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Oncomodulin: The Enigmatic Parvalbumin Protein.

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.

SUBMITTER: Climer LK

PROVIDER: S-EPMC6794386 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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Oncomodulin: The Enigmatic Parvalbumin Protein.

Climer Leslie K LK Cox Andrew M AM Reynolds Timothy J TJ Simmons Dwayne D DD

Frontiers in molecular neuroscience 20191009

EF-hand Ca<sup>2+</sup>-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<sup>2+</sup>-binding protein and describe potential mechanisms of OCM function within the inner ear and immune cells. Add ...[more]

PMID: 31649505

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