TY - JOUR
T1 - Sulfation is required for bone morphogenetic protein 2-dependent Id1 induction
AU - Osses, Nelson
AU - Gutierrez, Jaime
AU - Lopez-Rovira, Teresa
AU - Ventura, Francesc
AU - Brandan, Enrique
N1 - Funding Information:
This work was supported in part by grants from FONDAP-Biomedicine N° 13980001 (to E.B.), FONDECYT 2990088 (to N.O.), and MCyT BMC 2002-00737 (to F.V.). The research of E.B. was supported in part by an International Research Scholars grant from the Howard Hughes Medical Institute. The Millenium Institute for Fundamental and Applied Biology (MIFAB) is financed in part by the Ministerio de Planificación y Cooperación (Chile). N.O. was supported from a Fundacion Carolina Fellowship.
PY - 2006/6/16
Y1 - 2006/6/16
N2 - Different reports have suggested the dependence of bone morphogenetic protein (BMP) activity on the sulfated glycosaminoglycan (GAG) chains found in proteoglycans. However, the requirement of sulfated molecules in early BMP-2-signaling responses has not been established. We have used sodium chlorate to inhibit sulfation in C2C12 cells and have analyzed BMP-2 induction of Id1. We show here that sulfation inhibition strongly decreases the specific and early induction of Id1 at the transcriptional level. This effect is not reverted by the addition of extracellular components, such as GAGs or extracellular matrix (ECM). The inhibition of GAG incorporation into proteoglycans, or their removal by GAG lyases, does not mimic the negative effect on Id1 expression, while sulfation inhibition also represses the Id1-induction exerted by a constitutively active form of the BMP receptor, suggesting that BMP-2-mediated Id1 induction has an intracellular requirement for sulfated molecules.
AB - Different reports have suggested the dependence of bone morphogenetic protein (BMP) activity on the sulfated glycosaminoglycan (GAG) chains found in proteoglycans. However, the requirement of sulfated molecules in early BMP-2-signaling responses has not been established. We have used sodium chlorate to inhibit sulfation in C2C12 cells and have analyzed BMP-2 induction of Id1. We show here that sulfation inhibition strongly decreases the specific and early induction of Id1 at the transcriptional level. This effect is not reverted by the addition of extracellular components, such as GAGs or extracellular matrix (ECM). The inhibition of GAG incorporation into proteoglycans, or their removal by GAG lyases, does not mimic the negative effect on Id1 expression, while sulfation inhibition also represses the Id1-induction exerted by a constitutively active form of the BMP receptor, suggesting that BMP-2-mediated Id1 induction has an intracellular requirement for sulfated molecules.
KW - BMP-2
KW - Id1
KW - Muscle cells
KW - Proteoglycans
KW - Sulfation inhibitor
UR - http://www.scopus.com/inward/record.url?scp=33646481319&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2006.04.029
DO - 10.1016/j.bbrc.2006.04.029
M3 - Article
C2 - 16647687
AN - SCOPUS:33646481319
VL - 344
SP - 1207
EP - 1215
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -