TY  - GEN
T1  - GPN-1/glypican and UNC-52/perlecan do not appear to function in BMP signaling to pattern the C. elegans postembryonic mesoderm
AU  - DeGroot, Melisa S
AU  - Greer, Robert
AU  - Liu, Jun
DO  - 10.17912/micropub.biology.000437
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000437/
AB  - Heparan sulfate proteoglycans (HSPGs) are macromolecules composed of a protein core decorated with glycosaminoglycan (GAG) chains. These highly diverse molecules are classified based on their localization at the membrane or being secreted as part of the extracellular matrix (ECM), such as glypicans or perlecans, respectively (Sarrazin et al. 2011). HSPGs have been shown to play a structural role in the ECM as well as in the distribution of growth factors, such as transforming growth factor-β (TGF-β), fibroblast growth factor (FGF), Wnt, and Hedgehog (Hh), within tissues through highly specific binding interactions (Lin and Perrimon 2000). In vitro studies have demonstrated that human perlecan can bind to the BMP2 ligand (Decarlo et al. 2012). Understanding the biological roles of HSPGs in cell signaling has implications in disease diagnosis and potential treatment.
PY  - 2021
JO  - microPublication Biology
ER  -