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Related Experiment Video

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Osmotic Avoidance in Caenorhabditis elegans: Synaptic Function of Two Genes, Orthologues of Human NRXN1 and NLGN1, as Candidates for Autism

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An evolutionarily ancient NO synthase (NOS) in shrimp.

Chun-Hung Wu¹, Vinu S Siva, Yen-Ling Song

¹Institute of Zoology, National Taiwan University, Taipei 10617, Taiwan, ROC.

Fish & Shellfish Immunology

|September 3, 2013

Summary

Researchers characterized a nitric oxide synthase (NOS) from tiger shrimp, revealing its ancient evolutionary origins and tissue-specific functions. This study enhances understanding of NO signaling in invertebrates.

Keywords:

Ancient Nitric oxide synthase Penaeus monodon PmNOS

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Published on: September 17, 2011

Area of Science:

Molecular Biology
Biochemistry
Marine Biology

Background:

Nitric oxide (NO) is a crucial signaling molecule involved in diverse physiological processes.
Nitric oxide synthase (NOS) enzymes synthesize NO, but their characterization in crustaceans is limited.
Understanding crustacean NOS is vital for comparative immunology and physiology.

Purpose of the Study:

To clone and biochemically characterize a nitric oxide synthase (NOS) from the tiger shrimp (Penaeus monodon).
To investigate the expression patterns, enzymatic activity, and evolutionary relationships of PmNOS.
To elucidate the role of PmNOS in shrimp immune responses and physiological functions.

Main Methods:

Cloning of the full-length PmNOS cDNA from shrimp haemocytes.
Bioinformatic analysis of the deduced amino acid sequence and phylogenetic assessment.
Quantitative mRNA expression analysis (RT-qPCR) and enzyme activity assays.
Biochemical characterization including cofactor dependency and calcium sensitivity.

Main Results:

The PmNOS cDNA sequence was determined, encoding a 1193-amino acid protein with conserved NOS domains.
PmNOS exhibited high sequence identity to invertebrate NOS and clustered separately from vertebrate isoforms.
PmNOS mRNA was widely distributed, with highest enzyme activity in nervous tissues and haemocytes.
Enzyme activity was dependent on NADPH and calcium/calmodulin, and NO production was linked to granulocytic cells.

Conclusions:

PmNOS represents an ancient form of NOS, predating vertebrate isoform diversification.
The enzyme plays a significant role in shrimp physiology, particularly in immune-related tissues like haemocytes.
This characterization provides a foundation for further research into NO-mediated processes in penaeid shrimp.