Mechanistic insight into the elastin degradation process by the metalloprotease myroilysin from the deep-sea bacterium Myroides profundi D25

Marine Drugs
Jie YangYu-Zhong Zhang

Abstract

Elastases have been widely studied because of their important uses as medicine and meat tenderizers. However, there are relatively few studies on marine elastases. Myroilysin, secreted by Myroides profundi D25 from deep-sea sediment, is a novel elastase. In this study, we examined the elastin degradation mechanism of myroilysin. When mixed with insoluble bovine elastin, myroilysin bound hydrophobically, suggesting that this elastase may interact with the hydrophobic domains of elastin. Consistent with this, analysis of the cleavage pattern of myroilysin on bovine elastin and recombinant tropoelastin revealed that myroilysin preferentially cleaves peptide bonds with hydrophobic residues at the P1 and/or P1' positions. Scanning electron microscopy (SEM) of cross-linked recombinant tropoelastin degraded by myroilysin showed preferential damages of spherules over cross-links, as expected for a hydrophobic preference. The degradation process of myroilysin on bovine elastin fibres was followed by light microscopy and SEM, revealing that degradation begins with the formation of crevices and cavities at the fibre surface, with these openings increasing in number and size until the fibre breaks into small pieces, which are subsequently ...Continue Reading

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Citations

Jan 29, 2017·International Journal of Biological Macromolecules·Kiran JyotiJitender Madan
Feb 3, 2020·Clinical & Experimental Metastasis·Arnoud W KasteleinChristianne A R Lok
Nov 20, 2018·Journal of Biomaterials Applications·Wenlan QiaoJing Guo
Dec 1, 2019·International Journal of Biological Macromolecules·Tingting RanWeiwu Wang

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Methods Mentioned

BETA
light
scanning electron microscopy

Software Mentioned

Quantity One
MASCOT MS MS Ion Research

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