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Identification of Low-Level Oxidation Products in Calmodulin Using NanoSpray ,,, Ion Trap Mass Spectrometry

Andreas Hhmer, Helen Tran, and William S. Hancock

Protein Oxidation

The data presented here can be acquired using any Thermo Finnigan LCQTMion trap mass spectrometer with MSn capability.

Introduction

Calmodulin (CaM) is the primary high-affinity Ca2+-binding protein present in most eukaryotic cells. It regulates a variety of cellular Ca2+-dependent signaling pathways and plays a role in many cellular events, including protein phosphorylation. Ca2+binding induces a large conformational change in CaM that exposes methionine (Met) residues for interaction with CaM-binding enzymes that are otherwise inaccessible. CaM (MW 16706.40) has an unusual amino acid composition consisting of 148 amino acids with a high proportion of acidic residues (>34%) resulting in an isoelectric point around 3.9. CaM is particularly rich in Met residues, which account for more than 5% of its total composition, but it lacks significant amounts of other oxidatively sensitive amino acids such as cysteine, histidine and tryptophan. Evidence presented recently suggests that Met residues in CaM undergo an age-dependent modification to methionine sulfoxide (MetSO) in vivo1. The biological consequences of this oxidation can vary depending on the specific site of the oxidation: MetSO at the Nterminal end of CaM had an effect on CaM-dependent nitric oxide synthase (type-I) whereas MetSO near the C-terminus affected CaM-dependent cyclic phosphodiesterase. 2,3 For a range of biochemical studies, the detailed characterization of the age-related oxidative changes in CaM is important. Typically, this analysis
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