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PubMed1995

Association of vimentin intermediate filaments with the centrosome.

SW-13 cells that lack cytoplasmic intermediate filaments (IFs) were stably transfected with a human vimentin cDNA expression vector. Isolated subclones displayed two prevalent patterns of vimentin distribution as observed by indirect immuno-localization: (1) cytoplasmic filaments characteristic of a vimentin IF network; and (2) a distinct, juxtanuclear focus with limited filamentous extensions. Comparative analysis of two subclones that uniquely segregated these patterns of vimentin organization indicated that vimentin accumulated as a perinuclear focus in cells that expressed a 4-fold lower level of the protein. The observed variation in cellular organization was not due to detectable differences in vimentin protein modification, as determined by two-dimensional gel analysis. Increasing the amount of vimentin in a low expressing clone by a secondary transfection with human or mouse vimentin cDNA resulted in well-dispersed, cytoplasmic filaments, suggesting that the distinct juxtanuclear organization of vimentin arose due to lower cellular vimentin levels. Employing anti-gamma-tubulin and anti-vimentin antibodies, dual immunofluorescence together with confocal microscopy revealed that the juxtanuclear focus of vimentin was located in the centrosomal region. Electron microscopy showed a spheroidal, filamentous structure with at least some filaments closely associated with the pericentriolar material (PCM). Because vimentin IF organization is at least partially dependent on microtubules, the effects of nocodazole and taxol on perinuclear vimentin foci were examined. Neither drug affected the juxtanuclear localization of foci, although taxol (10 microM, 5 hours) caused a release of pericentriolar gamma-tubulin from the nuclear region in 50-60% of the cells. These studies indicate that lower, in vivo, levels of vimentin fail to form extended IFs but rather are organized as a perinuclear aggregate. Moreover, the PCM of the centrosome appears to possess attachment sites for vimentin IFs.

Animals↗
PubMed2004

Physiological and pathological expression of intermediate filaments in the equine endometrium.

The aim of this study was to investigate the expression of the intermediate filaments cytokeratin, vimentin and desmin in the equine endometrium by immunohistological techniques. For this purpose, endometrial biopsies of 151 mares were examined to determine physiological cycle patterns and changes resulting from endometriosis. During the physiological cycle epithelial cells and mesenchymal cells express cytokeratin and vimentin, respectively, whilst desmin and vimentin were coexpressed by the smooth muscle cells. Epithelial coexpression of cytokeratin and vimentin was seen in numerous fibrotic glands and in the uterine glands of three mares with pathologically inactive endometria. Three different staining patterns (basal, perinuclear, diffuse) of vimentin were associated with typical morphological alterations of the affected epithelia. In addition, in 14 cases a stromal coexpression of vimentin and desmin was found, indicating an atypical stromal differentiation in inactive endometria of older mares, barren for several years.

Animals↗
PubMed1998

Defining the interactions between intermediate filaments and desmosomes.

Desmoplakin (DP), plakoglobin (PG), and plakophilin 1 (PP1) are desmosomal components lacking a transmembrane domain, thus making them candidate linker proteins for connecting intermediate filaments and desmosomes. Using deletion and site-directed mutagenesis, we show that remarkably, removal of approximately 1% of DP's sequence obliterates its ability to associate with desmosomes. Conversely, when linked to a foreign protein, as few as 86 NH2-terminal DP residues are sufficient to target to desmosomes efficiently. In in vitro overlay assays, the DP head specifically associates with itself and with desmocollin 1a (Dsc1a). In similar overlay assays, PP1 binds to DP and Dsc1a, and to a lesser extent, desmoglein 1 (Dsg1), while PG binds to Dsg1 and more weakly to Dsc1a and DP. Interestingly, like DP, PG and PP1 associate with epidermal keratins, although PG is considerably weaker in its ability to do so. As judged by overlay assays, the amino terminal head domain of type II keratins appears to have a special importance in establishing these connections. Taken together, our findings provide new insights into the complexities of the links between desmosomes and intermediate filaments (IFs). Our results suggest a model whereby at desmosome sites within dividing epidermal cells, DP and PG anchor to desmosomal cadherins and to each other, forming an ordered array of nontransmembrane proteins that then bind to keratin IFs. As epidermal cells differentiate, PP1 is added as a molecular reinforcement to the plaque, enhancing anchorage to IFs and accounting at least partially for the increase in numbers and stability of desmosomes in suprabasal cells.

Amino Acid Sequence↗
PubMed1985

Intermediate-filament proteins in parathyroid glands and parathyroid adenomas.

The intermediate-filament proteins of normal, hyperplastic, and adenomatous parathyroid glands were analyzed immunohistochemically and by immunoblotting with monospecific antibodies. In both normal and adenomatous parathyroid glands, we found keratins with molecular weights of 52, 45, and 40 kilodaltons (Nos. 8, 18, and 19, respectively). Vimentin proteins could be identified only in stromal cells, while glial fibrillary acidic protein was not found. In normal parathyroid glands, neurofilament positivity was seen only in nerve axons. In five of 15 parathyroid gland adenomas some keratin-positive cells expressed neurofilamentlike immunoreactivity also. In cytoskeletal extracts of one adenoma, the 200-kilodalton neurofilament protein was identified by immunoblotting. Thus it appears that some parathyroid gland adenoma cells may acquire neurofilament proteins and coexpress cytokeratin and neurofilament polypeptide in a way comparable with that reported in certain neuroendocrine tumors.

Adenoma↗
PubMed2002

Intermediate filaments and the function of the dystrophin-protein complex.

Intermediate filament (IF) proteins and the dystrophin-associated protein complex (DPC) play important roles in cardiac and skeletal muscle. Both systems are mutated in several different forms of inherited muscular dystrophy and cardiomyopathy. Recently two articles have been published that propose a physical link between the DPC and the IF network in muscle. Two novel IF proteins, syncoilin and desmuslin, have been identified as binding partners for the dystrophin-associated protein, alpha-dystrobrevin, in muscle. These novel interactions suggest that alpha-dystrobrevin may tether the IF protein network to the DPC. Mice lacking alpha-dystrobrevin develop muscular dystrophy without perturbing the assembly of the DPC at the muscle membrane, suggesting the involvement of other non-DPC proteins in the disease. The interaction between the DPC and the IF network may be disrupted in patients with Duchenne muscular dystrophy and in mice lacking alpha-dystrobrevin.

Cytoskeletal Proteins↗
PubMed1988

Multiple elements are required for expression of an intermediate filament gene.

The expression of vimentin is unique within the intermediate filament multigene family. It is the only member which deviates from its usual tissue-specific expression pattern and whose 5'-flanking region contains multiple GC boxes, the binding site for Sp1. The activity of vimentin 5'-end:CAT fusions has been compared in cells where vimentin is highly expressed (mouse L cells) or not expressed at all (MH1C1). In addition, CAT activity has been examined by microinjection into Xenopus oocytes. Both in vivo expression and in vitro binding studies implicate Sp1 as a general regulatory factor in vimentin gene expression. Increased expression of 5'-end:CAT fusions in mouse L cells suggests that a fibroblast-specific enhancer element resides in the region -321 to -160. Low transcriptional activity in MH1C1 cells may be due to either the lack of this positive transcription factor(s) or the presence of a repressor element. Here, we demonstrate that the unique and complex pattern of vimentin gene expression is controlled by multiple cis-acting elements.

Animals↗
PubMed1994

Expression of the neuroectodermal intermediate filament nestin in human melanomas.

Nestin is a newly identified intermediate filament expressed in proliferating neuronal progenitor cells, but not in the adult brain. Nestin expression reappears in many tumors of the central nervous system and has in human glioblastomas been associated with a high degree of malignancy. Because melanocytes are of neuroectodermal origin, we studied nestin expression in benign and malignant cells of the melanocytic lineage using Northern blot and immunohistochemical analyses. Nestin mRNA was detected in 24 of 34 metastatic melanomas and in 1 of 4 benign nevi, whereas the protein was expressed in 10 of 15 primary melanomas, in 29 of 34 metastatic tumors, and in 3 of 4 nevi. Neither normal melanocytes nor any of 4 basal cell carcinomas showed detectable levels of the protein. The high fraction of melanocytic tumors which express nestin, particularly the metastatic melanomas, suggests that nestin may be a useful marker for such malignancies. Furthermore, although no significant correlation between nestin expression and tumor malignancy was observed, the protein was most abundantly expressed in the infiltrating part of the tumors, indicating a possible involvement of nestin in tumor invasion.

Biomarkers, Tumor↗
PubMed1988

Participation of cytoskeletal intermediate filaments in the infectious cycle of human respiratory syncytial virus (RSV).

RSV infection of Hep-2 or HeLa cells leads to biochemical and morphological changes of cytoskeletal intermediate filaments (IF). Thus, human cytokeratin 18 is modified to generate a more acidic polypeptide of slightly larger apparent molecular weight. In addition, the amounts of vimentin and other cytokeratins are reduced, probably as a consequence of proteolytic degradation. These changes are reflected in a decrease of immunofluorescence with specific antibodies in RSV-induced syncytia and a more disorganized arrangement of IF arrays. About 50% of virus nucleoprotein (NP) is extracted with the high salt and detergent-insoluble intermediate filament fraction. Pulse-chase experiments indicate that NP needs a maturation period after synthesis to associate with IF. It is suggested that RSV needs to interact with IF during its life cycle and that association of NP, and/or other viral components, with IF might then lead to cytoskeletal structures becoming unstable in RSV-infected cells.

Carcinoma, Hepatocellular↗
PubMed1989

Glial fibrillary acidic protein and desmin in salivary neoplasms. Expression of four different types of intermediate filament proteins within the same cell type.

The presence of intermediate filament proteins (IFP) in normal salivary gland tissue and investigated by immunohistochemical techniques on frozen sections. Cytokeratins (CKs) were seen in almost all normal epithelial cells. In the parotid gland and in palatal gland tissue, a co-expression of cytokeratin and glial fibrillary acidic protein (GFAP) was seen in some myoepithelial cells, but this was not apparent in the submandibular gland. In some pleomorphic adenomas, carcinomas in pleomorphic adenomas, one mucoepidermoid carcinoma, one mucus-producing adenopapillary carcinoma and one adenoid cystic carcinoma, cells expressing three different IFP classes were found (CKs, vimentin, GFAP). These cells were most often situated peripherally in the tumour cords or ducts. The cytokeratin pattern in these cells, as revealed by mAbs PKK1-3, was similar to that in normal myoepithelial cells. Furthermore, reactivity for a fourth class of IFP, desmin, could be seen in this cell type in two carcinomas in pleomorphic adenomas, and also in a few cells in a pleomorphic adenoma and an adenoid cystic carcinoma. Thus the pattern of IFP expression in salivary gland neoplasms, is very complex, and cannot always be related to the normal tissue.

Antibodies, Monoclonal↗
PubMed1991

Malnutrition induces an increase in intermediate filament protein content of rat cerebral cortex.

Wistar rats were fed a normal protein (25% casein) or an isoenergetic low protein (8% casein) diet from the day of giving birth until pups were weaned. Some litters were killed at weaning; others (both normal and malnourished animals) received the 25% protein diet until d 90 when they were killed. Intermediate filament (IF) preparations were obtained by extraction of the cerebral cortex with a high salt PBS solution containing 1% Triton X-100. The pellet contained the bulk of the cytoskeleton proteins from tissue, identified as the 150- and 68-kDa subunits of neurofilaments (NF-M and NF-L, respectively), the 66-kDa associated protein, the 57-kDa intermediate filament-like protein, and the 50-kDa glial fibrillary acidic protein. Intermediate filament-enriched fractions from control and malnourished rats at both d 21 and 90 were scanned following two-dimensional gel electrophoresis to determine the effects of postnatal malnutrition on the intermediate filament protein content. The results indicated that postnatal malnutrition imposed during the brain growth spurt period did not alter the expression of IF proteins of the cerebral cortex in 21-d-old rats, but increased the expression of NF-L and NF-M proteins in adult rats.

Animals↗
PubMed1988

Expression of intermediate filaments and desmoplakin in vertebrate olfactory mucosa.

