Alterations of intermediate filaments in various histopathological conditions

1995 ◽  
Vol 73 (9-10) ◽  
pp. 627-634 ◽  
Author(s):  
Monique Cadrin ◽  
Maria-Grazia Martinoli
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Lewy Bodies ◽  
Degenerative Diseases ◽  
Intermediate Filament Proteins ◽  
Mallory Bodies ◽  
Filament Structure ◽  
Cytoskeletal Component ◽  
Filament Networks ◽  
Precise Role

Intermediate filament proteins belong to a multigene family and constitute an important cytoskeletal component of most vertebrate cells. Their pattern of expression is tissue specific and is highly controlled during embryonic development. Numerous pathologies are known to be associated with modifications of intermediate filament organisation, although their precise role has not yet been elucidated. The present review focuses on the most recent data concerning the possible causes of intermediate filaments disorganization in specific pathologic conditions affecting the epidermis, the liver, and the nervous system. We discuss the formation of abnormal intermediate filament networks that arise as a consequence of mutations that directly affect intermediate filament structure or are induced by multifactorial causes such as modifications of post-translational processes and changes in the levels of expression.Key words: intermediate filaments, phosphorylation, Mallory bodies, Lewy bodies, degenerative diseases.

Paranemin and the organization of desmin filament networks

2001 ◽  
Vol 114 (6) ◽  
pp. 1079-1089 ◽  
Author(s):  
S.C. Schweitzer ◽  
M.W. Klymkowsky ◽  
R.M. Bellin ◽  
R.M. Robson ◽  
Y. Capetanaki ◽  
...  
Keyword(s):  
Cell Lines ◽  
Intermediate Filament ◽  
Transgene Expression ◽  
De Novo ◽  
Muscle Cells ◽  
The Other ◽  
Intermediate Filament Proteins ◽  
Mouse Fibroblasts ◽  
Filament Networks ◽  
Filament Network

De novo expression of vimentin, GFAP or peripherin leads to the assembly of an extended intermediate filament network in intermediate filament-free SW13/cl.2 cells. Desmin, in contrast, does not form extended filament networks in either SW13/cl.2 or intermediate filament-free mouse fibroblasts. Rather, desmin formed short thickened filamentous structures and prominent spot-like cytoplasmic aggregates that were composed of densely packed 9–11 nm diameter filaments. Analysis of stably transfected cell lines indicates that the inability of desmin to form extended networks is not due to a difference in the level of transgene expression. Nestin, paranemin and synemin are large intermediate filament proteins that coassemble with desmin in muscle cells. Although each of these large intermediate filament proteins colocalized with desmin when coexpressed in SW-13 cells, expression of paranemin, but not synemin or nestin, led to the formation of an extended desmin network. A similar rescue of desmin network organization was observed when desmin was coexpressed with vimentin, which coassembles with desmin, or with keratins, which formed a distinct filament network. These studies demonstrate that desmin filaments differ in their organizational properties from the other vimentin-like intermediate filament proteins and appear to depend upon coassembly with paranemin, at least when they are expressed in non-muscle cells, in order to form an extended filament network.

scholarly journals Assembly of type IV neuronal intermediate filaments in nonneuronal cells in the absence of preexisting cytoplasmic intermediate filaments

1993 ◽  
Vol 122 (6) ◽  
pp. 1323-1335 ◽  
Author(s):  
GY Ching ◽  
RK Liem
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Cultured Cells ◽  
Neuronal Cell ◽  
Intermediate Filament Protein ◽  
Amino Acid Residues ◽  
Intermediate Filament Proteins ◽  
Transfected Cells ◽  
Type Iv

We report here on the in vivo assembly of alpha-internexin, a type IV neuronal intermediate filament protein, in transfected cultured cells, comparing its assembly properties with those of the neurofilament triplet proteins (NF-L, NF-M, and NF-H). Like the neurofilament triplet proteins, alpha-internexin coassembles with vimentin into filaments. To study the assembly characteristics of these proteins in the absence of a preexisting filament network, transient transfection experiments were performed with a non-neuronal cell line lacking cytoplasmic intermediate filaments. The results showed that only alpha-internexin was able to self-assemble into extensive filamentous networks. In contrast, the neurofilament triplet proteins were incapable of homopolymeric assembly into filamentous arrays in vivo. NF-L coassembled with either NF-M or NF-H into filamentous structures in the transfected cells, but NF-M could not form filaments with NF-H. alpha-internexin could coassemble with each of the neurofilament triplet proteins in the transfected cells to form filaments. When all but 2 and 10 amino acid residues were removed from the tail domains of NF-L and NF-M, respectively, the resulting NF-L and NF-M deletion mutants retained the ability to coassemble with alpha-internexin into filamentous networks. These mutants were also capable of forming filaments with other wild-type neurofilament triplet protein subunits. These results suggest that the tail domains of NF-L and NF-M are dispensable for normal coassembly of each of these proteins with other type IV intermediate filament proteins to form filaments.

