Effect of therapy on keratin polypeptide profiles of psoriatic epidermis

LeVine, Mark J.

doi:10.1001/archderm.116.9.1028

Cited by 9 publications

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“…Baden et al (1975 suggested that psoriatic scales give rise to four main polypeptide bands, while horny cells from nonlesional skin of psoriatic patients or that from normal volunteers yield two polypeptide bands. Recently, Levine, McGilvray & Baden (1980) also showed that the four main polypeptide bands from psoriatic scales reverted to the normal two bands after PUVA treatment.…”

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A simplified method for studying fibrous proteins in psoriatic scales obtained by tape stripping

Kitajima¹,

Tsuneda²,

Mori³

et al. 1982

Br J Dermatol

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Polyacrylamide gel electrophoretic investigations were carried out on solubilized proteins from psoriatic and normal stratum corneum obtained by adhesive tape stripping. The proteins in the scales adhering to the tape were solubilized by incubating the tape in 1% sodium dodecyl sulphate (SDS) solution. The electrophoretic behaviour of these solubilized proteins on SDS-polyacrylamide gel was compared with the a-fibrous proteins (keratin) of callus. The proteins isolated from callus of normal human heel showed six main bands which were similar to those of the keratin isolated by the 8 M urea-mercaptoethanol method. The lesional skin of forty-five psoriatic patients consistently showed nine main bands on polyacrylamide gels, but only two main bands were observed in the non-lesional, non-heel skin. Six of these nine bands had mobilities and relative intensities almost identical with those of a-keratin extracted by the mercaptoethanol method, but the other three bands had greater mobilities on the gels. These results suggest that this technique may have considerable potential for studying changes in a-keratin in patients with psoriasis and other disorders of keratinization.The stratum corneum, the final product of keratinization, consists mainly of keratin filaments and an amorphous histidine-rich matrix embedding the filaments

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confidence: 96%

A simplified method for studying fibrous proteins in psoriatic scales obtained by tape stripping

Kitajima¹,

Tsuneda²,

Mori³

et al. 1982

Br J Dermatol

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“…Four major keratins (50, 56.5, 58, and 65-67 kd) have been identified in normal human epidermis (7, 21, 40, 72; cf. 4, 49, 62); significant alterations in epidermal keratin composition can occur, however, as a result of disease (1,3,5,25,26,28,33,34,36,37,40,50,52,54,66,71) as well as changes in cellular growth environment (10,20,29,55,61,62).Numerous attempts have been made to characterize such 'Abbreviations used in this paper: BCC, basal cell carcinoma; IEF, isoelectric focusing ; kd, kilodaltons .keratin variations in epidermal diseases. Recent studies have demonstrated that some, but not all, psoriatic epidermal specimens possess a reduced level of 65-67-kd keratins (1,5,8,37,50,54,66).…”

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confidence: 99%

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confidence: 99%

Monoclonal antibody analysis of keratin expression in epidermal diseases: a 48- and 56-kdalton keratin as molecular markers for hyperproliferative keratinocytes.

