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The Anti-Angiogenic Activity of a Cystatin F Homologue from the Buccal Glands of

Overview
Journal Mar Drugs
Publisher MDPI
Specialties Biology
Pharmacology
Date 2018 Dec 2
PMID 30501116
Citations 1
Authors
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Abstract

Cystatins are a family of cysteine protease inhibitors which are associated with a variety of physiological and pathological processes in vivo. In the present study, the cDNA sequence of a cystatin F homologue called Lm-cystatin F was cloned from the buccal glands of . Although Lm-cystatin F shares a lower homology with cystatin superfamily members, it is also composed of a signal peptide and three highly conserved motifs, including the G in the N-terminal, QXVXG, as well as the PW in the C-terminal of the sequence. After sequence optimization and recombination, the recombinant protein was expressed as a soluble protein in with a molecular weight of 19.85 kDa. Through affinity chromatography and mass spectrometry analysis, the purified protein was identified as a recombinant Lm-cystatin F (rLm-cystatin F). Additionally, rLm-cystatin F could inhibit the activity of papain. Based on MTT assay, rLm-cystatin F inhibited the proliferation of human umbilical vein endothelial cells (HUVECs) dose dependently with an IC of 5 μM. In vitro studies show that rLm-cystatin F suppressed the adhesion, migration, invasion, and tube formation of HUVECs, suggesting that rLm-cystatin F possesses anti-angiogenic activity, which provides information on the feeding mechanisms of and insights into the application of rLm-cystatin F as a potential drug in the future.

Citing Articles

Marine Compounds and Cancer: Updates 2020.

Dyshlovoy S, Honecker F Mar Drugs. 2020; 18(12).

PMID: 33333876 PMC: 7765281. DOI: 10.3390/md18120643.

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