Molecular analysis of intermediate filament cytoskeleton--a putative load-bearing structure

1984 ◽  
Vol 246 (4) ◽  
pp. H566-H572 ◽  
Author(s):  
M. G. Price
Keyword(s):  
Skeletal Muscle ◽  
Molecular Analysis ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Direct Evidence ◽  
Two Dimensional ◽  
Myocardial Cells ◽  
Intermediate Filament Proteins ◽  
Bovine Myocardium ◽  
Bearing Structure

Myocardial cells contain a cytoskeleton of intermediate filaments connecting the myofibrils. The present molecular analysis of the myocardial cytoskeleton was designed to identify the intermediate filament proteins and examine their assembly properties. The intermediate filament proteins desmin and vimentin were isolated from adult bovine myocardium by sequential extraction, urea solubilization, and chromatography on hydroxylapatite and DEAE columns. Desmin was obtained virtually pure in one peak and in a mixture of desmin and vimentin in the trailing fractions. Intermediate filaments of different morphologies polymerized in the desmin and the desmin-vimentin fractions. Isolated myocardial desmin occurs as three isozymes and isolated myocardial vimentin as two isozymes, which co-migrate on two-dimensional gels with corresponding isozymes from bovine skeletal and smooth muscle. Polypeptides of 200,000 and 220,000 daltons that fractionate with myocardial desmin and vimentin are also present in cytoskeletons of smooth and skeletal muscle. The results provide direct evidence that myocardial desmin can assemble to form intermediate filaments, suggesting that desmin is the major component of the cytoskeletal filaments in cardiomyocytes.

scholarly journals Stiffening and inelastic fluidization in vimentin intermediate filament networks

Soft Matter ◽  
2019 ◽  
Vol 15 (36) ◽  
pp. 7127-7136 ◽  
Author(s):  
Anders Aufderhorst-Roberts ◽  
Gijsje H. Koenderink
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Shear Rheology ◽  
Cellular Processes ◽  
Filament Networks ◽  
Nonlinear Shear ◽  
Vimentin Intermediate Filament

Nonlinear shear rheology reveals that intermediate filaments balance two contradictory roles: mechanoprotection by stiffening and dynamic cellular processes through softening.

Differential effect of arginine modification with 1,2-cyclohexanedione on the capacity of vimentin and desmin to assemble into intermediate filaments and to bind to nucleic acids

1984 ◽  
Vol 65 (1) ◽  
pp. 1-20
Author(s):  
P. Traub ◽  
C.E. Vorgias
Keyword(s):  
Nucleic Acids ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Specific Interaction ◽  
Inhibitory Effect ◽  
Affinity Column ◽  
Intermediate Filament Proteins ◽  
Amino Terminal ◽  
Short Period ◽  
Arginine Residues

When the intermediate filament proteins vimentin and desmin were reacted for a short period of time with the arginine-specific reagent 1,2-cyclohexanedione, the modification had a severe, inhibitory effect on the assembly of intermediate filaments and on the susceptibility of the basic, amino-terminal polypeptide of both proteins to degradation by the intermediate filament-specific, Ca2+-activated proteinase. However, it had only a slightly inhibitory effect on the binding of vimentin and desmin to ribosomal RNA from Ehrlich ascites tumour cells. Since the Ca2+-activated proteinase is very likely to be a trypsin-like enzyme, with a preference for arginyl and lysyl peptide bonds, the results indicate that the arginine residues of the amino-terminal polypeptide of vimentin and desmin are highly essential for filament assembly but largely dispensable for the binding of both proteins to nucleic acids. This was supported by the observation that two breakdown products of vimentin lacking a 5 X 10(3) Mr and an 8 X 10(3) Mr polypeptide from the amino terminus, respectively, did not assemble into intermediate filaments but were still capable of binding to rRNA. Both polypeptides also bound to single-stranded DNA-cellulose under non-denaturing conditions, but passed the affinity column in the presence of 6 M-urea. Thus, the binding of vimentin to nucleic acids appears to be based on two components: a non-specific electrostatic interaction mediated by the positively charged arginine residues of the amino-terminal polypeptide that is insensitive to denaturation by urea, and a specific interaction that is sensitive to denaturation by urea.

scholarly journals Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro.

