search
for
 About Bioline  All Journals  Testimonials  Membership  News  Donations


Zoological Research
Kunming Institute of Zoology, Chinese Academy of Sciences
ISSN: 2095-8137
Vol. 38, No. 2, 2017, pp. 103-109
Bioline Code: zr17012
Full paper language: English
Document type: Report
Document available free of charge

Zoological Research, Vol. 38, No. 2, 2017, pp. 103-109

 en Characterization of cyclophilin D in freshwater pearl mussel (Hyriopsis schlegelii)
Liu, Xiu-Xiu; Wang, Cheng-Yuan; Luo, Chun; Sheng, Jun-Qing; Wu, Di; Hu, Bei-Juan; Wang, Jun-Hua & Hong, Yi-Jiang

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 check for this species in other resources . 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.

Keywords
Hyriopsis schlegelii; Cyclophilin D; Sequence analysis

 
© Copyright 2016 - Editorial Office of ZOOLOGICAL RESEARCH
Alternative site location: http://www.zoores.ac.cn/

Home Faq Resources Email Bioline
© Bioline International, 1989 - 2017, Site last up-dated on 16-Oct-2017.
Site created and maintained by the Reference Center on Environmental Information, CRIA, Brazil
System hosted by the Internet Data Center of Rede Nacional de Ensino e Pesquisa, RNP, Brazil