Presentation_1_Oncomodulin: The Enigmatic Parvalbumin Protein.pdf (89.57 kB)
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Presentation_1_Oncomodulin: The Enigmatic Parvalbumin Protein.pdf

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posted on 09.10.2019, 04:20 by Leslie K. Climer, Andrew M. Cox, Timothy J. Reynolds, Dwayne D. Simmons

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.