The isolation and preliminary characterisation of human prekeratin

Skerrow, David

doi:10.1016/0005-2795(77)90179-9

Cited by 30 publications

(14 citation statements)

References 9 publications

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“…Lane 5, cultured newborn foreskin keratinocytes . Std, molecular weight standards that are, from top to bottom, bovine serum albumin (68 kd), catalase (60 kd), fumarase (49 kd), ovalbumin (45 kd), aldolase (40 kd), and trypsinogen (24 kd) . a denotes residual actin .…”

Section: A 48-and a 56-kd Keratin As Molecular Markers For Hyperprolimentioning

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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Section: A 48-and a 56-kd Keratin As Molecular Markers For Hyperprolimentioning

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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“…Keratins were extracted by homogenisation and sonication of lesional epidermis in 0.1 M citric acid/sodium citrate buffer, pH 2.65 at 4 °C, followed by centrifugation at 50,000 g for 30 min [ 10]. The ker atins in the supernatant were partially purified by serial isoelectric precipitation at pH 4.0.…”

Section: Extraction O F Keratinsmentioning

confidence: 99%

Epidermal Keratin Levels during Oral 1-Alpha-Hydroxyvitamin D<sub>3</sub> Treatment for Psoriasis

Holland

Wood²,

Roberts³

et al. 1989

Skin Pharmacol Physiol

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Recently the treatment of psoriasis with vitamin D3, its metabolites or analogues, has been reported to be clinically effective and free from side effects. We have quantified the changes in the levels of epidermal lesional keratins in 15 psoriatic patients receiving oral 1Α(OH)D₃ treatment. Lesions were sampled before treatment commenced and at monthly intervals for 4–6 months. Clinical resolution occurred in 7 patients within this time; 3 other patients showed incomplete lesion resolution and the remaining 5 patients showed a complete lack of response within the treatment period. Lesion resolution, as judged by clinical criteria, was accompanied by significant changes in the levels of three of the keratin polypeptides and smaller changes in others. Keratin 2 increased to levels greater than those in normal epidermis, while keratins 16 and 18 decreased to normal levels. Changes in the levels of keratins 1 and 5 were small and those of keratins 7, 10 and 14 minimal. These changes were compared with values found during lesion resolution with other therapies used in psoriasis, i.e. topical dithranol, PUVA, oral etretinate and hydroxyurea and were highly reminiscent of those observed during PUVA therapy but contrasted with those during etretinate treatment. The decrease in level of keratin 16, a hyperproliferation marker, suggests that 1Α(OH)D₃ inhibits keratinocyte proliferation, but at the same time the overproduction of keratin 2, a major keratin of the granular cells, indicates that there is an increase in the number of cells in the later stages of differentiation.

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“…Amino acid sequence analysis indicates that there is a central helical core with random regions present at the ends of the peptide chains (STEINERT et al 1985). Human prekeratin also consists of a number of polypeptides which are in the same molecular weight range as those reported for bovine epidermis (BADEN and LEE 1978;BAYNES et al 1978;SKERROW 1977;COOPER et al 1985). In the change from viable malpighian layer cells to dead stratum corneum cells several alterations in the fibrous proteins occur.…”

Section: B Fibrous Proteinsmentioning

confidence: 84%

Keratin

Baden¹

1989

Handbook of Experimental Pharmacology

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The isolation and preliminary characterisation of human prekeratin

Cited by 30 publications

References 9 publications

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

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

Epidermal Keratin Levels during Oral 1-Alpha-Hydroxyvitamin D<sub>3</sub> Treatment for Psoriasis

Keratin

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