Next Article in Journal
Molecular Characterization of Voltage-Gated Sodium Channels and Their Relations with Paralytic Shellfish Toxin Bioaccumulation in the Pacific Oyster Crassostrea gigas
Next Article in Special Issue
ATG5 Promotes Death Signaling in Response to the Cyclic Depsipeptides Coibamide A and Apratoxin A
Previous Article in Journal
Asymmetric Total Synthesis of Ieodomycin B
Previous Article in Special Issue
Tumor Protein (TP)-p53 Members as Regulators of Autophagy in Tumor Cells upon Marine Drug Exposure
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessArticle
Mar. Drugs 2017, 15(1), 20;

Quantitative Proteomic Profiling of Tachyplesin I Targets in U251 Gliomaspheres

School of Applied Chemistry and Biotechnology, Shenzhen Polytechnic, No. 2190 Liuxian Road, Nanshan District, Shenzhen 518055, Guangdong, China
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Paul Long
Received: 20 November 2016 / Revised: 5 January 2017 / Accepted: 12 January 2017 / Published: 18 January 2017
(This article belongs to the Special Issue Marine Compounds as Modulators of Autophagy and Lysosomal Activity)
Full-Text   |   PDF [3978 KB, uploaded 18 January 2017]   |  


Tachyplesin I is a cationic peptide isolated from hemocytes of the horseshoe crab and its anti-tumor activity has been demonstrated in several tumor cells. However, there is limited information providing the global effects and mechanisms of tachyplesin I on glioblastoma multiforme (GBM). Here, by using two complementary proteomic strategies (2D-DIGE and dimethyl isotope labeling-based shotgun proteomics), we explored the effect of tachyplesin I on the proteome of gliomaspheres, a three-dimensional growth model formed by a GBM cell line U251. In total, the expression levels of 192 proteins were found to be significantly altered by tachyplesin I treatment. Gene ontology (GO) analysis revealed that many of them were cytoskeleton proteins and lysosomal acid hydrolases, and the mostly altered biological process was related to cellular metabolism, especially glycolysis. Moreover, we built protein–protein interaction network of these proteins and suggested the important role of DNA topoisomerase 2-alpha (TOP2A) in the signal-transduction cascade of tachyplesin I. In conclusion, we propose that tachyplesin I might down-regulate cathepsins in lysosomes and up-regulate TOP2A to inhibit migration and promote apoptosis in glioma, thus contribute to its anti-tumor function. Our results suggest tachyplesin I is a potential candidate for treatment of glioma. View Full-Text
Keywords: tachyplesin I; glioblastoma multiforme; cancer stem cell; stable isotope dimethyl labeling; parallel reaction monitoring tachyplesin I; glioblastoma multiforme; cancer stem cell; stable isotope dimethyl labeling; parallel reaction monitoring

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Li, X.; Dai, J.; Tang, Y.; Li, L.; Jin, G. Quantitative Proteomic Profiling of Tachyplesin I Targets in U251 Gliomaspheres. Mar. Drugs 2017, 15, 20.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top