Journal
INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE
Volume 39, Issue 5, Pages 1072-1082Publisher
SPANDIDOS PUBL LTD
DOI: 10.3892/ijmm.2017.2941
Keywords
Spirulina sp.; angiotensin I-converting enzyme; angiotensin II; vascular dysfunction; mitogen-activated protein kinases
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Funding
- Marine Biotechnology Program - Ministry of Oceans and Fisheries, Republic of Korea [20150220]
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In this study, a marine microalga Spirulina sp.derived protein was hydrolyzed using gastrointestinal enzymes to produce an angiotensin I (Ang I)-converting enzyme (ACE) inhibitory peptide. Following consecutive purification, the potent ACE inhibitory peptide was composed of 7 amino acids, Thr-Met-Glu-Pro-Gly-Lys-Pro (molecular weight, 759 Da). Analysis using the Lineweaver-Burk plot and molecular modeling suggested that the purified peptide acted as a mixed non-competitive inhibitor of ACE. The inhibitory effects of the peptide against the cellular production of vascular dysfunction- related factors induced by Ang II were also investigated. In human endothelial cells, the Ang II-induced production of nitric oxide and reactive oxygen species was inhibited, and the expression of inducible nitric oxide synthase (iNOS) and endothelin-1 (ET-1) was downregulated when the cells were cultured with the purified peptide. Moreover, the peptide blocked the activation of p38 mitogen-activated protein kinase. These results indicated that this Spirulina sp.-derived peptide warrants further investigation as a potential pharmacological inhibitor of ACE and vascular dysfunction.
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