The expression of intermediate filaments (IF) and desmoplakin was investigated in frog, bovine, and human (fetal) olfactory mucosa. IF are tissue-specific molecular cytoskeletal markers; desmoplakin is the major desmosomal protein. Positive immunoreactivity was observed in the epithelium and in the subepithelial Bowman's glands to keratin and to desmoplakin, indicating the epithelial nature of this tissue. Desmin, neurofilaments, and glial fibrillary acidic protein (GFAP) were not detected in the mucosa. The absence of neurofilaments and GFAP in the tissue containing sensory neurons and glia-like supporting cells is a unique feature and may be related to the fact that the chemosensory neurons are situated in a bonafide epithelium and are known to undergo continuous turnover. In view of the controversy regarding the expression of vimentin in the olfactory neurons, three independently derived antibodies to vimentin were used; weak or no labeling was found in the epithelium, whereas mesenchymal cells in the lamina propia were labeled with all three antibodies. Olfactory nerve fascicles in the lamina propia were heterogenously labeled: VIM 13.2 gave very weak labeling; aVimAS showed mild labeling and SBV-21 showed intensive labeling in the nerve fascicle. This heterogenous labeling pattern may suggest that olfactory vimentin is distinct in reacting only with some of the antivimentin antibodies.

Animals↗
PubMed2002

A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization.

We present evidence that vimentin intermediate filament (IF) motility in vivo is associated with cytoplasmic dynein. Immunofluorescence reveals that subunits of dynein and dynactin are associated with all structural forms of vimentin in baby hamster kidney-21 cells. This relationship is also supported by the presence of numerous components of dynein and dynactin in IF-enriched cytoskeletal preparations. Overexpression of dynamitin biases IF motility toward the cell surface, leading to a perinuclear clearance of IFs and their redistribution to the cell surface. IF-enriched cytoskeletal preparations from dynamitin-overexpressing cells contain decreased amounts of dynein, actin-related protein-1, and p150Glued relative to controls. In contrast, the amount of dynamitin is unaltered in these preparations, indicating that it is involved in linking vimentin cargo to dynactin. The results demonstrate that dynein and dynactin are required for the normal organization of vimentin IF networks in vivo. These results together with those of previous studies also suggest that a balance among the microtubule (MT) minus and plus end-directed motors, cytoplasmic dynein, and kinesin are required for the assembly and maintenance of type III IF networks in interphase cells. Furthermore, these motors are to a large extent responsible for the long recognized relationships between vimentin IFs and MTs.

Animals↗
PubMed1987

Efficient interaction of nonpolar lipids with intermediate filaments of the vimentin type.

Based on the finding that vimentin isolated and purified from cultured mammalian cells is heavily contaminated by neutral lipids, the binding of a series of radioactively labeled nonpolar lipids to pure, delipidated vimentin was investigated. Employing gel permeation chromatography of the complexes on Sephacryl S-300, cholesterol, cholesteryl fatty acid esters and mono-, di- and triglycerides were found to efficiently associate with vimentin. These compounds also showed a strong tendency to bind to vimentin filaments. While the non-alpha-helical head piece of vimentin did not interact with neutral lipids under the above assay conditions, the alpha-helical rod domain was highly active. When cholesterol or 1,2-dioleoyl-glycerol was incorporated into phospholipid vesicles, the affinity of the liposomes for vimentin filaments was considerably increased. However, in sucrose density gradient equilibrium centrifugation the filament-vesicle adducts were only stable when the liposomes contained negatively charged phospholipids. These results suggest that the association of intermediate filaments with lipid vesicles is initiated by interaction of the arginine-rich N-termini of their subunit proteins with the negatively charged vesicle surface and stabilized by partial insertion of the protein molecules into the lipid bilayer, particularly at those sites where immiscible, nonpolar lipids create defects in phospholipid packing. Very likely, nonpolar lipids play a significant role in the interaction of intermediate filaments with natural membrane systems.

Animals↗
PubMed1986

Phenotypic analysis of cultured melanoma cells. Expression of cytokeratin-type intermediate filaments by the M5 human melanoma cell line.

