Pair formation and promiscuity of cytokeratins: formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides

@article{Hatzfeld1985PairFA,
  title={Pair formation and promiscuity of cytokeratins: formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides},
  author={M. Hatzfeld and W. Franke},
  journal={The Journal of Cell Biology},
  year={1985},
  volume={101},
  pages={1826 - 1841}
}
Cytokeratins are expressed in different types of epithelial cells in certain combinations of polypeptides of the acidic (type I) and basic (type II) subfamilies, showing "expression pairs." We have examined in vitro the ability of purified and denatured cytokeratin polypeptides of human, bovine, and rat origin to form the characteristic heterotypic subunit complexes, as determined by various electrophoretic techniques and chemical cross-linking, and, subsequently, intermediate-sized filaments… Expand
Cytokeratin domains involved in heterotypic complex formation determined by in-vitro binding assays.
TLDR
The results obtained indicate that the binding between cytokeratin polypeptides of the complementary type is stronger and more selective than interactions of cytokeratins with other IF and non-IF proteins; both the head and the tail portions of the proteins are not required for heterotypic complex formation; and the formation of the heterotypespeptide complex is not critically dependent upon ionic interactions. Expand
Intermediate filaments formed de novo from tail-less cytokeratins in the cytoplasm and in the nucleus
TLDR
To examine the requirement of the aminoterminal and the carboxyterminal domain of cytokeratins for de novo IF formation in the living cell, cDNAs coding for intact as well as head- and/or tail-less human CKs 8 and 18 and the naturally tail- less human CK 19 are constructed, all under the control of the human beta-actin promoter. Expand
Cytokeratin expression in simple epithelia. II. cDNA cloning and sequence characteristics of bovine cytokeratin A (no. 8).
TLDR
The high sequence homology of bovine cytokeratin A with published sequences of human tissue polypeptide antigen (TPA), a soluble serum component used as tumor marker in clinical oncology, supports the view that TPA is a proteolytically solubilized fragment containing the rod portion of human cytokersatin no. 8. Expand
Tissue-Specific Co-expression and in vitro Heteropolymer Formation of the Two Small Branchiostoma Intermediate Filament Proteins A3 and B2
The two small intermediate filament (IF) proteins A3 and B2 of the cephalochordate Amphioxus were investigated. Blot overlays indicated a heterotypic interaction pattern of the recombinant proteins.Expand
Tissue-specific co-expression and in vitro heteropolymer formation of the two small branchiostoma intermediate filament proteins A3 and B2.
The two small intermediate filament (IF) proteins A3 and B2 of the cephalochordate Amphioxus were investigated. Blot overlays indicated a heterotypic interaction pattern of the recombinant proteins.Expand
Synthesis and fate of keratins 8 and 18 in nonepithelial cells transfected with cDNA.
TLDR
It is demonstrated that assembly in heterocomplexes stabilizes keratins against cellular degradation, helping to explain why excess pools of simple keratin have never been detected. Expand
Identification of protein IT of the intestinal cytoskeleton as a novel type I cytokeratin with unusual properties and expression patterns
TLDR
It is concluded that polypeptide IT is an integral IF component which is related, though somewhat distantly, to type I CKs, and, therefore, it is proposed to add it to the human CK catalogue as CK 20. Expand
Monoclonal cytokeratin antibody recognizing a heterotypic complex: immunological probing of conformational states of cytoskeletal proteins in filaments and in solution.
TLDR
A novel type of monoclonal murine antibody directed against an epitope depending on human cytokeratin (CK) 18, a member of the acidic (type I) CK subfamily, is described and the existence of heterotypic CK 8 and 18 complexes in a distinct soluble form among supernatant proteins from cell homogenates is demonstrated. Expand
Elucidating the early stages of keratin filament assembly
TLDR
It is shown that remarkably, these keratins behave as 1:1 complexes even in 9 M urea and in the presence of a reducing agent, suggesting that there may not be a serial sequence of events leading to the assembly of keratin intermediate filaments, but rather a number of associations may take place in parallel. Expand
Characterization of dimer subunits of intermediate filament proteins.
TLDR
The results show that IF proteins from discrete complexes of two polypeptide chains in parallel orientation and probably in coiled-coil configuration, which apparently have a high tendency to further associate into double dimers. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 104 REFERENCES
Patterns of Expression and Organization of Cytokeratin Intermediate Filaments
TLDR
The building block of cytokeratin IFs is a heterotypic tetramer, consisting of two type I and two type II polypeptides arranged in pairs of laterally aligned coiled coils, thought to be generally applicable to IFs. Expand
Protein complexes of intermediate-sized filaments: melting of cytokeratin complexes in urea reveals different polypeptide separation characteristics.
TLDR
The data suggest that certain cytokeratin polypeptides are complementary and contain sequences that direct their association into specific complexes forming IF subunits, and that cytokeratins do not form complexes with vimentin, another type of IF protein. Expand
Identification of two types of keratin polypeptides within the acidic cytokeratin subfamily I.
TLDR
This work compares two polypeptides of the acidic cytokeratin subfamily, VIb and VII, which are co-expressed in large amounts in bovine epidermal keratinocytes and shows that in the same species keratins of the same subfamily can differ considerably. Expand
Diversity of cytokeratins. Differentiation specific expression of cytokeratin polypeptides in epithelial cells and tissues.
TLDR
Individual cytokeratins provide tissue- or cell type-specific markers that are useful in the definition and identification of the relatedness or the origin of epithelial and carcinoma cells. Expand
A subfamily of relatively large and basic cytokeratin polypeptides as defined by peptide mapping is represented by one or several polypeptides in epithelial cells.
TLDR
Diverse stratified epithelia and tumours derived therefrom contain two or more polypeptides of this subfamily, and the patterns of expression in different cell types suggest that some polypeptic are specific for certain routes of epithelial differentiation. Expand
Formation of cytoskeletal elements during mouse embryogenesis. Intermediate filaments of the cytokeratin type and desmosomes in preimplantation embryos.
TLDR
It is concluded from the absence of desmin and vimentin that intermediate filaments of both these types are not essential for the development of the preimplantation embryo and that the trophectoderm resembles a differentiated cytokeratin-rich epithelium, and the desmosome-tonofilament complex is involved in epithelial differentiation during early murine embryogenesis. Expand
Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cells.
TLDR
Cytoskeletal residues obtained after extraction of rat liver and cultured rat hepatoma cells were used to isolate cytokeratin subunit complexes by solubilization in low salt buffer containing 4 M-urea, similar to the tetrameric complex of rat and human vimentin formed under the same conditions. Expand
Human epithelial cell intermediate filaments: isolation, purification, and characterization
TLDR
Ulastructural studies of HeLa cells revealed two distinct IF organizational stages including bundles and loose arrays and results obtained indicate that the major HeLa IF protein is the same major IF structural protein found in fibroblasts. Expand
The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors and cultured cells
TLDR
During cell transformation and tumor devel- opment this cell type specificity of intermediate filaments is largely conserved’ and classification of tumors by their specific type of intermediate Filaments has re- cently become very valuable in clinical histodiagnosis. Expand
Intermediate filament proteins in nonfilamentous structures: Transient disintegration and inclusion of subunit proteins in granular aggregates
TLDR
It is found that vimentin and cytokeratins can be organized in structures other than intermediate filaments, and at least during mitosis of some cell types, factors occur that promote unraveling of intermediate Filaments into protofilament-like threads and organization of intermediate filament proteins into distinct granules that form large aggregate bodies. Expand
...
1
2
3
4
5
...