Characterization of cyclophilin D in freshwater pearl mussel ().

Zool Res

School of Life Sciences, Nanchang University, Nanchang Jiangxi 330031, China; Key Laboratory of Aquatic Animals Resources and Utilization of Jiangxi, Nanchang University, Nanchang Jiangxi 330031, China.

Published: March 2017

AI Article Synopsis

  • Cyclophilin D (HsCypD) was isolated from the freshwater pearl mussel, identified with a full-length cDNA of 2,671 bp that encodes a 367-amino-acid protein.
  • HsCypD is characterized as a hydrophilic intracellular protein with 10 phosphorylation sites, four tetratricopeptide repeat (TPR) domains, and lacks a signal peptide.
  • Phylogenetic analysis suggests a common ancestry for CypD across species, with HsCypD most closely related to that from the sea snail Lottia gigantea, and its mRNA expression shows tissue-specific patterns peaking in the intestines.

Article Abstract

Cyclophilin D (referred to as ) was obtained from the freshwater pearl mussel (). 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 exhibited tissue-specific patterns, with the highest level detected in the intestines, followed by the gonads, and the lowest expression found in the hemocytes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5396027PMC
http://dx.doi.org/10.24272/j.issn.2095-8137.2017.018DOI Listing

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