Expression of intermediate filament (IF) isotypes was studied in six human and two murine melanoma cell lines. With one exception, these lines expressed IFs only of the vimentin type; neurofilament peptides, desmin and GFAP were not detected. However, the M5 human melanoma line also expressed extensive cytokeratin tonofilament arrays, as visualized by immunofluorescence with a panel of eleven monoclonal antibodies and hetero-antisera to cytokeratins; only the keratin 19-specific antibody BA16 did not react. By 2 D gel electrophoresis, five major keratin peptides were detected (keratins 7, 8, 13, 17 and 18), and an additional 57 kD peptide was detected on immunoblots with several antikeratin antibodies. Also observed in M5 cells was focal collapse of tonofilament arrays in mitotic cells. All the melanoma lines tested were positive for S100; M5 and two other cell lines were also positive for the 220-240 kD neuroectoderm-associated cell-surface differentiation antigen defined by monoclonal antibody UJ 127:11. In all the melanoma cell lines, secretion of extracellular matrix proteins (fibronectin, laminin and collagen type IV) was sparse or absent, and all were negative for the epithelial cell markers HMG-1 and HMG-2. Co-expression of keratin and vimentin by a melanoma cell line is discussed in the light of recent controversy concerning expression of cytokeratins by other neoplasms of putative neuroectodermal origins.

Antibodies, Monoclonal↗
PubMed1991

Organization of coiled-coil molecules in native mouse keratin 1/keratin 10 intermediate filaments: evidence for alternating rows of antiparallel in-register and antiparallel staggered molecules.

There is considerable diversity of opinion in the literature concerning the organization of two-chain coiled-coil molecules in intermediate filaments. I have reexplored this issue using the limited proteolysis paradigm with native mouse epidermal keratin intermediate filaments (KIF), consisting of keratins 1 and 10. KIF were harvested as cytoskeletal pellets, dissociated into subfilamentous forms at pH 9.8, 9.0, or 2.6, and were subjected to limited proteolytic digestion to recover alpha-helix-enriched particles that derived from the rod domains of the constituent chains, using conditions that do not promote reorganization of the constituent protein chains or coiled-coil molecules. The multichain particles were subjected to physicochemical analyses, amino acid sequencing, and electron microscopy in order to determine their composition, structure, and organization within the intact KIF. The results predict two principal modes of alignment: neighboring molecules may be aligned in register and antiparallel or staggered and antiparallel. From known structural constraints, this permits construction of a two-dimensional surface lattice for KIF which consists of alternating antiparallel rows of in-register and staggered molecules. These data establish the level of hierarchy at which the well-known antiparallelity and staggered features of KIF are introduced. This model supports the proposals of KIF structure based on theoretical considerations of ionic interactions scores (Crewther et al., 1983). When the KIF are dissociated at extremes of pH, this structural model allows for disruption along alternate axes; the in-register antiparallel alignment is seen only when KIF are dissociated at high pH values; below pH 9, only the staggered antiparallel alignment is seen. The process of molecule realignment especially in concentrated urea solutions indicates that the staggered antiparallel alignment is the more thermodynamically stable form in solution.

Amino Acid Sequence↗
PubMed2004

Functions of intermediate filaments in neuronal development and disease.

Five major types of intermediate filament (IF) proteins are expressed in mature neurons: the three neurofilament proteins (NF-L, NF-M, and NF-H), alpha-internexin, and peripherin. While the differential expression of IF genes during embryonic development suggests potential functions of these proteins in axogenesis, none of the IF gene knockout experiments in mice caused gross developmental defects of the nervous system. Yet, deficiencies in neuronal IF proteins are not completely innocuous. Substantial developmental loss of motor axons was detected in mice lacking NF-L and in double knockout NF-M;NF-H mice, supporting the view of a role for IFs in axon stabilization. Moreover, the absence of peripherin resulted in approximately 30% loss of small sensory axons. Mice lacking NF-L had a scarcity of IF structures and exhibited a severe axonal hypotrophy, causing up to 50% reduction in conduction velocity, a feature that would be very detrimental for large animal species. Unexpectedly, the NF-M rather than NF-H protein turned out to be required for proper radial growth of large myelinated axons. Studies with transgenic mice suggest that some types of IF accumulations, reminiscent of those found in amyotrophic lateral sclerosis (ALS), can have deleterious effects and even cause neurodegeneration. Additional evidence for the involvement of IFs in pathogenesis came from the recent discovery of neurofilament gene mutations linked to ALS and Charcot-Marie-Tooth disease (CMT2E). Conversely, we discuss how certain types of perikaryal neurofilament aggregates might confer protection in motor neuron disease.

Animals↗
PubMed1994

Structural features of keratin intermediate filaments.

