1982
DOI: 10.1111/j.1432-0436.1982.tb01220.x
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An Unusual Type of Cytokeratin Filament in Cells of a Human Cloacogenic Carcinoma Derived from the Anorectal Transition Zone

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Cited by 38 publications
(26 citation statements)
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“…These systems are advantageous in that they are readily available, easy to maintain, and amenable to manipulation. Cell lines are often altered in their protein and receptor expression patterns because of their immortal nature and continued laboratory maintenance (54, 60,76,111,127,135,137,140,144,145,165,166,188,215,219,220,222,223,224,237,255). Additionally, altered protein expression can result in additive or synergistic alternative functional responses within these immortal cells compared to their respective parental tissues.…”
Section: Models Used To Study Gonococcal Pathogenesismentioning
confidence: 99%
“…These systems are advantageous in that they are readily available, easy to maintain, and amenable to manipulation. Cell lines are often altered in their protein and receptor expression patterns because of their immortal nature and continued laboratory maintenance (54, 60,76,111,127,135,137,140,144,145,165,166,188,215,219,220,222,223,224,237,255). Additionally, altered protein expression can result in additive or synergistic alternative functional responses within these immortal cells compared to their respective parental tissues.…”
Section: Models Used To Study Gonococcal Pathogenesismentioning
confidence: 99%
“…At 40 kDa, this type I keratin is the smallest known IF protein (6,7). The primary structure of human, bovine, and mouse K19 is highly conserved and made unique by virtue of an exceptionally short (13-residue long) tail domain at the carboxyl terminus (8 -11).…”
Section: Keratins (K)mentioning
confidence: 99%
“…The following antibodies were used: (i) Guinea pig antibodies (ammonium sulfate-precipitated globulin fraction) to human epidermal prekeratin, prepared from body skin as described for bovine material [19,24], have been used previously [9]; (ii) guinea pig antibodies (ammonium sulfate-precipitated globulin fraction) to cytokeratin polypeptide D from mouse liver hepatocytes (for details of preparation see Refs. [lo, 14, 171); (iii) guinea pig antibodies (IgG) raised against bovine muzzle prekeratin from desmosome-tonofilament fractions which show broad cross-reaction between epidermal prekeratin polypeptides and cytokeratins from various tissues [14,17,19, 24,251; (iv) [31]. Alternatively, for exclusion of possible cross-reactions with keratin-like proteins, vimentin antibodies (sera, IgG fractions purified by chromatography on DEAE cellulose, and affinity-purified IgG) were absorbed exhaustively by incuba-…”
Section: Antibodiesmentioning
confidence: 99%
“…In all cases the staining with cytokeratin antibodies was significantly diminished when the immunoglobulins used were absorbed first on purified keratin prepared as 'acetone-powder' or in the form of reconstituted filaments (for details see Methods and Ref. [31]).…”
Section: (6) Cells Of Connective Tissue and Vascular Walls Subsumed Umentioning
confidence: 99%
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