Weiß¹,

Eichner²,

Sun³

1984

The Journal of Cell Biology

529

308

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The polypeptide composition of epidermal keratin varies in disease . To better understand the biological meaning of these variations, we have analyzed keratins from a number of human epidermal diseases by the immunoblot technique using AE1 and AE3 monoclonal antikeratin antibodies . The results reveal a continuous spectrum of keratin expression ranging from one closely resembling the normal in vivo pattern to one almost identical to cultured epidermal keratinocytes . Specifically, a 50-kilodalton (kd) (AEl-positive) and a 58-kd (AE3-positive) keratin are present in all diseases, supporting the concept that they represent "permanent" markers for keratinocytes . A 56.5-kd (AE1) and a 65-67-kd (AE3) keratin, previously shown to be markers for keratinization, are expressed only by lesions retaining a keratinized morphology . A 48-kd (AE1) and a 56-kd (AE3) keratin are present in all hyperproliferative (para-or nonkeratinized) disorders, but not in normal abdominal epidermis or in ichthyosis vulgaris which is a non hyperproliferative disease . These two keratins have previously been found in various nonepidermal keratinocytes undergoing hyperproliferation, suggesting that these keratins are not epidermis-specific and may represent markers for hyperproliferative keratinocytes in general . In various epidermal diseases, there is a reciprocal expression of the (keratin) markers for hyperproliferation and keratinization, supporting the mutual exclusiveness of the two cellular events . Moreover, our results indicate that, as far as keratin expression is concerned, cultured human epidermal cells resemble and thus may be regarded as a model for epidermal hyperplasia. Finally, the apparent lack of any major, diseasespecific keratin changes in the epidermal disorders studied so far implies that keratin abnormalities probably represent the consequence, rather than the cause, of these diseases.The keratins are a group of water-insoluble proteins (40-70 Kdaltons [kd])' that form 10-nm desmosome-associated tonofilaments in all epithelia (15,17,18,61,63,64). Four major keratins (50, 56.5, 58, and 65-67 kd) have been identified in normal human epidermis (7, 21, 40, 72; cf. 4, 49, 62); significant alterations in epidermal keratin composition can occur, however, as a result of disease (1,3,5,25,26,28,33,34,36,37,40,50,52,54,66,71) as well as changes in cellular growth environment (10,20,29,55,61,62 -67-kd keratins (1, 5, 8, 37, 50, 54, 66). In addition, Thaler et al. (65,66) reported that two water-insoluble proteins of -54 and 57 kd are unique to psoriatic scale, although Baden et al. (5) found no "psoriasis-specific" keratin changes . Hunter and Skerrow (26) reported that certain abnormal keratin polypeptides ranging from 55-63 kd (probably corresponding to 50-58 kd in our gel system) are present in the scales of psoriasis, atopic dermatitis, and seborrheic dermatitis, as well as in the stratum comeum oftape-stripped epidermis . Interestingly, Kubilus et al. (28) found that keratins of another disease, basal cell 13...

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“…However, the mechanism of action of retinoids remains unknown. The fibrous proteins of the stratum corneum are a terminal product in keratinization of epidermal cells and are biochemically altered in psoriatic lesional skin (4)(5)(6)(7)(8). It is well known that retinoids affect keratinocyte differentiation, especially by suppressing keratinization (9,10).…”

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confidence: 99%

Effects of Oral Retinoid on the Sds‐page Profile of Stratum Corneum Keratin in Patients With Psoriasis

Kitajima

Tsuneda

Furuta

et al. 1983

The Journal of Dermatology

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a-Keratins from horny cells of lesional and non-Iesional skin in psoriatic patients were examined by sodium dodecylsulfate polyacrylamide gel electrophoresis before and after oral retinoid (etretinate at a dose of 50 mg/day) treatment. Horny cell specimens were obtained from lesional, nonlesional, and normal human skin of the back or thigh by scraping with scalpel and/or tape stripping before retinoid treatment. Horny cell specimens of healed-lesional skin and retinoidaffected skin were obtained by tape stripping because the horny cell layer was too thin to use a scalpel. a-Keratins from lesional horny cells showed 3 major polypeptide bands with molecular weights (mw) of 53,000, 55,000, and 59,000 and some minor bands with mw of 62,000, 66,000, and less than 53,000. Non-lesions showed two polypeptides (mw, 59,000 and 66,000) before treatment. After treatment, a-keratins from horny cells of both non-lesions and resolved lesions showed three polypeptides bands (mw, 59,000, 62,000, and 66,000).

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Effect of therapy on keratin polypeptide profiles of psoriatic epidermis

Cited by 9 publications

References 0 publications

A simplified method for studying fibrous proteins in psoriatic scales obtained by tape stripping

A simplified method for studying fibrous proteins in psoriatic scales obtained by tape stripping

Monoclonal antibody analysis of keratin expression in epidermal diseases: a 48- and 56-kdalton keratin as molecular markers for hyperproliferative keratinocytes.

Effects of Oral Retinoid on the Sds‐page Profile of Stratum Corneum Keratin in Patients With Psoriasis

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