The origins of marine bioluminescence

McCapra, Frank; Hart, Russell C.

doi:10.1038/286660a0

Cited by 38 publications

(23 citation statements)

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“…In bioluminescent reactions, luciferase generates visible light through the oxidation of enzyme-specific substrates such as D-luciferin for terrestrial organisms (29,30) and coelenterazine for marine organisms (31,53). Luciferases from different organisms can be distinguished by their abbreviations: lux (bacterial), luc (firefly), and lcf (dinoflagellate).…”

Section: Principles Of Bioluminescencementioning

confidence: 99%

In vivo bioluminescence for tracking cell fate and function

Almeida¹,

Rappard

2011

American Journal of Physiology-Heart and Circulatory Physiology

101

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Tracking the fate and function of cells in vivo is paramount for the development of rational therapies for cardiac injury. Bioluminescence imaging (BLI) provides a means for monitoring physiological processes in real time, ranging from cell survival to gene expression to complex molecular processes. In mice and rats, BLI provides unmatched sensitivity because of the absence of endogenous luciferase expression in mammalian cells and the low background luminescence emanating from animals. In the field of stem cell therapy, BLI provides an unprecedented means to monitor the biology of these cells in vivo, giving researchers a greater understanding of their survival, migration, immunogenicity, and potential tumorigenicity in a living animal. In addition to longitudinal monitoring of cell survival, BLI is a useful tool for semiquantitative measurements of gene expression in vivo, allowing a better optimization of drug and gene therapies. Overall, this technology not only enables rapid, reproducible, and quantitative monitoring of physiological processes in vivo but also can measure the influences of therapeutic interventions on the outcome of cardiac injuries.

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Section: Principles Of Bioluminescencementioning

confidence: 99%

In vivo bioluminescence for tracking cell fate and function

Almeida¹,

Rappard

2011

American Journal of Physiology-Heart and Circulatory Physiology

101

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“…Phylogenetic distribution of imidazolopyrazine bioluminescence. (1976), Cormier (1978), McCapra and Hart (1980), Shimomura et al (1980), Campbell et al (1981) (Tables 1 and 2 ;, demonstrate the occurrence of coelenterazine and either its luciferase or photoprotein in sufficient quantities to explain the luminescence of animals from six phyla: Protozoa (Sarcomastigophora), Cnidaria, Ctenophora, Mollusca, Arthropoda and Chordata (Pisces) ( Table 3). (1974), Morin (1974), Inoue etal.…”

Section: Caz+-activated Photoproteins In Luminous Radiolariansmentioning

confidence: 97%

“…The widespread nature of coelenterazine in the luminous copepods poses questions as to its origin (McCapra and Hart 1980). The widespread nature of coelenterazine in the luminous copepods poses questions as to its origin (McCapra and Hart 1980).…”

Section: Caz+-activated Photoproteins In Luminous Radiolariansmentioning

confidence: 99%

Imidazolopyrazine bioluminescence in copepods and other marine organisms

Campbell

Herring

1990

Mar. Biol.

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The aim of this work was to establish the role of imidazolopyrazines in the bioluminescence of copepods and other marine organisms. A highly sensitive assay (down to 10-17 mol) for coelenterazine was established using reactivation of the CaZ+-activated photoprotein obelin, and for vargulin using Vargula hilgendorfi luciferase. Coelenterazine and its luciferase was found in all (8 species) the luminous copepods examined. In Euaugaptilus species more than 90% of the luciferase was found in the legs, with the luminous cells, but over 40% of the coelenterazine was found in the bodies. Coelenterazine was found in luminous organisms from six phyla: Sarcomastigophora (Radiolaria), Cnidaria, Ctenophora, Arthropoda, Mollusca. Chordata (Pisces). Only in the first three of these were Ca 2 +-activated photoproteins present.

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“…The food chain hypothesis [88,119] has not been systematically tested in the case of coelenterate-type luciferin; however, it appears very unlikely that a single ultimate source of coelenterate-type luciferin will be found to account for the widespread distribution of this molecule among six animal phyla. Mnemiopsis, for example, retains luminous capacity when raised from the 2 m m cydippid larval stage to adult (30 mm) size, feeding exclusively on brine shrimp (Artemia) larvae in artificial seawater aquaria (W. Ward, unpublished).…”

Section: Coelenterate-type Systemsmentioning

confidence: 99%

Bioluminescence: Biochemical and Physiological Advances

Ward

1981

Photochem & Photobiology

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P h o f o c h n i s t r !~ trrttl PltorohiologyBioluminescent organisms are to be found among the bacteria, fungi, unicellular algae, and most of the major animal phyla, some of which contain hundreds of luminescent species. Early biochemical studies reflected this taxonomic diversity and often a primary focus of attention was the uniqueness of each newly isolated system. Relatively few in v i m cross-reactions were discovered among unrelated species and five of the first six luciferins to be characterized proved to be structurally unrelated compounds. The functions of bioluminescence in many organisms were unknown and, while several theories arose, these theories seldom addressed the part that light production might play in the ecology of an organism or a population.Major advances on each of these fronts have been made during the past decade. Biochemical research has centered on the chemical mechanism(s) of luminescence and a single type of chemical species, a diox-

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The origins of marine bioluminescence

Cited by 38 publications

References 0 publications

In vivo bioluminescence for tracking cell fate and function

In vivo bioluminescence for tracking cell fate and function

Imidazolopyrazine bioluminescence in copepods and other marine organisms

Bioluminescence: Biochemical and Physiological Advances

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