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Identification and molecular characterization of Parkin in Clonorchis sinensis.

Bai X, Kim TI, Lee JY, Dai F, Hong SJ - Korean J. Parasitol. (2015)

Bottom Line: CsParkin was localized in the locomotive and male reproductive organs of C. sinensis adults, and extensively in metacercariae.Parkin has been found to participate in regulating mitochondrial function and energy metabolism in mammalian cells.From these results, it is suggested that CsParkin play roles in energy metabolism of the locomotive organs, and possibly in protein metabolism of the reproductive organs of C. sinensis.

View Article: PubMed Central - PubMed

Affiliation: Department of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul 156-756, Korea.

ABSTRACT
Clonorchis sinensis habitating in the bile duct of mammals causes clonorchiasis endemic in East Asian countries. Parkin is a RING-between-RING protein and has E3-ubiquitin ligase activity catalyzing ubiquitination and degradation of substrate proteins. A cDNA clone of C. sinensis was predicted to encode a polypeptide homologous to parkin (CsParkin) including 5 domains (Ubl, RING0, RING1, IBR, and RING2). The cysteine and histidine residues binding to Zn(2+) were all conserved and participated in formation of tertiary structural RINGs. Conserved residues were also an E2-binding site in RING1 domain and a catalytic cysteine residue in the RING2 domain. Native CsParkin was determined to have an estimated molecular weight of 45.7 kDa from C. sinensis adults by immunoblotting. CsParkin revealed E3-ubiquitin ligase activity and higher expression in metacercariae than in adults. CsParkin was localized in the locomotive and male reproductive organs of C. sinensis adults, and extensively in metacercariae. Parkin has been found to participate in regulating mitochondrial function and energy metabolism in mammalian cells. From these results, it is suggested that CsParkin play roles in energy metabolism of the locomotive organs, and possibly in protein metabolism of the reproductive organs of C. sinensis.

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Localization of CsParkin in the C. sinensis adults and metacercariae. Panels A and D, sperms (Sp) in seminal receptacle. Panels B and E, oral sucker (OS); Panels C and F, testis (Ts) and mesenchymal tissue (Ms); Panels G and H, metacercariae. Panels A, B, C, and G were probed with mouse anti-CsParkin immune sera, and Panels D, E, F, and H with normal mouse sera. For technical information, refer to the Materials and Methods.
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f7-kjp-53-1-65: Localization of CsParkin in the C. sinensis adults and metacercariae. Panels A and D, sperms (Sp) in seminal receptacle. Panels B and E, oral sucker (OS); Panels C and F, testis (Ts) and mesenchymal tissue (Ms); Panels G and H, metacercariae. Panels A, B, C, and G were probed with mouse anti-CsParkin immune sera, and Panels D, E, F, and H with normal mouse sera. For technical information, refer to the Materials and Methods.

Mentions: Immunohistochemical staining using mouse immune sera revealed native CsParkin in the developmental stages. In the adult worms, CsParkin was localized in the testes, sperms in the seminal receptacle and oral sucker. Weak staining was recognized in the mesenchymal tissues. In metacercariae, the CsParkin was extensively localized in the tegument, subtegument, mesenchymal tissues, and oral and ventral suckers (Fig. 7).


Identification and molecular characterization of Parkin in Clonorchis sinensis.

Bai X, Kim TI, Lee JY, Dai F, Hong SJ - Korean J. Parasitol. (2015)

Localization of CsParkin in the C. sinensis adults and metacercariae. Panels A and D, sperms (Sp) in seminal receptacle. Panels B and E, oral sucker (OS); Panels C and F, testis (Ts) and mesenchymal tissue (Ms); Panels G and H, metacercariae. Panels A, B, C, and G were probed with mouse anti-CsParkin immune sera, and Panels D, E, F, and H with normal mouse sera. For technical information, refer to the Materials and Methods.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4384794&req=5

f7-kjp-53-1-65: Localization of CsParkin in the C. sinensis adults and metacercariae. Panels A and D, sperms (Sp) in seminal receptacle. Panels B and E, oral sucker (OS); Panels C and F, testis (Ts) and mesenchymal tissue (Ms); Panels G and H, metacercariae. Panels A, B, C, and G were probed with mouse anti-CsParkin immune sera, and Panels D, E, F, and H with normal mouse sera. For technical information, refer to the Materials and Methods.
Mentions: Immunohistochemical staining using mouse immune sera revealed native CsParkin in the developmental stages. In the adult worms, CsParkin was localized in the testes, sperms in the seminal receptacle and oral sucker. Weak staining was recognized in the mesenchymal tissues. In metacercariae, the CsParkin was extensively localized in the tegument, subtegument, mesenchymal tissues, and oral and ventral suckers (Fig. 7).

Bottom Line: CsParkin was localized in the locomotive and male reproductive organs of C. sinensis adults, and extensively in metacercariae.Parkin has been found to participate in regulating mitochondrial function and energy metabolism in mammalian cells.From these results, it is suggested that CsParkin play roles in energy metabolism of the locomotive organs, and possibly in protein metabolism of the reproductive organs of C. sinensis.

View Article: PubMed Central - PubMed

Affiliation: Department of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul 156-756, Korea.

ABSTRACT
Clonorchis sinensis habitating in the bile duct of mammals causes clonorchiasis endemic in East Asian countries. Parkin is a RING-between-RING protein and has E3-ubiquitin ligase activity catalyzing ubiquitination and degradation of substrate proteins. A cDNA clone of C. sinensis was predicted to encode a polypeptide homologous to parkin (CsParkin) including 5 domains (Ubl, RING0, RING1, IBR, and RING2). The cysteine and histidine residues binding to Zn(2+) were all conserved and participated in formation of tertiary structural RINGs. Conserved residues were also an E2-binding site in RING1 domain and a catalytic cysteine residue in the RING2 domain. Native CsParkin was determined to have an estimated molecular weight of 45.7 kDa from C. sinensis adults by immunoblotting. CsParkin revealed E3-ubiquitin ligase activity and higher expression in metacercariae than in adults. CsParkin was localized in the locomotive and male reproductive organs of C. sinensis adults, and extensively in metacercariae. Parkin has been found to participate in regulating mitochondrial function and energy metabolism in mammalian cells. From these results, it is suggested that CsParkin play roles in energy metabolism of the locomotive organs, and possibly in protein metabolism of the reproductive organs of C. sinensis.

Show MeSH
Related in: MedlinePlus