Secretional luciferase of the luminous shrimp<i>Oplophorus gracilirostris</i>: cDNA cloning of a novel imidazopyrazinone luciferase

Inouye, Satoshi; Watanabe, Ken; Nakamura, Hideshi; Shimomura, Osamu

doi:10.1016/s0014-5793(00)01963-3

Cited by 120 publications

(112 citation statements)

References 31 publications

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“…Naturally occurring secreted luciferases are very suitable for this purpose, and this idea stimulates investigation of new bioluminescent systems. To date the cDNAs encoding several secreted luciferases have been cloned (23,24). Vargula luciferase has been expressed in mammalian cells and has shown promising properties as a reporter enzyme (25)(26)(27)(28).…”

Section: Monitoring Of Activity Of A2a and Npy2 G-protein-coupled Recmentioning

confidence: 99%

“…However, its large size (62.2 kDa) probably limits the value of Vargula luciferase as a reporter. Another secreted luciferase tested as a reporter is from the deep sea shrimp O. gracilorostris (24). This luciferase is a complex composed of 35-and 19-kDa proteins, and only the smaller one catalyzes the luminescent oxidation of coelenterazine.…”

Section: Monitoring Of Activity Of A2a and Npy2 G-protein-coupled Recmentioning

confidence: 99%

“…These include the marine ostracod Vargula hilgendorfii (23), the deep sea shrimp Oplophorus gracilorostris (24), and the marine copepod Gaussia princeps (GenBank TM /EBI accession number AY015993). The Vargula and Oplophorus luciferases have been expressed in mammalian cells (23)(24)(25)(26)(27)(28), and the Vargula luciferase has shown promising results. For instance, in Chinese hamster ovary (CHO) cells transfected with a plasmid bearing the cDNA for Vargula luciferase it was demonstrated that the secretory process could be monitored in real time from individual cells (26).…”

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confidence: 99%

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Cloning and Expression of cDNA for a Luciferase from the Marine Copepod Metridia longa

Markova

Gölz

Frank

et al. 2004

Journal of Biological Chemistry

139

133

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Metridia longa is a marine copepod from which a blue bioluminescence originates as a secretion from epidermal glands in response to various stimuli. We demonstrate that Metridia luciferase is specific for coelenterazine to produce blue light ( max ‫؍‬ 480 nm). Using an expression cDNA library and functional screening, we cloned and sequenced the cDNA encoding the Metridia luciferase. The cDNA is an 897-bp fragment with a 656-bp open reading frame, which encodes a 219-amino acid polypeptide with a molecular weight of 23,885. The polypeptide contains an N-terminal signal peptide of 17 amino acid residues for secretion. On expression of the Metridia luciferase gene in mammalian Chinese hamster ovary cells the luciferase is detected in the culture medium confirming the existence of a naturally occurring signal peptide for secretion in the cloned luciferase. The novel secreted luciferase was tested in a practical assay application in which the activity of A2a and NPY2 G-protein-coupled receptors was detected. These results clearly suggest that the secreted Metridia luciferase is well suited as a reporter for monitoring gene expression and, in particular, for the development of novel ultrahigh throughput screening technologies.Continuous monitoring of dynamic changes in gene expression from living cells in response to various stimuli provides important information about cell physiology. For this purpose bioluminescent and fluorescent reporters have been introduced as tools for sensitive and convenient monitoring of gene expression. A cDNA encoding a bioluminescent or fluorescent reporter such as a luciferase or green fluorescent protein (GFP) 1 is fused to the promoter region of the target gene, and the construct is transfected to mammalian cells. The gene expression is monitored simply by measuring light emitted through an enzymatic reaction or fluorescence. To date several bioluminescent proteins have been widely and successfully used for optical monitoring of gene expression in living cells: firefly luciferase (FL) (for review, see Refs. 1-3), bacterial luciferase (for review, see Refs. 4 -6), the Ca 2ϩ -regulated photoprotein aequorin (for review, see Refs. 7-9), Renilla luciferase (for review, see Refs. 10 and 11), and GFP (for review, see . Although time course studies of gene expression have been determined by real time imaging with these reporter genes, intracellular assays present difficulties for continuous measurements in some cases. For instance, it is not easy to keep an intracellular concentration of luciferin at a constant level in the case of application of firefly and Renilla luciferases. In the case of FL, additional methods may be required to facilitate the passage of the substrate across the cell membrane. In addition, the intensity and stability of the bioluminescent response of FL in living cells are reported to be affected by concentrations of ATP, luciferin, and luciferin-luciferase complex (15, 16). Despite the fact that the GFP possesses excellent properties as a reporter, it has some short...

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Section: Monitoring Of Activity Of A2a and Npy2 G-protein-coupled Recmentioning

confidence: 99%

Section: Monitoring Of Activity Of A2a and Npy2 G-protein-coupled Recmentioning

confidence: 99%

mentioning

confidence: 99%

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Cloning and Expression of cDNA for a Luciferase from the Marine Copepod Metridia longa

Markova

Gölz

Frank

et al. 2004

Journal of Biological Chemistry

139

133

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“…Some squid, when attacked, give off a luminescent secretion which confuses the attacker, and luminescent secretion from a shrimp (Inouye et al 2000 ) may serve a similar purpose. A kind of marine annelid called a scale worm is covered on the dorsal side by scales which fi rst emit fl ashes when the animal is attacked and then are shed, still glowing (Herrera et al 1974 ).…”

Section: Protection From Predationmentioning

confidence: 99%

Bioluminescence

Björn¹,

Ghiradella²

2014

Photobiology

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“…Oplophorus luciferase of the deep sea shrimp Oplophorus gracilorostris is a secretory protein [1] that catalyzes the oxidation of coelenterazine (a luciferin) to emit light (k max = $460 nm) [2]. The luciferase consists of the 19 kDa and 35 kDa proteins with a total molecular weight of 106 kDa [2], and the cDNA cloning of the 19 kDa and 35 kDa proteins showed that both proteins have a putative secretory signal peptide at the amino terminus [2].…”

Section: Introductionmentioning

confidence: 99%

Unconventional secretion of the mutated 19kDa protein of Oplophorus luciferase (nanoKAZ) in mammalian cells

Inouye¹,

Sato²,

Sahara-Miura³

et al. 2014

Biochemical and Biophysical Research Communications

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Secretional luciferase of the luminous shrimpOplophorus gracilirostris: cDNA cloning of a novel imidazopyrazinone luciferase

Cited by 120 publications

References 31 publications

Cloning and Expression of cDNA for a Luciferase from the Marine Copepod Metridia longa

Cloning and Expression of cDNA for a Luciferase from the Marine Copepod Metridia longa

Bioluminescence

Unconventional secretion of the mutated 19kDa protein of Oplophorus luciferase (nanoKAZ) in mammalian cells

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