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Updated: Jun 25, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
A Ca(2+)-binding protein with numerous roles and uses: parvalbumin in molecular biology and physiology
1Section of Genetics, Department of Zoology, Aligarh Muslim University, Aligarh, UP, India. shasanamu@yahoo.co.uk
Abstract:
Parvalbumins (PVs) are acidic, intracellular Ca(2+)-binding proteins of low molecular weight. They are associated with several Ca(2+)-mediated cellular activities and physiological processes. It has been suggested that PV might function as a "Ca2+ shuttle" transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus, PV may contribute to the performance of rapid, phasic movements by accelerating the contraction-relaxation cycle of fast-twitch muscle fibers. Interestingly, PVs promote the generation of power stroke in fish by speeding up the rate of relaxation and thus provide impetus to attain maximal sustainable speeds. However, immunological monitoring of diverse tissues demonstrated that PVs are also present in non-muscle cells. The axoplasmic transport and various intracellular secretory mechanisms including the endocrine secretions seem to be controlled by the Ca2+ regulation machinery. Any defect in the Ca2+ handling apparatus may cause several clinical problems; for instance, PV deficiency alters the neuronal activity, a key mechanism leading to epileptic seizures. Moreover, atypical relaxation of the heart results in diastolic dysfunction, which is a major cause of heart failure predominantly among the aged people. PV may offer a unique potential to correct defective relaxation in energetically compromised failing hearts through PV gene transfer. Consequently, PV gene transfer may present a new therapeutic approach to correct cellular disturbances in Ca2+ signaling pathways of diseased organs. Hence, PVs appear to be amazingly useful candidate proteins regulating a variety of cellular functions through action on Ca2+ flux management.
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