Type III Intermediate Filaments Desmin, Glial Fibrillary Acidic Protein (GFAP), Vimentin, and Peripherin
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SummaryType 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.
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GFAP astrocytes were almost limited to layer II in CNT, while they were abundant throughout layers I-III in AD.
“Consistent with previous reports [90, 91] and similar to vimentin, GFAP astrocytes were almost limited to layer II in CNT, while they were abundant throughout layers I–III in AD.”
From Gliovascular alterations in sporadic and familial Alzheimer's disease: <scp><i>APOE3</i></scp> Christchurch homozygote glioprotection (2023) · cites this paper as [91]
Section 3.2.2 (page unavailable) reports increased GFAP in Alzheimer’s brain tissue, supporting the general association with AD. It does not report that GFAP-positive astrocytes are largely confined to layer II in controls or abundant across layers I–III in AD. (LLM, conf=0.82)
Experimental — accuracy not yet measuredAlteration of cell shape is one of the changes associated with astroglial reactivity and modification of vimentin and GFAP.
“alteration of cell shape is one of the changes associated with astroglial reactivity and modification of vimentin and GFAP [15, 28, 42, 43, 91].”
From Gliovascular alterations in sporadic and familial Alzheimer's disease: <scp><i>APOE3</i></scp> Christchurch homozygote glioprotection (2023) · cites this paper as [91]
Section 3.2.2 (GFAP in Reactive Gliosis; page unavailable) says reactive gliosis involves increased GFAP and vimentin and thicker intermediate-filament bundles in astrocytic processes. It does not explicitly identify altered cell shape as a feature of reactive gliosis; section 3.2.3 links morphology changes to filament-network changes in astrocytoma cells, a different setting. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAstroglial proliferation has also been related with GFAP upregulation.
“Astroglial proliferation has also been related with GFAP upregulation [71, 91, 110].”
From Gliovascular alterations in sporadic and familial Alzheimer's disease: <scp><i>APOE3</i></scp> Christchurch homozygote glioprotection (2023) · cites this paper as [91]
Section 3.2.2 (page not available) states that GFAP is upregulated in reactive astrocytes during gliosis. It does not establish that astroglial proliferation, specifically, is related to that upregulation; reactivity and proliferation are not interchangeable. (LLM, conf=0.84)
Experimental — accuracy not yet measuredFine‐tuned modification of astrocytic GFAP and vimentin expression is critical for the execution of the astrocyte reactive program.
“fine‐tuned modification of astrocytic GFAP and vimentin expression is critical for the execution of the astrocyte reactive program [28, 71, 91].”
From Gliovascular alterations in sporadic and familial Alzheimer's disease: <scp><i>APOE3</i></scp> Christchurch homozygote glioprotection (2023) · cites this paper as [91]
Section 3.2.2 (page unavailable) says GFAP and vimentin increase during reactive gliosis and that deficiency in GFAP or both proteins weakens the response. It does not establish that fine-tuned changes in their expression are critical for executing the reactive program; the section says the precise contributions of the intermediate-filament proteins need further study. (LLM, conf=0.86)
Experimental — accuracy not yet measuredGFAP influences astrocyte morphology.
“Considering the differential abundance of GFAP in AD and APOEch, and as GFAP influences astrocyte morphology [45, 91, 92, 93], we analyzed morphometric descriptors related to the scale, complexity, and shape of both the astrocytes themselves and their spatial domains.”
From Gliovascular alterations in sporadic and familial Alzheimer's disease: <scp><i>APOE3</i></scp> Christchurch homozygote glioprotection (2023) · cites this paper as [91]
Vimentin astrocytes were almost restricted to layer II in CNT, and their distribution in APOEch was remarkably similar, accumulating 80% of cells at around 500 μm in depth.
“As previously described for healthy brains [91], vimentin astrocytes were almost restricted to layer II in CNT, and their distribution in APOEch was remarkably similar to that, accumulating 80% of cells at around 500 μm in depth (Figure 2A,C).”
From Gliovascular alterations in sporadic and familial Alzheimer's disease: <scp><i>APOE3</i></scp> Christchurch homozygote glioprotection (2023) · cites this paper as [91]
The citation is attached to the comparison with healthy brains, not to the citing authors’ CNT and APOEch measurements. Our copy discusses astrocytes and vimentin, but the passages in §3.1.1 and §3.2.3 do not describe vimentin-positive astrocytes as nearly restricted to cortical layer II. Searches for layer II, cortical distribution, and the reported depth yielded no supporting passage; page numbers were not available. (LLM, conf=0.74)
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- Mitsui T, Kawajiri M, Kunishige M, Endo T, Akaike M, Aki K, Matsumoto T. 2000. Functional association between nicotinic acetylcholine recep- Type III Intermediate Filaments Cite this article as Cold Spring Harb Perspect Biol 2017;9:a021642 tor and sarcomeric proteins via actin and desmin filaments. J Cell Biochem 77: 584-595.
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- Authors
- Hol, E. M., & Capetanaki, Y.
- Affiliations
- Netherlands Institute for Neuroscience (NL)
- Academy of Athens (GR)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2017-12
- Volume
- 9
- Issue
- 12
- Pages
- a021642
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC5710105
- OpenAlex
- W2773697358
- Cited by
- 144
- References
- 150
- Citations by year
- 2026: 13 · 2025: 16 · 2024: 21 · 2023: 15 · 2022: 22 · 2021: 24 · 2020: 15 · 2019: 12 · 2018: 6
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KNAW Research Portal (The Royal Netherlands Academy of Arts and Sciences) (publishedVersion)
- KNAW research portal (Royal Academy of Art and Sciences (KNAW)) (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Funders
- Stichting voor Fundamenteel Onderzoek der Materie
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
- Hersenstichting
- Internationale Stichting Alzheimer Onderzoek
- National Institutes of Health
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR039617)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Keywords
- type III intermediate filaments, desmin, glial fibrillary acidic protein, vimentin, peripherin, cytoskeleton, muscle cells, brain cells, mesenchymal cells, cell death protection, aging
- MeSH terms
- Animals, Brain, Brain Neoplasms, Cell Nucleus, Cell Survival, Cytoskeleton, Desmin, Glial Fibrillary Acidic Protein, Gliosis, Humans, Intermediate Filaments, Lysosomes, Mitochondria, Muscles, Nervous System, Stress, Mechanical, Vimentin, Signal Transduction, Muscle, Skeletal, Molecular Chaperones, Myocytes, Cardiac, Mice, Mesenchymal Stem Cells, Peripherins
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