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Wound healing potential: evaluation of molecular profiling and amplification of Lucilia sericata angiopoietin-1 mRNA mid-part
OBJECTIVE: High prevalence of chronic ulcers and the burden of disease necessitate the increasingly significant production of new recombinant proteins in the world. The angiopoietin-1 enzyme is a part of the growth factors group which is secreted by Lucilia sericata (Diptera: Calliphoridae) larvae w...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7329540/ https://www.ncbi.nlm.nih.gov/pubmed/32611449 http://dx.doi.org/10.1186/s13104-020-05141-y |
Sumario: | OBJECTIVE: High prevalence of chronic ulcers and the burden of disease necessitate the increasingly significant production of new recombinant proteins in the world. The angiopoietin-1 enzyme is a part of the growth factors group which is secreted by Lucilia sericata (Diptera: Calliphoridae) larvae when they meet lesions to ensure maggot therapy. It is one of the most potent proteins in wound healing. Given its essential role, the angiopoietin-1 gene of L. sericata was characterized, which provided some necessary information on its identity. RESULTS: The mid-part of the angiopoietin-1 mRNA sequence was thus characterized based on the design of different primers such as exon-exon junction, conserved regions, and specific region primers via conventional polymerase chain reaction (PCR). Its structural features were configured by in silico method. The sequence of mid-part (390 bp) of angiopoietin-1 was determined empirically, and BLAST analysis unraveled its high identity (85%) with the sequence of angiopoietin-1 mRNA of the larval housefly, Musca domestica. The homology of this enzyme also exhibited that its nucleic acid sequence was very similar to the domains of angiopoietin-1 in Lucilia cuprina. The current data are instructive and critical to evaluate the action of this enzyme in recombinant protein production in future molecular studies on wound healing. |
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