Wound healing potential: evaluation of molecular profiling and amplification of Lucilia sericata angiopoietin-1 mRNA mid-part

• Published in: BMC research notes 2020-07, Vol.13 (1), p.308-308, Article 308
• Main Authors: Alipour, Hamzeh, Shahriari-Namadi, Marziae, Ebrahimi, Saeedeh, Moemenbellah-Fard, Mohammad D
• Format: Article
• Language: English
• Subjects: Amplification; Analysis; Angiogenesis; Angiopoietin; Angiopoietin-1 - genetics; Animals; Antibiotics; Bacterial infections; Blowflies; Calliphoridae - genetics; Chemical properties; Deoxyribonucleic acid; Design; Diabetes; Diptera; DNA; Drug resistance; Enzymes; Extracellular matrix; Genes, Insect - genetics; Genome, Insect - genetics; Growth factors; Homology; Infections; Insects; Iran; Larva; Lucilia sericata; Maximum likelihood method; mRNA; Physiological aspects; Polymerase chain reaction; Recombinant proteins; Research Note; RNA, Messenger - genetics; Sequence Analysis, Protein; Software; Studies; Therapy; Tropical diseases; Ulcers; Wound Healing
• ISSN: 1756-0500; 1756-0500
• DOI: 10.1186/s13104-020-05141-y

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. 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.