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Science and Technology
Quincy Bioscience is pursuing novel therapeutics for the treatment of the diseases of aging. The company's technology has led to patent filings for both nutraceutical and pharmaceutical applications of the calcium-binding protein aequorin. Aequorin, comes from the jellyfish - an organism with one of the simplest nervous systems. While aequorin has been commonly used in laboratory research for nearly forty years, to date, it had never been used in any therapeutic manner before Quincy Bioscience's research began. Aequorin is unique in that it is from a family of molecules that are called calcium-binding proteins. Calcium-binding proteins are known to deplete in the aging process. Quincy Bioscience sets itself apart through its introduction of aequorin to help restore of calcium homeostasis in the human body.
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Click here for information about the Aequorea victoria jellyfish
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Aequorin
One calcium-binding protein (CaBP) that might be effective in treating neurodegenerative disorders is
aequorin, a naturally-occurring calcium-sensitive bioluminescent protein originally isolated from
jellyfish (Inouye et al., 1985 [1]). Its natural bioluminescent
properties (when bound to calcium) make it ideal not only for observing changes in calcium ion
concentrations but also make it easy to observe uptake by neurons.
Jellyfish have a very simple nervous system, and aequorin works within jellyfish to
sequester excess calcium ions by binding with them so they utilize the calcium for
predation and self-defense. Maintenance of this internal calcium balance is critical to the nervous
system in jellyfish as well as humans.
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Aequorea Victorea Were First Found in Puget Sound by Researchers at the Friday Harbor Laboratories
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Aequorin has been used as a calcium indicator for several decades in laboratory settings
(Ridgeway, 1967 [2]). The function of aequorin is unique
from any other calcium-binding protein and has several distinguishing characteristics:
Aequorin is non-toxic and does not interfere with internal cellular stoichiometry.
(Miller et al., 1994 [3]) Each molecule of aequorin will bind with
three calcium ions (Inouye et al., 1985 [4]).
The protein is non-toxic when introduced into foreign cells (Blinks, 1990 [5]).
Aequorin is considered a ‘relative’ to the calcium-regulated effector protein calmodulin
(Tsuji et al., 1995 [6]), which plays an important part in controlling a variety of cellular
functions. Aequorin is from a family of calcium-binding proteins known as the EF-hand family.
EF-hand proteins also constitute the other CaBPs endogenous to the human body.
Aequorin and many of these endogenous proteins (i.e. calmodulin, parvalbumin, calbindin, calretinin)
are homologous in structure and show strong nucleotide sequence similarity (Moncrief et al. 1990 [7], Tsuji et al., 1995 [8]).
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Bibliography
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