Parvalbumin

Group of acidic, water-soluble, calcium-binding proteins with a low molecular weight. Parvalbumin is related to calmodulin and troponin C and has so-called 3 EF hand structural motifs. The proteins belong to a subgroup of inhibitory Ca2+-binding GABAergic interneurons.

Parvalbumin is related to calmodulin and troponin C and has so-called 3 EF hand structural motifs that serve to bind calcium. Important allergens of animal and plant origin belong to the EF hand proteins. They bind both calcium and magnesium ions. The ion binding is important for the stability of the molecules.

Parvalbumines are expressed in various human tissues. They are found in the muscle tissue of all vertebrates and are involved in muscle relaxation. They are also found in the brain and in endocrine organs. Rapidly contracting muscles, especially the white muscle of fish, contain large amounts of parvalbumines. There are large fluctuations in the respective concentrations (e.g. high for herring, low for tuna fish with predominantly red meat).

1. Bublin M et al (2015) Cross-Reactive Human Single-Chain Antibody for Detection of Major Fish Allergen, Parvalbumins, and Identification of a Major IgE-Binding Epitope. PLoS One 10:e0142625.
2. Kobayashi Y et al (2016) Quantification of major allergen parvalbumin in 22 species of fish by SDS-PAGE. Food Chem 194:345-353.
3. Sano A et al. (2015) Two Cases of Occupational Contact Urticaria Caused by Percutaneous Sensitization to Parvalbumin. Case Rep Dermatol 7:227-232.