Effect of nitric oxide and calpastatin on the inhibition of µ-calpain activity, autolysis and proteolysis of myofibrillar proteins. (1st March 2019)

• Record Type: Journal Article
• Authors: Liu, Rui; Lonergan, Steven; Steadham, Edward; Zhou, Guanghong; Zhang, Wangang; Huff-Lonergan, Elisabeth
• Is Part Of: Food chemistry. Volume 275(2019)
• Page Start: 77
• Page End: 84
• Publication Date: 2019-03-01
• Subjects: Nitric oxide -- S-nitrosylation -- Calpastatin -- µ-Calpain -- Protein degradation; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2018.09.104
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Nitric oxide could induce S-nitrosylation and the cross-linkage of calpain-1. Nitric oxide inhibits calpain-1 autolysis of both catalytic and regulatory unit. Nitric oxide and calpastatin have synergistic effect on calpain-1 proteolysis. Calpastatin potentially protects calpain-1 from the nitric oxide modification. Abstract: The aim of this study was to investigate the dual effect of the nitric oxide donor NOR-3 and calpastatin on µ-calpain activity, autolysis, and proteolytic ability. µ-Calpain and calpastatin were purified and allocated to the following five treatments: µ-calpain, µ-calpain + calpastatin, µ-calpain + NOR-3, µ-calpain + calpastatin + NOR-3, and µ-calpain + NOR-3 + calpastatin. µ-Calpain autolysis and the activity against purified myofibrils was initiated by addition of calcium. Results showed that NOR-3 could induce µ-calpain S-nitrosylation and effectively block the activity via the inhibition of µ-calpain autolysis. Calpastatin inhibited µ-calpain activity in a dose-dependent manner. The combined treatment of NOR-3 and calpastatin exerted a further inhibitory effect on µ-calpain activity, autolysis and proteolysis which was affected by the addition order of NOR-3 and calpastatin. Our data suggest that S-nitrosylation may play a regulatory role in mediating µ-calpain activity in the presence of calpastatin.