Characterization of human cytokeratin 2, an Epidermal cytoskeletal protein synthesized late during differentiation
Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and pr...
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E-Artikel |
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Englisch |
| Erschienen: |
1992 |
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Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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in: Experimental Cell Research - Amsterdam : Elsevier, 202(1992), 1, Seite 132-141 |
| Übergeordnetes Werk: |
volume:202 ; year:1992 ; number:1 ; pages:132-141 |
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| 520 | |a Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. | ||
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(DE-627)NLEJ183682092 (DE-599)GBVNLZ183682092 DE-627 ger DE-627 rakwb eng Characterization of human cytokeratin 2, an Epidermal cytoskeletal protein synthesized late during differentiation 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Collin, C. oth Moll, R. oth Kubicka, S. oth Ouhayoun, J.-P. oth Franke, W.W. oth in Experimental Cell Research Amsterdam : Elsevier 202(1992), 1, Seite 132-141 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:202 year:1992 number:1 pages:132-141 http://dx.doi.org/10.1016/0014-4827(92)90412-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 202 1992 1 132-141 |
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(DE-627)NLEJ183682092 (DE-599)GBVNLZ183682092 DE-627 ger DE-627 rakwb eng Characterization of human cytokeratin 2, an Epidermal cytoskeletal protein synthesized late during differentiation 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Collin, C. oth Moll, R. oth Kubicka, S. oth Ouhayoun, J.-P. oth Franke, W.W. oth in Experimental Cell Research Amsterdam : Elsevier 202(1992), 1, Seite 132-141 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:202 year:1992 number:1 pages:132-141 http://dx.doi.org/10.1016/0014-4827(92)90412-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 202 1992 1 132-141 |
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(DE-627)NLEJ183682092 (DE-599)GBVNLZ183682092 DE-627 ger DE-627 rakwb eng Characterization of human cytokeratin 2, an Epidermal cytoskeletal protein synthesized late during differentiation 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Collin, C. oth Moll, R. oth Kubicka, S. oth Ouhayoun, J.-P. oth Franke, W.W. oth in Experimental Cell Research Amsterdam : Elsevier 202(1992), 1, Seite 132-141 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:202 year:1992 number:1 pages:132-141 http://dx.doi.org/10.1016/0014-4827(92)90412-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 202 1992 1 132-141 |
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(DE-627)NLEJ183682092 (DE-599)GBVNLZ183682092 DE-627 ger DE-627 rakwb eng Characterization of human cytokeratin 2, an Epidermal cytoskeletal protein synthesized late during differentiation 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Collin, C. oth Moll, R. oth Kubicka, S. oth Ouhayoun, J.-P. oth Franke, W.W. oth in Experimental Cell Research Amsterdam : Elsevier 202(1992), 1, Seite 132-141 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:202 year:1992 number:1 pages:132-141 http://dx.doi.org/10.1016/0014-4827(92)90412-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 202 1992 1 132-141 |
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(DE-627)NLEJ183682092 (DE-599)GBVNLZ183682092 DE-627 ger DE-627 rakwb eng Characterization of human cytokeratin 2, an Epidermal cytoskeletal protein synthesized late during differentiation 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Collin, C. oth Moll, R. oth Kubicka, S. oth Ouhayoun, J.-P. oth Franke, W.W. oth in Experimental Cell Research Amsterdam : Elsevier 202(1992), 1, Seite 132-141 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:202 year:1992 number:1 pages:132-141 http://dx.doi.org/10.1016/0014-4827(92)90412-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 202 1992 1 132-141 |
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characterization of human cytokeratin 2, an epidermal cytoskeletal protein synthesized late during differentiation |
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Characterization of human cytokeratin 2, an Epidermal cytoskeletal protein synthesized late during differentiation |
| abstract |
Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. |
| abstractGer |
Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. |
| abstract_unstemmed |
Among the more than 30 different human proteins of the cytokeratin (CK) group of intermediate filament (IF) proteins, the significance of the epidermal polypeptide CK 2 (Moll et al., 1982, Cell 31, 11-24) has been repeatedly questioned in the literature. Here, we show, by in vitro translation and protein gel electrophoresis, that human epidermis from various body sites does indeed contain relatively large amounts of mRNA encoding a distinct polypeptide comigrating with native epidermal CK 2. We also report the isolation of a cDNA clone encoding the complete sequence of CK 2, which is a type II CK different from-but related to-epidermal CKs 1 and 5 on the one hand and corneal CK 3 on the other. The mRNA of ~2.6 kb encodes a polypeptide of 645 amino acids and M"r 65,852, in good agreement with the value of 65.5 kDa previously estimated from gel electrophoresis. This human CK, the largest so far known, displays several features typical of CKs of stratified epithelia, including numerous repeats of glycinerich tetrapeptides in the head and tail domains. Northern blot and in situ hybridizations have shown that CK 2 is expressed strictly suprabasally, usually starting in the third or fourth cell layer of epidermis, and this was confirmed at the protein level by immunohistochemistry using CK 2-specific antibodies. The protein has been detected as a regular epidermal component in skin samples from different body sites, albeit as a minor CK in ''soft skin'' (e.g., breast nipple, penile shaft, axilla), but not in foreskin epithelium and in other epithelia, in squamous metaplasias and carcinomas, or in cultured cell lines derived therefrom. We propose that CK 2 is a late cytoskeletal IF addition synthesized during maturation of epidermal keratinocytes which probably contributes to terminal cornification. |
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Characterization of human cytokeratin 2, an Epidermal cytoskeletal protein synthesized late during differentiation |
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Collin, C. Moll, R. Kubicka, S. Ouhayoun, J.-P. Franke, W.W. |
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