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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| Format: | Article |
| Language: | English |
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Universiti Kebangsaan Malaysia
2014
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| Online Access: | http://journalarticle.ukm.my/7509/1/04_Shariza.pdf |
| _version_ | 1825726049442332672 |
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| author | Shariza Azizan, Kiew, Lian Wan Adura Mohd-Adnan, |
| author_facet | Shariza Azizan, Kiew, Lian Wan Adura Mohd-Adnan, |
| author_sort | Shariza Azizan, |
| collection | UKM |
| 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. |
| first_indexed | 2024-03-06T04:04:56Z |
| format | Article |
| id | ukm.eprints-7509 |
| institution | Universiti Kebangsaan Malaysia |
| language | English |
| last_indexed | 2024-03-06T04:04:56Z |
| publishDate | 2014 |
| publisher | Universiti Kebangsaan Malaysia |
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| spelling | ukm.eprints-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 |
| spellingShingle | Shariza Azizan, Kiew, Lian Wan Adura Mohd-Adnan, Molecular characterisation and expression analysis of cathepsin D from the Asian seabass lates calcarifer |
| title | 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_short | 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 |
| url | http://journalarticle.ukm.my/7509/1/04_Shariza.pdf |
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