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Extracellular proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation.
Matrix Biol. 2006 Aug; 25(6):332-41.MB

Abstract

The onset and progression of skeletal muscle regeneration are controlled by a complex set of interactions between muscle precursor cells and their environment. Satellite cells constitute the main source of muscle precursor cells for growth and repair. After skeletal muscle injury, cell-derived signals induce their re-entry into the cell cycle and their migration into the damaged zone, where they proliferate and differentiate into mature myofibers. The surrounding extracellular matrix (ECM) together with inhibitory growth factors, such as transforming growth factor-beta (TGF-beta), also likely play an important role in growth control and muscle differentiation. Decorin, biglycan and betaglycan are proteoglycans that bind TGF-beta during skeletal muscle differentiation. In this paper, we show that the binding of TGF-beta to the receptors TGF-betaRI and-betaRII diminished in a satellite cell-derived cell line during differentiation, in spite of an increase expression of both receptors. In contrast, during the differentiation of decorin-null myoblasts (Dcn null), which lack decorin expression, the binding of TGF-beta to TGF-betaRI and -betaRII increased concomitantly with receptors levels. Both the addition and re-expression of decorin, in these myoblasts, diminished the binding of TGF-beta to its transducing receptors. Similar results were obtained when biglycan was added or over-expressed in Dcn null myoblasts. The binding of TGF-beta to TGF-betaRIII, alternatively known as betaglycan, was also augmented in Dcn null myoblasts and diminished by decorin, biglycan and betaglycan. These results suggest that decorin, biglycan and betaglycan compete for the binding of TGF-beta to its transducing receptors. Transfection studies with the TGF-beta-dependent promoter of the plasminogen activator inhibitor-1, coupled with luciferase, revealed that the addition of each proteoglycan diminished TGF-beta-dependent activity, for both TGF-beta1 and -beta2. The modulation of TGF-beta signaling by ECM proteoglycans diminishing the bio-availability of TGF-beta for its transducing receptors appears to be a feasible mechanism for the attenuation of this inhibitory growth factor during skeletal muscle formation.

Authors+Show Affiliations

Centro de Regulación Celular y Patología, Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, MIFAB, P. Universidad Católica de Chile, Santiago, Chile.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16766169

Citation

Droguett, Rebeca, et al. "Extracellular Proteoglycans Modify TGF-beta Bio-availability Attenuating Its Signaling During Skeletal Muscle Differentiation." Matrix Biology : Journal of the International Society for Matrix Biology, vol. 25, no. 6, 2006, pp. 332-41.
Droguett R, Cabello-Verrugio C, Riquelme C, et al. Extracellular proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation. Matrix Biol. 2006;25(6):332-41.
Droguett, R., Cabello-Verrugio, C., Riquelme, C., & Brandan, E. (2006). Extracellular proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation. Matrix Biology : Journal of the International Society for Matrix Biology, 25(6), 332-41.
Droguett R, et al. Extracellular Proteoglycans Modify TGF-beta Bio-availability Attenuating Its Signaling During Skeletal Muscle Differentiation. Matrix Biol. 2006;25(6):332-41. PubMed PMID: 16766169.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Extracellular proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation. AU - Droguett,Rebeca, AU - Cabello-Verrugio,Claudio, AU - Riquelme,Cecilia, AU - Brandan,Enrique, Y1 - 2006/04/27/ PY - 2006/03/15/received PY - 2006/04/19/revised PY - 2006/04/20/accepted PY - 2006/6/13/pubmed PY - 2007/1/11/medline PY - 2006/6/13/entrez SP - 332 EP - 41 JF - Matrix biology : journal of the International Society for Matrix Biology JO - Matrix Biol VL - 25 IS - 6 N2 - The onset and progression of skeletal muscle regeneration are controlled by a complex set of interactions between muscle precursor cells and their environment. Satellite cells constitute the main source of muscle precursor cells for growth and repair. After skeletal muscle injury, cell-derived signals induce their re-entry into the cell cycle and their migration into the damaged zone, where they proliferate and differentiate into mature myofibers. The surrounding extracellular matrix (ECM) together with inhibitory growth factors, such as transforming growth factor-beta (TGF-beta), also likely play an important role in growth control and muscle differentiation. Decorin, biglycan and betaglycan are proteoglycans that bind TGF-beta during skeletal muscle differentiation. In this paper, we show that the binding of TGF-beta to the receptors TGF-betaRI and-betaRII diminished in a satellite cell-derived cell line during differentiation, in spite of an increase expression of both receptors. In contrast, during the differentiation of decorin-null myoblasts (Dcn null), which lack decorin expression, the binding of TGF-beta to TGF-betaRI and -betaRII increased concomitantly with receptors levels. Both the addition and re-expression of decorin, in these myoblasts, diminished the binding of TGF-beta to its transducing receptors. Similar results were obtained when biglycan was added or over-expressed in Dcn null myoblasts. The binding of TGF-beta to TGF-betaRIII, alternatively known as betaglycan, was also augmented in Dcn null myoblasts and diminished by decorin, biglycan and betaglycan. These results suggest that decorin, biglycan and betaglycan compete for the binding of TGF-beta to its transducing receptors. Transfection studies with the TGF-beta-dependent promoter of the plasminogen activator inhibitor-1, coupled with luciferase, revealed that the addition of each proteoglycan diminished TGF-beta-dependent activity, for both TGF-beta1 and -beta2. The modulation of TGF-beta signaling by ECM proteoglycans diminishing the bio-availability of TGF-beta for its transducing receptors appears to be a feasible mechanism for the attenuation of this inhibitory growth factor during skeletal muscle formation. SN - 0945-053X UR - https://www.unboundmedicine.com/medline/citation/16766169/Extracellular_proteoglycans_modify_TGF_beta_bio_availability_attenuating_its_signaling_during_skeletal_muscle_differentiation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0945-053X(06)00046-1 DB - PRIME DP - Unbound Medicine ER -