INTERMEDIATE FILAMENTS: Structure, Dynamics, Function and Disease

Fuchs, Elaine; Weber, Klaus

doi:10.1146/annurev.bi.63.070194.002021

Cited by 1,338 publications

(991 citation statements)

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“…Vimentin is composed of a central ␣-helical rod domain flanked by the non-␣-helical sequences of the N-terminal head and C-terminal tail domains (for a review, see Fuchs & Weber 1994). The head domain has been observed to be essential for intermediate filament formation (Andreoli & Trevor 1994;Beuttenmüller et al 1994).…”

Section: Discussionmentioning

confidence: 99%

“…Taken together with the fact that the vimentin cleavage is efficiently suppressed by Z-VAD-fmk in Jurkat cells, we concluded that the vimentin cleavage occurs at Asp85 and Asp259 in vivo. It is interesting to note that apoptotic cleavage of lamin B, another intermediate filament protein, has been detected at the 231st residue within a nonhelical linker segment between the second and third helices, which topologically corresponds to Asp259 in vimentin (Fuchs & Weber 1994).…”

Section: Determination Of the Cleavage Sites Within The Vimentin Polymentioning

confidence: 99%

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Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl‐2 action

Morishima

1999

Genes to Cells

102

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Background: Upon Fas stimulation, procaspase-8 is recruited to the death-inducing signalling complex where autoactivation of caspase-8 occurs. Active caspase-8 can directly activate downstream caspases (e.g. caspase-3, 6, and 7) for the execution of apoptosis (mitochondria-independent pathway), while caspase-8 can also lead to executioner caspase activation through mitochondrial damage (mitochondria-dependent pathway). Caspase activation results in the dismantling of intracellular structure through specific proteolysis.

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Section: Discussionmentioning

confidence: 99%

Section: Determination Of the Cleavage Sites Within The Vimentin Polymentioning

confidence: 99%

Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl‐2 action

Morishima

1999

Genes to Cells

102

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“…Their main role is to provide cellular structure and integrity. They are classified into two types: acidic type I (CK9-CK20) and basic type II (CK1-CK8) [99]. Epithelial cells are targets of caspase-mediated proteolysis during apoptosis [100].…”

Section: Cytokeratin 19mentioning

confidence: 99%

Relevance of circulating tumor cells, extracellular nucleic acids, and exosomes in breast cancer

Friel

Corcoran

Crown

et al. 2010

Breast Cancer Res Treat

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Early detection of cancer is vital to improved overall survival rates. At present, evidence is accumulating for the clinical value of detecting occult tumor cells in peripheral blood, plasma, and serum specimens from cancer patients. Both molecular and cellular approaches, which differ in sensitivity and specificity, have been used for such means. Circulating tumor cells and extracellular nucleic acids have been detected within blood, plasma, and sera of cancer patients. As the presence of malignant tumors are clinically determined and/or confirmed upon biopsy procurement-which in itself may have detrimental effects in terms of stimulating cancer progression/metastases-minimally invasive methods would be highly advantageous to the diagnosis and prognosis of breast cancer and the subsequent tailoring of targeted treatments for individuals, if reliable panels of biomarkers suitable for such an approach exist. Herein, we review the current advances made in the detection of such circulating tumor cells and nucleic acids, with particular emphasis on extracellular nucleic acids, specifically extracellular mRNAs and discuss their clinical relevance.

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“…16 At least 65 different IFs have been identified in humans. 17 IFs are known to play a structural role in eukaryotic cells by participating in formation of the cell cytoskeleton and providing mechanical stability to the cells.…”

Section: Intermediate Filaments Of the Musclementioning

confidence: 99%

Intermediate Filament Diseases: Desminopathy

Goldfarb

Olivé

Vicart³

et al. 2008

Advances in Experimental Medicine and Biology

104

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Desminopathy is one of the most common intermediate filament human disorders associated with mutations in closely interacting proteins, desmin and alphaB-crystallin. The inheritance pattern in familial desminopathy is characterized as autosomal dominant or autosomal recessive, but many cases have no family history. At least some and likely most sporadic desminopathy cases are associated with de novo DES mutations. The age of disease onset and rate of progression may vary depending on the type of inheritance and location of the causative mutation. Typically, the illness presents with lower and later upper limb muscle weakness slowly spreading to involve truncal, neckflexor, facial and bulbar muscles. Skeletal myopathy is often combined with cardiomyopathy manifested by conduction blocks, arrhythmias and chronic heart failure resulting in premature sudden death. Respiratory muscle weakness is a major complication in some patients. Sections of the affected skeletal and cardiac muscles show abnormal fibre areas containing chimeric aggregates consisting of desmin and other cytoskeletal proteins. Various DES gene mutations: point mutations, an insertion, small in-frame deletions and a larger exon-skipping deletion, have been identified in desminopathy patients. The majority of these mutations are located in conserved alpha-helical segments, but additional mutations have recently been identified in the tail domain. Filament and network assembly studies indicate that most but not all disease-causing mutations make desmin assembly-incompetent and able to disrupt a pre-existing filamentous network in dominant-negative fashion. AlphaBcrystallin serves as a chaperone for desmin preventing its aggregation under various forms of stress; mutant CRYAB causes cardiac and skeletal myopathies identical to those resulting from DES mutations.

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INTERMEDIATE FILAMENTS: Structure, Dynamics, Function and Disease

Cited by 1,338 publications

References 0 publications

Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl‐2 action

Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl‐2 action

Relevance of circulating tumor cells, extracellular nucleic acids, and exosomes in breast cancer

Intermediate Filament Diseases: Desminopathy

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