Description
Title: Why Use Parvalbumin?
Abstract: A member of the EF-hand superfamily, parvalbumin (PA) is a small, acidic, primarily cytosolic Ca2+-binding protein. Although the structural and physical characteristics of PA have been extensively studied, two highly conserved structural motifs (clusters I and II), each consisting of three amino acids, have recently come to light. These motifs help to form the hydrophobic core of the EF-hand domains. Even after decades of research, little is still understood about how PA affects physiological processes. Since PA’s target proteins have not yet been identified, it is thought that PA functions as a slow calcium buffer. Multiple studies using different muscle systems have demonstrated that PA speeds up the relaxation of fast skeletal muscles. Reactive oxygen species (ROS) have been found to oxidize PA in a conformation-dependent manner, suggesting that PA in fast muscles may serve the additional physiological function of shielding these cells from ROS. Gamma-aminobutyric acid (GABA) neurons are a population of calcium-dependent metabolic and electric processes that are thought to be regulated by PA. Changes in GABAergic synaptic transmission follow genetic PA elimination. The vestibular and cochlear outer hair cells express the most mammalian oncomodulin (OM), the isoform of PA. After three to four months, OM knockout mice lose their hearing. It was proposed that OM maintains auditory function in sensory cells, most likely by influencing the motility mechanisms of outer hair cells.
Keywords: parvalbumin; oncomodulin; structure; stability; calcium binding; physiological functions
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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