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Molecular Cloning and Functional Characterization of Catalase in Stress Physiology, Innate Immunity, Testicular Development, Metamorphosis, and Cryopreserved Sperm of Pacific Abalone

Authors :
Shaharior Hossen
Zahid Parvez Sukhan
Soo Cheol Kim
Md. Abu Hanif
Il-Keun Kong
Kang Hee Kho
Source :
Antioxidants; Volume 12; Issue 1; Pages: 109
Publication Year :
2023
Publisher :
Multidisciplinary Digital Publishing Institute, 2023.

Abstract

Catalase is a crucial enzyme of the antioxidant defense system responsible for the maintenance of cellular redox homeostasis. The aim of the present study was to evaluate the molecular regulation of catalase (Hdh-CAT) in stress physiology, innate immunity, testicular development, metamorphosis, and cryopreserved sperm of Pacific abalone. Hdh-CAT gene was cloned from the digestive gland (DG) of Pacific abalone. The 2894 bp sequence of Hdh-CAT had an open reading frame of 1506 bp encoding 501 deduced amino acids. Fluorescence in situ hybridization confirmed Hdh-CAT localization in the digestive tubules of the DG. Hdh-CAT was induced by different types of stress including thermal stress, H2O2 induction, and starvation. Immune challenges with Vibrio, lipopolysaccharides, and polyinosinic–polycytidylic acid sodium salt also upregulated Hdh-CAT mRNA expression and catalase activity. Hdh-CAT responded to cadmium induced-toxicity by increasing mRNA expression and catalase activity. Elevated seasonal temperature also altered Hdh-CAT mRNA expression. Hdh-CAT mRNA expression was relatively higher at the trochophore larvae stage of metamorphosis. Cryopreserved sperm showed significantly lower Hdh-CAT mRNA expression levels compared with fresh sperm. Hdh-CAT mRNA expression showed a relationship with the production of ROS. These results suggest that Hdh-CAT might play a role in stress physiology, innate immunity, testicular development, metamorphosis, and sperm cryo-tolerance of Pacific abalone.

Details

Language :
English
ISSN :
20763921
Database :
OpenAIRE
Journal :
Antioxidants; Volume 12; Issue 1; Pages: 109
Accession number :
edsair.doi.dedup.....34a8a3e082c35085517cec82bca24497
Full Text :
https://doi.org/10.3390/antiox12010109