Abstract

Cyclophilin D (referred to as HsCypD) was obtained from the freshwater pearl mussel (Hyriopsis schlegelii). The full-length cDNA was 2 671 bp, encoding a protein consisting of 367 amino acids. HsCypD was determined to be a hydrophilic intracellular protein with 10 phosphorylation sites and four tetratricopeptide repeat (TPR) domains, but no signal peptide. The core sequence region YKGCIFHRIIKDFMVQGG is highly conserved in vertebrates and invertebrates. Phylogenetic tree analysis indicated that CypD from all species had a common origin, and HsCypD had the closest phylogenetic relationship with CypD from Lottia gigantea. The constitutive mRNA expression levels of HsCypD exhibited tissue-specific patterns, with the highest level detected in the intestines, followed by the gonads, and the lowest expression found in the hemocytes.

Highlights

  • Cyclophilin is a type of intracellular receptor of cyclosporin A (CsA)

  • The Cyclophilin D (CypD) protein protect cells from death that is induced by oxidative stress and mediated by mitochondria (Basso et al, 2005)

  • It is a key factor in the regulation of the mitochondrial permeability transition pore (MPTP), which plays a role in the release of cytochrome C and other apoptotic factors from mitochondria during cell apoptosis (Forte & Bernardi, 2006)

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Summary

Introduction

Cyclophilin is a type of intracellular receptor of cyclosporin A (CsA). It has a peptidyl-prolyl cis-trans isomerase (PPIase) region and can be combined with CsA (Feng & Xin, 2013). The CypD protein protect cells from death that is induced by oxidative stress and mediated by mitochondria (Basso et al, 2005). It is a key factor in the regulation of the mitochondrial permeability transition pore (MPTP), which plays a role in the release of cytochrome C and other apoptotic factors from mitochondria during cell apoptosis (Forte & Bernardi, 2006). CypD can suppress apoptosis when it is overexpressed (Li et al, 2004; Lin & Lechleiter, 2002; Schubert & Grimm, 2004)

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