TY - JOUR
T1 - Type III intermediate filaments desmin, glial fibrillary acidic protein (GFAP), vimentin, and peripherin
AU - Hol, Elly M.
AU - Capetanaki, Yassemi
N1 - Funding Information:
We thank Ismini Klookina for Figure 2I, George Ksistris for his artwork for Figure 3, Nicholas Flytzanis for reading the review, and Roland van Dijk and Martina Moeton for sharing their images for Figure 4. The human brain tissue in Figure 4 was obtained from the Netherlands Brain Bank. The authors’ work reviewed here was supported by ESPA 2007-2013 grants from the Greek General Secretariat of Research and Development/Ministerium of Education (PENED 01ED371, EPAN YB-22, PEP ATT-39, and ESPA 09SYN-21-965), grant of Excellence II/ ARISTEIA II 5342, and the U.S. National Institutes of Health RO1 AR39617 to Y.C., and COST (Cooperation of Science and Technology) BM (Biomedicine and Molecular Sciences) 1002, NWO (Nederlandse Organisatie voor Wetenschappelijk Onder-zoek), ISAO (Internationale Stichting Alzheimer Onder-zoek). FOM (Stichting voor Fundamenteel Onderzoek der Materie), Hersenstichting Nederland, Stichting Parkinson Fonds, and Dorpmans-Wigmans Stichting to E.M.H.
Funding Information:
We thank Ismini Klookina for Figure 2I, George Ksistris for his artwork for Figure 3, Nicholas Flytzanis for reading the review, and Roland van Dijk andMartinaMoeton for sharing their images for Figure 4. The human brain tissue in Figure 4 was obtained from the Netherlands Brain Bank. The authors’ work reviewed here was supported by ESPA 2007-2013 grants from the Greek General Secretariat of Research and Development/Ministerium of Education (PENED 01ED371, EPAN YB-22, PEP ATT-39, and ESPA 09SYN-21-965), grant of Excellence II/ARISTEIA II 5342, and the U.S. National Institutes of Health RO1 AR39617 to Y.C., and COST (Cooperation of Science and Technology) BM (Biomedicine and Molecular Sciences) 1002, NWO (Nederlandse Organisatie voor Wetenschappelijk Onderzoek), ISAO (Internationale Stichting Alzheimer Onderzoek). FOM (Stichting voor Fundamenteel Onderzoek derMaterie), HersenstichtingNederland, Stichting Parkinson Fonds, and Dorpmans-Wigmans Stichting to E.M.H.
Publisher Copyright:
© 2017 Cold Spring Harbor Laboratory Press; all rights reserved.
PY - 2017/12/1
Y1 - 2017/12/1
N2 - Type III intermediate filament (IF) proteins assemble into cytoplasmic homopolymeric and heteropolymeric filaments with other type III and some type IV IFs. These highly dynamic structures form an integral component of the cytoskeleton of muscle, brain, and mesenchymal cells. Here, we review the current ideas on the role of type III IFs in health and disease. It turns out that they not only offer resilience to mechanical strains, but, most importantly, they facilitate very efficiently the integration of cell structure and function, thus providing the necessary scaffolds for optimal cellular responses upon biochemical stresses and protecting against cell death, disease, and aging.
AB - Type III intermediate filament (IF) proteins assemble into cytoplasmic homopolymeric and heteropolymeric filaments with other type III and some type IV IFs. These highly dynamic structures form an integral component of the cytoskeleton of muscle, brain, and mesenchymal cells. Here, we review the current ideas on the role of type III IFs in health and disease. It turns out that they not only offer resilience to mechanical strains, but, most importantly, they facilitate very efficiently the integration of cell structure and function, thus providing the necessary scaffolds for optimal cellular responses upon biochemical stresses and protecting against cell death, disease, and aging.
UR - http://www.scopus.com/inward/record.url?scp=85036624058&partnerID=8YFLogxK
U2 - 10.1101/cshperspect.a021642
DO - 10.1101/cshperspect.a021642
M3 - Review article
AN - SCOPUS:85036624058
SN - 1943-0264
VL - 9
SP - 1
EP - 18
JO - Cold Spring Harbor Perspectives in Biology
JF - Cold Spring Harbor Perspectives in Biology
IS - 12
M1 - a021642
ER -