The first step in the assembly of a keratin intermediate filament (KIF) is the formation of a type I/type II heterodimer molecule in which two chains become aligned in parallel and close axial registration to form a flexible segmented alpha-helical coiled-coil rope 46 nm long. The segments of coiled-coil are interspersed by sequences that introduce irregularities of unknown structure. Here we have modeled two of these, the link L2 and the heptad discontinuity located near the middle of segment 2B. In a model for L2, the orientation of the coiled-coil structure is turned through about 180 degrees over the eight residue stretch constituting this link segment. In contrast, the heptad discontinuity in segment 2B would seem to result in only minimal distortion of the coiled-coil rope, contrary to previous expectations. Little is known about how the neighboring molecules are aligned and packed within the assembled KIF. Crosslinking experiments with KIF have determined that two neighboring molecules are aligned anti-parallel and axially in three ways, and predict that similarly-directed molecules could be overlapped by about 1 nm. The two-dimensional surface lattice resulting from these data predicts an axial periodicity of 22.6 nm, which in fact is visible by electron microscopy of shadowed KIF. Interestingly, most of the amino acid substitutions resulting from mutations in the keratin genes found in genodermatoses are clustered in this molecular overlap region. Although we do not yet know how the rows of antiparallel molecules fold in three dimensions to form an intact KIF, certain of the observed crosslinks could also occur between nearest neighbor parallel molecules across a four-molecule strand; that is, KIF may be built from bundles or protofibrils. These insights on molecular structure and molecular packing provide new constraints on models for KIF structure.

Amino Acid Sequence↗
PubMed2002

Interaction in vitro of type III intermediate filament proteins with triplex DNA.

As previously shown, type III intermediate filaments (IFs) select from a mixture of linear mouse genomic DNA fragments mobile and repetitive, recombinogenic sequences that have also been identified in SDS-stable crosslinkage products of vimentin and DNA isolated from intact fibroblasts. Because these sequences also included homopurine.homopyrimidine (Pu.Py) tracts known to adopt triple-helical conformation under superhelical tension, and because IF proteins are single-stranded (ss) and supercoiled DNA-binding proteins, it was of interest whether they have a particular affinity for triplex DNA. To substantiate this, IF-selected DNA fragments harboring a (Pu.Py) segment and synthetic d(GA)(n) microsatellites were inserted into a vector plasmid and the constructs analyzed for their capacity to interact with IF proteins. Band shift assays revealed a substantially higher affinity of the IF proteins for the insert-containing plasmids than for the empty vector, with an activity decreasing in the order of vimentin > glial fibrillary acidic protein > desmin. In addition, footprint analyses performed with S1 nuclease, KMnO(4), and OsO(4)/bipyridine showed that the (Pu.Py) inserts had adopted triplex conformation under the superhelical strain of the plasmids, and that the IF proteins protected the triple-helical insert sequences from nucleolytic cleavage and chemical modification. All these activities were largely reduced in extent when analyzed on linearized plasmid DNAs. Because intramolecular triplexes (H-DNA) expose single-stranded loops, and the prokaryotic ssDNA-binding proteins g5p and g32p also protected at least the Pu-strand of the (Pu.Py) inserts from nucleolytic degradation, it seemed likely that the IF proteins take advantage of their ssDNA-binding activity in interacting with H-DNA. However, in contrast to g5p and E. coli SSB, they produced no clear band shifts with single-stranded d(GA)(20) and d(TC)(20), so that the interactions rather appear to occur via the duplex-triplex and triplex-loop junctions of H-DNA. On the other hand, the IF proteins, and also g32p, promoted the formation of intermolecular triplexes from the duplex d[A(GA)(20).(TC)(20)T] and d(GA)(20) and d(TC)(20) single strands, with preference of the Py (Pu.Py) triplex motif, substantiating an affinity of the proteins for the triplex structure as such. This triplex-stabilizing effect of IF proteins also applies to the H-DNA of (Pu.Py) insert-containing plasmids, as demonstrated by the preservation of intramolecular triplex-vimentin complexes upon linearization of their constituent supercoiled DNAs, in contrast to poor complex formation from free, linearized plasmid DNA and vimentin. Considering that (Pu.Py) sequences are found near MAR/replication origins, in upstream enhancer and promoter regions of genes, and in recombination hot spots, these results might point to roles of IF proteins in DNA replication, transcription, recombination, and repair.

Animals↗