TY - JOUR
T1 - The fibrillin microfibril scaffold
T2 - A niche for growth factors and mechanosensation?
AU - Sengle, Gerhard
AU - Sakai, Lynn Y.
N1 - Funding Information:
We thank the many individuals who have contributed to the results and concepts discussed in this review. We also gratefully acknowledge our funding sources (Shriners Hospitals for Children (grant # 85110 to LYS), National Institutes of Health ( P01 AR049698 to LYS), the Marfan Foundation (to LYS), and the Deutsche Forschungsgemeinschaft ( SFB829 /Project B12 to GS)).
Publisher Copyright:
© 2015.
PY - 2015/9/1
Y1 - 2015/9/1
N2 - The fibrillins, large extracellular matrix molecules, are polymerized to form "microfibrils." The fibrillin microfibril scaffold is populated by microfibril-associated proteins and by growth factors, which are likely to be latent. The scaffold, associated proteins, and bound growth factors, together with cellular receptors that can sense the microfibril matrix, constitute the fibrillin microenvironment. Activation of TGFβ signaling is associated with the Marfan syndrome, which is caused by mutations in fibrillin-1. Today we know that mutations in fibrillin-1 cause the Marfan syndrome as well as Weill-Marchesani syndrome (and other acromelic dysplasias) and result in opposite clinical phenotypes: tall or short stature; arachnodactyly or brachydactyly; joint hypermobility or stiff joints; hypomuscularity or hypermuscularity. We also know that these different syndromes are associated with different structural abnormalities in the fibrillin microfibril scaffold and perhaps with specific cellular receptors (mechanosensors). How does the microenvironment, framed by the microfibril scaffold and populated by latent growth factors, work? We must await future investigations for the molecular and cellular mechanisms that will answer this question. However, today we can appreciate the importance of the fibrillin microfibril niche as a contextual environment for growth factor signaling and potentially for mechanosensation.
AB - The fibrillins, large extracellular matrix molecules, are polymerized to form "microfibrils." The fibrillin microfibril scaffold is populated by microfibril-associated proteins and by growth factors, which are likely to be latent. The scaffold, associated proteins, and bound growth factors, together with cellular receptors that can sense the microfibril matrix, constitute the fibrillin microenvironment. Activation of TGFβ signaling is associated with the Marfan syndrome, which is caused by mutations in fibrillin-1. Today we know that mutations in fibrillin-1 cause the Marfan syndrome as well as Weill-Marchesani syndrome (and other acromelic dysplasias) and result in opposite clinical phenotypes: tall or short stature; arachnodactyly or brachydactyly; joint hypermobility or stiff joints; hypomuscularity or hypermuscularity. We also know that these different syndromes are associated with different structural abnormalities in the fibrillin microfibril scaffold and perhaps with specific cellular receptors (mechanosensors). How does the microenvironment, framed by the microfibril scaffold and populated by latent growth factors, work? We must await future investigations for the molecular and cellular mechanisms that will answer this question. However, today we can appreciate the importance of the fibrillin microfibril niche as a contextual environment for growth factor signaling and potentially for mechanosensation.
KW - Bone morphogenetic protein
KW - Fibrillin
KW - LTBP
KW - Marfan syndrome
KW - Mechanosensation
KW - TGFβ
KW - Weill-Marchesani syndrome
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U2 - 10.1016/j.matbio.2015.05.002
DO - 10.1016/j.matbio.2015.05.002
M3 - Review article
C2 - 25957947
AN - SCOPUS:84943665692
SN - 0945-053X
VL - 47
SP - 3
EP - 12
JO - Collagen and Related Research
JF - Collagen and Related Research
ER -