parvalbumin


Also found in: Wikipedia.

par·val·bu·min

(par'val-byū'min), [MIM*168890]
Any of a group of small water-soluble calcium-binding proteins distinct from calmodulin and other calcium-binding proteins; found in the brain, skeletal muscle, and retina, but not in the heart, liver, or spleen, of various species.
[L. parvus, small, + albumin]

parvalbumin

A small, stable, water-soluble calcium-binding protein with three EF-hand-type-binding domains.
References in periodicals archive ?
Immunohistochemically, they are also positive for markers of proximal convoluted tubule (PCT) (CD10, carbonic anhydrase IX, vimentin, AMACR) as well as distal tubule/collecting duct (CK7, CK19, parvalbumin, BerEp4).
Paired-pulse facilitation at recurrent Purkinje neuron synapses is independent of calbindin and parvalbumin during high-frequency activation.
These entities can also be positive for PAX2, kidney-specific cadherin, carbonic anhydrase IX, and parvalbumin (3).
Other proteins such as calretinin, calbindin, and parvalbumin function as localized calcium buffers, especially in the pre- and postsynaptic regions, regulating Ca2+ densities to affect the sensitivity of the neuron to various stresses such as oxidative damage, ischemia, and depolarization.
Conversely, activation of these parvalbumin interneurons significantly reduces fear responses in rodents.
Previous studies have proposed the primary pathway is a parvalbumin positive pathway and the diffuse pathway is calbindin positive.
University researchers were able to pinpoint a specific protein, parvalbumin - which aids in high-speed relaxation of fast twitching muscles in nature - and optimize it to become a calcium sponge for heart muscle.
Several markers are available for these diagnostic goals, including the renal cell carcinoma marker antigen (RCCM), kidney-specific cadherin, cytokeratin subtypes, CD10, vimentin, alpha-methylacyl coenzyme A racemase, parvalbumin, and carbonic anhydrase IX.
Functional characterization of parvalbumin from the Arctic cod (Boreogadus saida): similarity in calcium affinity among parvalbumins from polar teleosts.
One possible reason for this difference is that calretinin and parvalbumin expression might be regulated at the translational level after blast exposures, which needs to be investigated further.
A recombinant hypoallergenic parvalbumin mutant for immunotherapy of IgE-mediated fish allergy.
The expression of parvalbumin is relatively low in both the central and the basomedial nuclei of the amygdala; the expression of calretinin and calbindin, however, shows some variation between these nuclei.