Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Jan 18;9:784983. doi: 10.3389/fcell.2021.784983

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2022 Guo, Wu, Lei, Zhong, Wang, Zhang, Zhao, Huang, Shi and Wu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Structure of SDC-1. (A) The SDC-1 core protein consists of three major (extracellular, transmembrane and cytoplasmic) domains. (B) The extracellular domain is bound via glycosaminoglycan (heparan sulfate, HS; chondroitin sulfate, CS) chains. The HS and CS chains are composed of repeating disaccharide units (glycan structures are represented according to the Symbol Nomenclature for Glycans (SNFG) (Cheng et al., 2017)) linked to core protein serine residues. Growth factors and receptors (e.g., HER2, VEGF, HGF and EGFR) bind to HS chains, which can be fragmented by heparanase. (C) The extracellular domain of SDC-1 is cleaved by sheddases (e.g., MMPs, ADAMs, MT-MMP), a phenomenon known as shedding. This results in the release of attached glycosaminoglycan chains as well as any bound ligands from the cell surface into the extracellular environment.