites; D029742:Caenorhabditis elegans Proteins; D053148:Caspase 3; D020169:Caspases / Q000032:analysis / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D003078:Colchicine / Q000494:pharmacology; D003546:Cysteine Endopeptidases / Q000737:chemistry; D019143:Evolution, Molecular; D015801:Helminth Proteins / Q000737:chemistry; D006801:Humans; D006829:Hydra / Q000166:cytology / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D010587:Phagocytosis; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid
D029742:Caenorhabditis elegans Proteins; D015801:Helminth Proteins; C505407:CASP3 protein, human; D053148:Caspase 3; D020169:Caspases; D003546:Cysteine Endopeptidases; C089223:ced-3 protein, C elegans; D003078:Colchicine