Next Article in Journal
New Biscoumarin Derivatives: Synthesis, Crystal Structure, Theoretical Study and Antibacterial Activity against Staphylococcus aureus
Next Article in Special Issue
Purification and Characterization of Chitinases from Ridgetail White Prawn Exopalaemon carinicauda
Previous Article in Journal
Novel Polyprenylated Phloroglucinols from Hypericum sampsonii
Previous Article in Special Issue
Artificial and Natural Sialic Acid Precursors Influence the Angiogenic Capacity of Human Umbilical Vein Endothelial Cells
Open AccessArticle

Profiling of Concanavalin A-Binding Glycoproteins in Human Hepatic Stellate Cells Activated with Transforming Growth Factor-β1

1
Department of Genetics and Molecular Biology, Xi'an Jiaotong University College of Medicine, Xi'an 710061, Shaanxi, China
2
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, Shaanxi, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Molecules 2014, 19(12), 19845-19867; https://doi.org/10.3390/molecules191219845
Received: 27 September 2014 / Revised: 18 November 2014 / Accepted: 24 November 2014 / Published: 28 November 2014
(This article belongs to the Collection Advances in Carbohydrate Chemistry)
Glycoproteins play important roles in maintaining normal cell functions depending on their glycosylations. Our previous study indicated that the abundance of glycoproteins recognized by concanavalin A (ConA) was increased in human hepatic stellate cells (HSCs) following activation by transforming growth factor-β1 (TGF-β1); however, little is known about the ConA-binding glycoproteins (CBGs) of HSCs. In this study, we employed a targeted glycoproteomics approach using lectin-magnetic particle conjugate-based liquid chromatography-tandem mass spectrometry to compare CBG profiles between LX-2 HSCs with and without activation by TGF-β1, with the aim of discovering novel CBGs and determining their possible roles in activated HSCs. A total of 54 and 77 proteins were identified in the quiescent and activated LX-2 cells, respectively. Of the proteins identified, 14.3% were glycoproteins and 73.3% were novel potential glycoproteins. Molecules involved in protein processing in the endoplasmic reticulum (e.g., calreticulin) and calcium signaling (e.g., 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase β-2 [PLCB2]) were specifically identified in activated LX-2 cells. Additionally, PLCB2 expression was upregulated in the cytoplasm of the activated LX-2 cells, as well as in the hepatocytes and sinusoidal cells of liver cirrhosis tissues. In conclusion, the results of this study may aid future investigations to find new molecular mechanisms involved in HSC activation and antifibrotic therapeutic targets. View Full-Text
Keywords: ConA-binding glycoprotein; hepatic stellate cells; transforming growth factor-β1; mass spectrometry; peptides; KEGG pathway ConA-binding glycoprotein; hepatic stellate cells; transforming growth factor-β1; mass spectrometry; peptides; KEGG pathway
Show Figures

Figure 1

MDPI and ACS Style

Qin, Y.; Zhong, Y.; Yang, G.; Ma, T.; Jia, L.; Huang, C.; Li, Z. Profiling of Concanavalin A-Binding Glycoproteins in Human Hepatic Stellate Cells Activated with Transforming Growth Factor-β1. Molecules 2014, 19, 19845-19867.

Show more citation formats Show less citations formats

Article Access Map by Country/Region

1
Only visits after 24 November 2015 are recorded.
Search more from Scilit
 
Search
Back to TopTop