Safety assessment of the calcium-binding protein, apoaequorin, expressed by Escherichia coli.

  title={Safety assessment of the calcium-binding protein, apoaequorin, expressed by Escherichia coli.},
  author={Daniel L Moran and A. Tetteh and R. Goodman and Mark Y. Underwood},
  journal={Regulatory toxicology and pharmacology : RTP},
  volume={69 2},
Calcium-binding proteins are ubiquitous modulators of cellular activity and function. Cells possess numerous calcium-binding proteins that regulate calcium concentration in the cytosol by buffering excess free calcium ion. Disturbances in intracellular calcium homeostasis are at the heart of many age-related conditions making these proteins targets for therapeutic intervention. A calcium-binding protein, apoaequorin, has shown potential utility in a broad spectrum of applications for human… Expand
Subchronic toxicity of lyophilized apoaequorin protein powder in Sprague-Dawley rats
Apoaequorin is a bioluminescent calcium-binding apoprotein endogenous to the Aequorea species of jellyfish and is commercially available in a dietary supplement in support of brain and cognitiveExpand
Food safety assessment of Cry8Ka5 mutant protein using Cry1Ac as a control Bt protein.
  • D. Farias, M. P. Viana, +6 authors A. F. Carvalho
  • Biology, Medicine
  • Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association
  • 2015
The history of safe use revealed no convincing hazard reports for Bt pesticides and three-domain Cry proteins, and the bioinformatics analysis with the primary amino acids sequence of Cry8Ka5 showed no similarity to any known toxic, antinutritional or allergenic proteins. Expand
Computational comparison of a calcium-dependent jellyfish protein (apoaequorin) and calmodulin-cholesterol in short-term memory maintenance
The results suggest that a physiological calmodulin-cholesterol complex, not cholesterol-free jellyfish protein, may better serve as a dietary supplement to facilitate memory maintenance. Expand
Lipid emulsion enhances fish allergen parvalbumin's resistance to in vitro digestion and IgG/IgE binding capacity.
Lipid emulsion decreased the digestive ability of PV in stomach, increasing resistance to gastrointestinal digestion by pepsin proteases and altered IgG/IgEbinding ability of digestion products, thereby indicating that PV with lipid emulsion was resistant to digestion and possessed increased IgE binding ability resulting in higher risk of allergy among sensitized individuals. Expand
In silico tools for exploring potential human allergy to proteins
Information concerning PeptideRanker, as well as the Hydrophobic Cluster Analysis (HCA) method used for identifying IgE-binding epitopes in food allergens is discussed. Expand
Bioactive Compounds of Nutraceutical Value from Fishery and Aquaculture Discards
The possible valorisation of seafood and their by-products are focused on, which represent a source of biomolecules, useful for the sustainable production of high-value nutraceutical compounds in the authors' circular economy era. Expand
Nutraceuticals for Cognitive Dysfunction
Various nutraceuticals and substances that have potential to improve cognition and memory in senior dogs and cats are described. Expand


Calcium-binding proteins: basic concepts and clinical implications.
  • C. Heizmann
  • Biology, Medicine
  • General physiology and biophysics
  • 1992
Another protein family are the annexins, members of which interact with phospholipids and cellular membranes in a calcium-dependent manner, and in some cases members of the annexin family were even found to interact with EF-hand proteins. Expand
Digestive Stability in the Context of Assessing the Potential Allergenicity of Food Proteins
The relationship of the resistance to digestion by pepsin and the likelihood that a dietary protein is an allergen was identified as a means of aiding the assessment of proteins added to commodity crops through biotechnology. Expand
A multi-laboratory evaluation of a common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins.
Overall, assay pH did not influence the time to disappearance of the full-length protein or protein fragments, however, results across laboratories were more consistent at pH 1.2 than pH 2.0, demonstrating that this common protocol for evaluating the in vitro digestibility of proteins is reproducible and yields consistent results when performed using the same proteins at different laboratories. Expand
Calcium-binding proteins.
Safety assessment of Apoaequorin, a protein preparation: subchronic toxicity study in rats.
The No Observed-Adverse-Effect Level (NOAEL) for Apoaequorin was determined as 666.7 mg/kg bw/day, the highest dose tested, based on the results of this study. Expand
Measurement of cytosolic free calcium in mammalian cells with aequorin.
Evidence is presented that the aequorin-Ca light signal originates in the cytosol and that the cells subjected to the HOST procedure have a normal viability and functional integrity with respect to growth, respiration, membrane transport calcium metabolism, and hormone responsiveness. Expand
Stability of food allergens to digestion in vitro
The data are consistent with the hypothesis that food allergens must exhibit sufficient gastric stability to reach the intestinal mucosa where absorption and sensitization can occur, and indicate the stability to digestion is a significant and valid parameter that distinguishes food allergen from nonallergens. Expand
Crystal Structure of a Ca2+-discharged Photoprotein
The crystal structure of the Ca2+-discharged photoprotein obelin is reported and a significant repositioning and flipping of the His-175 imidazole ring as crucially required in the trigger hypothesis are lent support to the proposed mechanisms and provide new structural insight into details of these processes. Expand
Establishing objective detection limits for the pepsin digestion assay used in the assessment of genetically modified foods.
Differences in pH and pepsin concentration only had minor effects on digestion of intermediately stable proteins: concanavalin A, ovalbumin, and lysozyme, but not on rapidly digested or stable proteins. Expand
All three Ca2+‐binding loops of photoproteins bind calcium ions: The crystal structures of calcium‐loaded apo‐aequorin and apo‐obelin
There are easily discerned shifts in both helix and loop regions, and it is suggested that these subtle shifts are the basis of the ability of these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. Expand