Molecular cloning, characterization and 3D modelling of spotted snakehead fbn1 C-terminal region encoding asprosin and expression analysis of fbn1
Abstract The FBN1 gene encodes profibrillin protein that is cleaved by the enzyme furin to release fibrillin-1 and a glucogenic hormone, asprosin. Asprosin is implicated in diverse metabolic functions as well as pathological conditions in mammals. However, till date, there are no studies on asprosin...
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Nature Portfolio
2023-03-01
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Online Access: | https://doi.org/10.1038/s41598-023-31271-x |
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author | Priyanka Sathoria Bhawna Chuphal Umesh Rai Brototi Roy |
author_facet | Priyanka Sathoria Bhawna Chuphal Umesh Rai Brototi Roy |
author_sort | Priyanka Sathoria |
collection | DOAJ |
description | Abstract The FBN1 gene encodes profibrillin protein that is cleaved by the enzyme furin to release fibrillin-1 and a glucogenic hormone, asprosin. Asprosin is implicated in diverse metabolic functions as well as pathological conditions in mammals. However, till date, there are no studies on asprosin in any non-mammalian vertebrate. In this study, we have retrieved the spotted snakehead Channa punctata fbn1 gene (ss fbn1) from the testicular transcriptome data and validated it. The transcript is predicted to encode 2817 amino acid long putative profibrillin protein. Amino acid sequence alignment of deduced ss profibrillin with human profibrillin revealed that the furin cleavage site in profibrillin is well conserved in C. punctata. Further, differential expression of ss fbn1 was observed in various tissues with the highest expression in gonads. Prominent expression of furin was also observed in the gonads suggesting the possibility of proteolytic cleavage of profibrillin protein and secretion of asprosin in C. punctata. In addition, the C-terminal of the fbn1 gene of C. punctata that codes for asprosin protein has been cloned. Using in silico approach, physicochemical properties of the putative ss asprosin were characterized and post-translational changes were predicted. The putative ss asprosin protein sequence is predicted to consist of 142 amino acid residues, with conserved glycosylation sites. Further, the 3D model of ss asprosin was predicted followed by MD (molecular dynamics) simulation for energy minimization. Thus, the current study, for the first time in non-mammalian vertebrates, predicts and characterizes the novel protein asprosin using in silico approach. |
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language | English |
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spelling | doaj.art-3b54945803044ca4975e628b0a82ee9e2023-03-22T11:07:59ZengNature PortfolioScientific Reports2045-23222023-03-0113111110.1038/s41598-023-31271-xMolecular cloning, characterization and 3D modelling of spotted snakehead fbn1 C-terminal region encoding asprosin and expression analysis of fbn1Priyanka Sathoria0Bhawna Chuphal1Umesh Rai2Brototi Roy3Department of Zoology, Maitreyi College, University of DelhiDepartment of Zoology, University of DelhiUniversity of JammuDepartment of Zoology, Maitreyi College, University of DelhiAbstract The FBN1 gene encodes profibrillin protein that is cleaved by the enzyme furin to release fibrillin-1 and a glucogenic hormone, asprosin. Asprosin is implicated in diverse metabolic functions as well as pathological conditions in mammals. However, till date, there are no studies on asprosin in any non-mammalian vertebrate. In this study, we have retrieved the spotted snakehead Channa punctata fbn1 gene (ss fbn1) from the testicular transcriptome data and validated it. The transcript is predicted to encode 2817 amino acid long putative profibrillin protein. Amino acid sequence alignment of deduced ss profibrillin with human profibrillin revealed that the furin cleavage site in profibrillin is well conserved in C. punctata. Further, differential expression of ss fbn1 was observed in various tissues with the highest expression in gonads. Prominent expression of furin was also observed in the gonads suggesting the possibility of proteolytic cleavage of profibrillin protein and secretion of asprosin in C. punctata. In addition, the C-terminal of the fbn1 gene of C. punctata that codes for asprosin protein has been cloned. Using in silico approach, physicochemical properties of the putative ss asprosin were characterized and post-translational changes were predicted. The putative ss asprosin protein sequence is predicted to consist of 142 amino acid residues, with conserved glycosylation sites. Further, the 3D model of ss asprosin was predicted followed by MD (molecular dynamics) simulation for energy minimization. Thus, the current study, for the first time in non-mammalian vertebrates, predicts and characterizes the novel protein asprosin using in silico approach.https://doi.org/10.1038/s41598-023-31271-x |
spellingShingle | Priyanka Sathoria Bhawna Chuphal Umesh Rai Brototi Roy Molecular cloning, characterization and 3D modelling of spotted snakehead fbn1 C-terminal region encoding asprosin and expression analysis of fbn1 Scientific Reports |
title | Molecular cloning, characterization and 3D modelling of spotted snakehead fbn1 C-terminal region encoding asprosin and expression analysis of fbn1 |
title_full | Molecular cloning, characterization and 3D modelling of spotted snakehead fbn1 C-terminal region encoding asprosin and expression analysis of fbn1 |
title_fullStr | Molecular cloning, characterization and 3D modelling of spotted snakehead fbn1 C-terminal region encoding asprosin and expression analysis of fbn1 |
title_full_unstemmed | Molecular cloning, characterization and 3D modelling of spotted snakehead fbn1 C-terminal region encoding asprosin and expression analysis of fbn1 |
title_short | Molecular cloning, characterization and 3D modelling of spotted snakehead fbn1 C-terminal region encoding asprosin and expression analysis of fbn1 |
title_sort | molecular cloning characterization and 3d modelling of spotted snakehead fbn1 c terminal region encoding asprosin and expression analysis of fbn1 |
url | https://doi.org/10.1038/s41598-023-31271-x |
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