Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer

The lysosomal aspartic proteinase cathepsin D is an acute phase protein involved in various physiological processes, including vitellogenesis, yolk processing and immune responses. In this study, we characterised the cathepsin D from the Asian seabass Lates calcarifer and examined its expression pro...

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Main Authors:	Shariza Azizan, Kiew, Lian Wan, Adura Mohd-Adnan
Format:	Article
Language:	English
Published:	Universiti Kebangsaan Malaysia 2014
Online Access:	http://journalarticle.ukm.my/7509/ http://journalarticle.ukm.my/7509/ http://journalarticle.ukm.my/7509/1/04_Shariza.pdf

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spelling	ukm-75092016-12-14T06:44:18Z http://journalarticle.ukm.my/7509/ Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer Shariza Azizan, Kiew, Lian Wan Adura Mohd-Adnan, The lysosomal aspartic proteinase cathepsin D is an acute phase protein involved in various physiological processes, including vitellogenesis, yolk processing and immune responses. In this study, we characterised the cathepsin D from the Asian seabass Lates calcarifer and examined its expression profile during infection. The complete coding sequence of L. calcarifer cathepsin D consists of 1191 nucleotides, encoding a 396 amino acid protein molecule that is made up of a putative signal peptide, a leader peptide and a mature peptide. Phylogenetic analyses showed that two types of cathepsin D are present in the teleost lineage i.e. cathepsin D1 and D2, whereas higher vertebrates possess only one type of cathepsin D. L. calcarifer cathepsin D was clustered together with cathepsin D1 from other teleosts. Compared to mammalian sequences, L. calcarifer cathepsin D lacks the β-hairpin loop that forms the double chain and is present as a single chain peptide with conserved aspartic active sites like other fish. Both multiple sequence alignment and phylogenetic analysis indicated that the L. calcarifer cathepsin D sequence codes for cathepsin D1 and suggested that it shares the same functions with cathepsin D from other fish. Expression profiling analysis of cathepsin D in L. calcarifer infected with Aeromonas hydrophila showed that it is up-regulated in immune-related tissues such as gills, spleen and liver, suggesting that cathepsin D plays an important role in the innate immune response of L. calcarifer against pathogens. Universiti Kebangsaan Malaysia 2014-08 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/7509/1/04_Shariza.pdf Shariza Azizan, and Kiew, Lian Wan and Adura Mohd-Adnan, (2014) Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer. Sains Malaysiana, 43 (8). pp. 1139-1148. ISSN 0126-6039 http://www.ukm.my/jsm
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Kebangasaan Malaysia
building	UKM Institutional Repository
collection	Online Access
language	English
description	The lysosomal aspartic proteinase cathepsin D is an acute phase protein involved in various physiological processes, including vitellogenesis, yolk processing and immune responses. In this study, we characterised the cathepsin D from the Asian seabass Lates calcarifer and examined its expression profile during infection. The complete coding sequence of L. calcarifer cathepsin D consists of 1191 nucleotides, encoding a 396 amino acid protein molecule that is made up of a putative signal peptide, a leader peptide and a mature peptide. Phylogenetic analyses showed that two types of cathepsin D are present in the teleost lineage i.e. cathepsin D1 and D2, whereas higher vertebrates possess only one type of cathepsin D. L. calcarifer cathepsin D was clustered together with cathepsin D1 from other teleosts. Compared to mammalian sequences, L. calcarifer cathepsin D lacks the β-hairpin loop that forms the double chain and is present as a single chain peptide with conserved aspartic active sites like other fish. Both multiple sequence alignment and phylogenetic analysis indicated that the L. calcarifer cathepsin D sequence codes for cathepsin D1 and suggested that it shares the same functions with cathepsin D from other fish. Expression profiling analysis of cathepsin D in L. calcarifer infected with Aeromonas hydrophila showed that it is up-regulated in immune-related tissues such as gills, spleen and liver, suggesting that cathepsin D plays an important role in the innate immune response of L. calcarifer against pathogens.
format	Article
author	Shariza Azizan, Kiew, Lian Wan Adura Mohd-Adnan,
spellingShingle	Shariza Azizan, Kiew, Lian Wan Adura Mohd-Adnan, Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer
author_facet	Shariza Azizan, Kiew, Lian Wan Adura Mohd-Adnan,
author_sort	Shariza Azizan,
title	Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer
title_short	Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer
title_full	Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer
title_fullStr	Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer
title_full_unstemmed	Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer
title_sort	molecular characterisation and expression analysis of cathepsin d from the asian seabass lates calcarifer
publisher	Universiti Kebangsaan Malaysia
publishDate	2014
url	http://journalarticle.ukm.my/7509/ http://journalarticle.ukm.my/7509/ http://journalarticle.ukm.my/7509/1/04_Shariza.pdf
first_indexed	2023-09-18T19:49:55Z
last_indexed	2023-09-18T19:49:55Z
_version_	1777406150392676352

Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer

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