Abstract:

EF-hand Ca²⁺-binding protein family members, α- and β-parvalbumins have been studied for decades. Yet, considerable information is lacking distinguishing functional differences between mammalian α-parvalbumin (PVALB) and oncomodulin (OCM), a branded β-parvalbumin. Herein, we provide an overview detailing the current body of work centered around OCM as an EF-Hand Ca²⁺-binding protein and describe potential mechanisms of OCM function within the inner ear and immune cells. Additionally, we posit that OCM is evolutionarily distinct from PVALB and most other β-parvalbumins. This review summarizes recent studies pertaining to the function of OCM and emphasizes OCM as a parvalbumin possessing a unique cell and tissue distribution, Ca²⁺ buffering capacity and phylogenetic origin.

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Oncomodulin: The Enigmatic Parvalbumin Protein

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^{Department of Biology, Baylor University, Waco, TX, United States}

^{Department of Psychology and Neuroscience, Baylor University, Waco, TX, United States}

^{Biomedical Sciences Program, Baylor University, Waco, TX, United States}

Edited by: Beat Schwaller, Universitè de Fribourg, Switzerland

Reviewed by: Elizabeth K. Lucas, North Carolina State University, United States; Eugene Anatolievich Permyakov, Institute for Biological Instrumentation (RAS), Russia; Michael Thomas Henzl, University of Missouri, United States

*Correspondence: Dwayne D. Simmons ude.rolyab@snommis_enyawd

^{Co-first authors}

Edited by: Beat Schwaller, Universitè de Fribourg, Switzerland

Reviewed by: Elizabeth K. Lucas, North Carolina State University, United States; Eugene Anatolievich Permyakov, Institute for Biological Instrumentation (RAS), Russia; Michael Thomas Henzl, University of Missouri, United States

Received 2019 Jul 7; Accepted 2019 Sep 13.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

Abstract

EF-hand Ca^{-binding protein family members, α- and β-parvalbumins have been studied for decades. Yet, considerable information is lacking distinguishing functional differences between mammalian α-parvalbumin (PVALB) and oncomodulin (OCM), a branded β-parvalbumin. Herein, we provide an overview detailing the current body of work centered around OCM as an EF-Hand Ca}^{-binding protein and describe potential mechanisms of OCM function within the inner ear and immune cells. Additionally, we posit that OCM is evolutionarily distinct from PVALB and most other β-parvalbumins. This review summarizes recent studies pertaining to the function of OCM and emphasizes OCM as a parvalbumin possessing a unique cell and tissue distribution, Ca}^{buffering capacity and phylogenetic origin.}

Keywords: EF-hand Ca-binding protein ++, cochlea, hair cell, macrophage, beta parvalbumin, phylogeneticanalysis

Abstract

Acknowledgments

We thank Dr. E. Baker for advice and technical assistance on phylogenetic analyses. We also thank Drs. W. Marcotti, F. Ceriani, J. Niemi, and L. Benowitz for their helpful comments.

Acknowledgments

Footnotes

Funding. This work was supported in part by NIH grant DC013304.

Footnotes

Click here for additional data file.^{(90K, pdf)}

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