Different polypeptides form the intermediate filaments in bovine hoof and esophageal epithelium and in aortic endothelium.

Milstone, Leonard M.; McGuire, Joseph

doi:10.1083/jcb.88.2.312

Cited by 63 publications

(28 citation statements)

References 25 publications

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“…Peptide mapping has established homologies between vimentin and desmin (21). Likewise, immunological and biochemical studies revealed extensive crossreactivity within a given class of polypeptides, keratins (22,23 Similar to the findings, reported here, with the monoclonal IgM antibody produced by patient GON, the availability of hybridoma-derived monoclonal antibodies will undoubtedly uncover new crossreactivities within the family of structurally and functionally related IF proteins. Recently, a mouse hybridoma antibody has been shown to react with an antigenic determinant shared by the five classes ofIF (25).…”

supporting

confidence: 59%

Human monoclonal IgM with autoantibody activity against intermediate filaments.

Dellagi¹,

Brouet²,

Perreau³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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Monoclonal IgMs from two patients with Waldenstrom macroglobulinemia were found to react with intermediate filaments. This was shown by (a) immunostaining of various tissues and cultured cells and (b) immunological characterization of the reactive antigen after blotting of polypeptides separated from total cell extracts by gel electrophoresis or purified intermediate filaments on nitrocellulose sheets. One monoclonal IgM had an activity directed only against vimentin, whereas the other reacted with four different classes of intermediate filaments-vimentin, desmin, glial fibrillary protein, and keratins.

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supporting

confidence: 59%

Human monoclonal IgM with autoantibody activity against intermediate filaments.

Dellagi¹,

Brouet²,

Perreau³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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“…Differences in the polypeptide complexity of the keratins produced by various epithelial cells have been demonstrated both for the intact tissue (10,11,15,23,24,43) and for cells grown in culture (9,16,40,41,46). However, it was not determined previously whether this variation in keratins with cell type represents tissue-specific differences in the synthesis of keratin mRNAs or, alternatively, posttranslational processing or modification of a defined set of keratin polypeptides.…”

Section: Discussionmentioning

confidence: 96%

“…The large keratins are abundant only in differentiating epidermal cells and are probably associated with stratum corneum formation (7,13,15,35). The smaller keratins are present in conjunctival cells (16,41), the intestinal epithelium (10), mesothelial cells (46), and many simple and glandular epithelia (24), but they are not prominent in epidermal cells, esophageal cells, or epithelial cells of the oral cavity (10,15,23).…”

mentioning

confidence: 99%

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Tissue specificity of epithelial keratins: differential expression of mRNAs from two multigene families.

Kim¹,

Rheinwald²,

Fuchs³

1983

Mol. Cell. Biol.

120

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Human epithelial cells cultured from stratified and simple squamous tissues all produce keratins of 40,000 to 58,000 daltons, but within this range the number and sizes vary with different epithelial cells. We have shown that this tissue-specific variation in the keratins is not due to posttranslational modification or processing, but rather to the differential expression of a family of heterogeneous but closely related mRNAs. All of these epithelial keratin mRNAs can be further grouped into two distinct subfamilies by their ability to hybridize with either of two cloned epidermal keratin cDNAs. All of the keratin mRNAs hybridize to one or the other, but not both, of the two cloned cDNAs. However, the mRNAs within each group hybridize with varying degrees of stringency, indicating that they are of similar but not identical sequence. Both types of keratin mRNAs are always expressed in every epithelial cell line studied, suggesting that filament assembly is dependent on the presence of both types of keratins. Within each of these two groups, the slight sequence differences in each class may reflect subtle tissue-specific variations in the structural and functional requirements of the epithelial cytoskeleton.

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“…Biochemical data indicate that the polypeptide composition of keratin filaments varies depending on epithelial cell type (12,14,15,18,21,26,39), cellular growth environment (3,12,20,22,23,32,53,60), histological differentiation stage (6, 9, 2 l, 49, 5 l, 56, 66, 67, 70), and embryonic development period (4, 11). It is therefore not surprising that many keratin species have been described in the literature.…”

mentioning

confidence: 99%

The 50- and 58-kdalton keratin classes as molecular markers for stratified squamous epithelia: cell culture studies.

Nelson¹,

Sun²

1983

The Journal of Cell Biology

338

169

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The keratins are a highly heterogeneous group of proteins that form intermediate filaments in a wide variety of epithelial cells. These proteins can be divided into at least seven major classes according to their molecular weight and their immunological reactivity with monoclonal antibodies. Tissue-distribution studies have revealed a correlation between the expression of specific keratin classes and different morphological features of in vivo epithelial differentiation (simple vs. stratified; keratinized vs. nonkeratinized). Specifically, a 50,000-and a 58,000-dalton keratin class were found in all stratified epithelia but not in simple epithelia, and a 56,500-and a 65-67,000-dalton keratin class were found only in keratinized epidermis. To determine whether these keratin classes can serve as markers for identifying epithelial cells in culture, we analyzed cytoskeletal proteins from various cultured human cells by the immunoblot technique using AE1 and AE3 monoclonal antikeratin antibodies. The 56,500-and 65-67,000-dalton keratins were not expressed in any cultured epithelial cells examined so far, reflecting the fact that none of them underwent morphological keratinization. The 50,000-and 58,000-dalton keratin classes were detected in all cultured cells that originated from stratified squamous epithelia, but not in cells that originated from simple epithelia. Furthermore, human epidermal cells growing as a monolayer in low calcium medium continued to express the 50,000-and 58,000-dalton keratin classes. These findings suggest that the 50,000-and 58,000-dalton keratin classes may be regarded as "permanent" markers for stratified squamous epithelial cells (keratinocytes), and that the expression of these keratin markers does not depend on the process of cellular stratification. The selective expression of the 50,000-and 58,000-dalton keratin classes, which are synthesized in large quantities on a per cell basis, may explain the high keratin content of cultured keratinocytes.The keratins are a family of water-insoluble proteins that form tonofilaments (a class of intermediate-sized filament), which are present in almost all vertebrate epithelia (13,16,17,59,61,62). Since keratins are usually not detectable in nonepithelial tissues including fibroblasts, muscles, and nerves, immunohistochemical staining of keratins facilitates the detection and identification of epithelial cells, both in tissue section and in culture (1, 2, 7, 8, 24, 35, 37, 46-48, 54, 55, 69).Biochemical data indicate that the polypeptide composition of keratin filaments varies depending on epithelial cell type (12,14,15,18,21,26,39), cellular growth environment (3,12,20,22,23,32,53,60), histological differentiation stage (6, 9, 2 l, 49, 5 l, 56, 66, 67, 70), and embryonic development period (4, 11). It is therefore not surprising that many keratin species have been described in the literature. To study the biological significance of keratin heterogeneity, we have previously prepared three monoclonal antikeratin antibodies (designated A...

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Different polypeptides form the intermediate filaments in bovine hoof and esophageal epithelium and in aortic endothelium.

Cited by 63 publications

References 25 publications

Human monoclonal IgM with autoantibody activity against intermediate filaments.

Human monoclonal IgM with autoantibody activity against intermediate filaments.

Tissue specificity of epithelial keratins: differential expression of mRNAs from two multigene families.

The 50- and 58-kdalton keratin classes as molecular markers for stratified squamous epithelia: cell culture studies.

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