1990 ◽  
Vol 111 (6) ◽  
pp. 3049-3064 ◽  
Author(s):  
P A Coulombe ◽  
Y M Chan ◽  
K Albers ◽  
E Fuchs
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
Amino Terminal ◽  
Filament Assembly ◽  
Keratin Filaments ◽  
Keratin Filament ◽  
Filament Networks ◽  
10 Nm Filaments

To investigate the sequences important for assembly of keratins into 10-nm filaments, we used a combined approach of (a) transfection of mutant keratin cDNAs into epithelial cells in vivo, and (b) in vitro assembly of mutant and wild-type keratins. Keratin K14 mutants missing the nonhelical carboxy- and amino-terminal domains not only integrated without perturbation into endogenous keratin filament networks in vivo, but they also formed 10-nm filaments with K5 in vitro. Surprisingly, keratin mutants missing the highly conserved L L E G E sequence, common to all intermediate filament proteins and found at the carboxy end of the alpha-helical rod domain, also assembled into filaments with only a somewhat reduced efficiency. Even a carboxy K14 mutant missing approximately 10% of the rod assembled into filaments, although in this case filaments aggregated significantly. Despite the ability of these mutants to form filaments in vitro, they often perturbed keratin filament organization in vivo. In contrast, small truncations in the amino-terminal end of the rod domain more severely disrupted the filament assembly process in vitro as well as in vivo, and in particular restricted elongation. For both carboxy and amino rod deletions, the more extensive the deletion, the more severe the phenotype. Surprisingly, while elongation could be almost quantitatively blocked with large mutations, tetramer formation and higher ordered lateral interactions still occurred. Collectively, our in vitro data (a) provide a molecular basis for the dominance of our mutants in vivo, (b) offer new insights as to why different mutants may generate different phenotypes in vivo, and (c) delineate the limit sequences necessary for K14 to both incorporate properly into a preexisting keratin filament network in vivo and assemble efficiently into 10-nm keratin filaments in vitro.

scholarly journals SUMOylation of periplakin is critical for efficient reorganization of keratin filament network

2019 ◽  
Vol 30 (3) ◽  
pp. 357-369 ◽  
Author(s):  
Mansi Gujrati ◽  
Rohit Mittal ◽  
Lakhan Ekal ◽  
Ram Kumar Mishra
Keyword(s):  
Intermediate Filaments ◽  
Okadaic Acid ◽  
Intermediate Filament ◽  
Time Lapse ◽  
Intermediate Filament Proteins ◽  
Enhanced Sensitivity ◽  
Response To Stress ◽  
Keratin Filament ◽  
Time Lapse Imaging ◽  
Linker Domain

The architecture of the cytoskeleton and its remodeling are tightly regulated by dynamic reorganization of keratin-rich intermediate filaments. Plakin family proteins associate with the network of intermediate filaments (IFs) and affect its reorganization during migration, differentiation, and response to stress. The smallest plakin, periplakin (PPL), interacts specifically with intermediate filament proteins K8, K18, and vimentin via its C-terminal linker domain. Here, we show that periplakin is SUMOylated at a conserved lysine in its linker domain (K1646) preferentially by small ubiquitin-like modifier 1 (SUMO1). Our data indicate that PPL SUMOylation is essential for the proper reorganization of the keratin IF network. Stresses perturbing intermediate-filament and cytoskeletal architecture induce hyper-­SUMOylation of periplakin. Okadaic acid induced hyperphosphorylation-dependent collapse of the keratin IF network results in a similar hyper-SUMOylation of PPL. Strikingly, exogenous overexpression of a non-SUMOylatable periplakin mutant (K1646R) induced aberrant bundling and loose network interconnections of the keratin filaments. Time-lapse imaging of cells expressing the K1646R mutant showed the enhanced sensitivity of keratin filament collapse upon okadaic acid treatment. Our data identify an important regulatory role for periplakin SUMOylation in dynamic reorganization and stability of keratin IFs.

scholarly journals Desmoplakin interacts with the coil 1 of different types of intermediate filament proteins and displays high affinity for assembled intermediate filaments

PLoS ONE ◽  
2018 ◽  
Vol 13 (10) ◽  
pp. e0205038 ◽  
Author(s):  
Bertrand Favre ◽  
Nadja Begré ◽  
Jamal-Eddine Bouameur ◽  
Prakash Lingasamy ◽  
Gloria M. Conover ◽  
...  
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Intermediate Filament Proteins ◽  
High Affinity ◽  
Different Types

Reactivity of monoclonal antibodies against intermediate filament proteins during embryonic development

Development ◽  
1981 ◽  
Vol 64 (1) ◽  
pp. 45-60
Author(s):  
Rolf Kemler ◽  
Philippe Brûlet ◽  
Marie-Thérèse Schnebelen ◽  
Jean Gaillard ◽  
François Jacob
Keyword(s):  
Monoclonal Antibodies ◽  
Epithelial Cells ◽  
Embryonic Development ◽  
Tissue Distribution ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Adult Tissue ◽  
Reactivity Pattern ◽  
Germ Layers ◽  
Intermediate Filament Proteins

Monoclonal antibodies (mAbs) against a preparation of intermediate filaments from trophoblastoma cells were studied for their reactivity pattern during embryonic development and on adult tissue cells. Up to day 12 of embryonic development, epithelial cells of the three germ layers reacted with these mAbs. Later during development and in adult tissues, positive reactions could be observed only with epithelial cells derived from mesoderm and endoderm. Because of their tissue distribution, the proteins reacting with these mAbs might belong to the keratin family of intermediate filaments or they might represent a new group of intermediate filaments.

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