Changes in the Pattern of Cytokeratin Polypeptides in Epidermis and Hair Follicles During Skin Development in Human Fetuses

Moll, Roland; Moll, Ingrid; Wiest, W.

doi:10.1111/j.1432-0436.1982.tb01280.x

Cited by 224 publications

(138 citation statements)

References 35 publications

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“…As compared to these CK polypeptides, mAb K8. [14]. In the present study, it was noted that CK polypeptides detected by mAb K8.13 strongly reacted with the epithelial cell in the basal layer.…”

Section: Discussionsupporting

confidence: 58%

“…Prior to the immunohistochemical stainings, we examined the molecular weight of CK polypeptides detected by mAbs K8.13 and K8.12 in the ruminal extract of the bovine fetuses by the Western blotting, because both mAbs reacted with many types of CK polypeptides. MAb K8.13 reacted with [13,14], and mAb K8.12 with Nos. 13 (51.0 kD), 15 (50.0 kD) and 16 (48.0 kD) CK polypeptides [8,20].…”

Section: Discussionmentioning

confidence: 99%

“…Bovine CK family consists of about 20 polypeptides [7,9,15]. Skin-type (56.5/62.0-65.0 kD) [13], esophagus-type (43.0/58.0 kD) [14], hyperproliferated epithelial-type (46.0/57.0 kD) [20] and simple layered epithelial-type CK polypeptides [7] have been characterized as markers for various epithelial differentiations. In this study, we examined the relationship between the distributions of CK polypeptides and the histogenesis of the containing 8 M urea, and then reduced in boiling water for 10 min.…”

Section: Sodium Dodecyl Sulfate-polyacrilamide Gel Electrophoresis (Smentioning

confidence: 99%

“…Sci. 61(3): 261-265, 1999 ruminal epithelium using two mAbs ; i.e., MAb K8.13 raised against the stratified epithelial type CK polypetides [10,13,14], and mAb K8.12 against the non-stratified hyperproliferative epithelial type CK polypeptides [10,20]. These mAbs recognize the broad-range of CK polypeptides in species including man, cow, chick and amphibia, but show only limited reactivity with only a few rodent CK polypeptides [10].…”

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confidence: 99%

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Distribution of Cytokeratin Polypeptides Detected by Monoclonal Antibodies K8.13 and K8.12 in the Fetal Bovine Ruminal Epithelium.

Amasaki

Takanosu

Mawatari

1999

The Journal of Veterinary Medical Science

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ABSTRACT. Temporal and spatial distributions of cytokeratin (CK) polypeptides were detected by monoclonal antibodies (mAbs) K8.13 and K8.12 during the development of the bovine ruminal epithelium. By the Western blotting analysis after the sodium dodecyl sulfatepolyacrilamide gel electrophoresis, mAb K8.13 confirmed 60.8 and 63.0 kD CK polypeptides in the fetal ruminal epithelial extract, and mAb K8.12 also 48.0 and 54.0 kD CK polypeptides. Immunohistochemical reactivities against both mAbs were detected only in the epithelial cells throughout the fetal periods. Distributions of CK polypeptides detected only by mAb K8.13 were observed on the basal side of the epitherial layer, but not by mAb K8.12 in the 7 cm fetus in crown-rump length. MAb K8.13 reacted also intensely with columnar-shaped cells in the basal layer in the fetuses of the later developmental periods. These results suggest that CK polypeptides detected by mAb K8.13 might be involved in the differentation and/or the maintenance of the basal layer in the ruminal epithelial development.-KEY WORDS: bovine, cytokeratin, development, epithelium, rumen.J. Vet. Med. Sci. 61(3): 261-265, 1999 ruminal epithelium using two mAbs ; i.e., MAb K8.13 raised against the stratified epithelial type CK polypetides [10,13,14], and mAb K8.12 against the non-stratified hyperproliferative epithelial type CK polypeptides [10,20]. These mAbs recognize the broad-range of CK polypeptides in species including man, cow, chick and amphibia, but show only limited reactivity with only a few rodent CK polypeptides [10]. MATERIAL AND METHODS Sodium dodecyl sulfate-polyacrilamide gel electrophoresis (SDS-PAGE) and Werstern blotting:Fourteen bovine fetuses from 7 to 90 cm in crown-rump length (CRL) were obtained from a local slaughterhouse, Saitama Prefecture, Japan (Table 1). The ruminal epithelium was homogenized in 50 mM Tris-HCl, pH 7.4, with 1 M KCl, 1 mM ethylenediaminetetraacetic acid disodium salt, 1 mM phenylmethylsulfonyl fluoride, 1 mM dithiothreit and 1% Triton X-100 (all reagents were purchased from Sigma Chemical Co., Ltd., U.S.A.), stirred at 4°C overnight, and then centrifugated at 18,000 g for 30 min at 4°C. The precipitate was resolved in the Laemmli's buffer [12] We have been interested in the mechanism of the morphogenetical regulations under the epithelialmesenchymal interaction, and have studied the morphogenesis of the bovine ruminal papillae and the palatine ridge [1,2,[16][17][18]. The epithelial-mesenchymal interaction is known to conduct several morphogenetic processes such as the digestive tract [21] and the chick feather germ [11]. The finger-and/or leaf-like ruminal papillae have regulary aligned on the ruminal inner surface. We have studied temporal and spatial distributions of extracellular matrix such as fibronectin, laminin, chondroitin sulfate proteoglycans and some collagens as the marker of the mesenchymal differentiation, and those of carbonic anhydrase isozyme III as the marker of the epithelial one in the ruminal papillae (RP) [1,16,17] and pa...

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Section: Discussionsupporting

confidence: 58%

Section: Discussionmentioning

confidence: 99%

Section: Sodium Dodecyl Sulfate-polyacrilamide Gel Electrophoresis (Smentioning

confidence: 99%

mentioning

confidence: 99%

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Distribution of Cytokeratin Polypeptides Detected by Monoclonal Antibodies K8.13 and K8.12 in the Fetal Bovine Ruminal Epithelium.

Amasaki

Takanosu

Mawatari

1999

The Journal of Veterinary Medical Science

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“…The lack of interest in K15 also rests in prior assumptions that it was a minor cytoskeletal component of stratified tissues (Moll et al, 1982a,b;Nelson and Sun, 1983). This misconception seems to have arisen from extrapolation of studies on skin, where K15 is a minor component (Moll et al, 1982b), and from studies on adult internal stratified tissues, where the levels of K14 are higher than in the corresponding neonatal tissues (Moll et al, 1982a;Leube et al, 1988). When taken together with its unusual expression pattern, our studies on K15 suggest that in contrast to K14 mutations which give rise to EBS, K15 mutations might give rise to patients with perhaps mild symptoms of EBS in the skin, but more severe symptoms in internal stratified squamous epithelia.…”

Section: A New Basal Keratin In the Picture: New Insights Into Diseasmentioning

confidence: 99%

The basal keratin network of stratified squamous epithelia: defining K15 function in the absence of K14.

Lloyd

Cheng

et al. 1995

The Journal of Cell Biology

250

254

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Abstract. Keratin 5 and keratin 14 have been touted as the hallmarks of the basal keratin networks of all stratified squamous epithelia. Absence of K14 gives rise to epidermolysis bullosa simplex, a human blistering skin disorder involving cytolysis in the basal layer of epidermis. To address the puzzling question of why this disease is primarily manifested in skin rather than other stratified squamous epithelia, we ablated the K14 gene in mice and examined various tissues expressing this gene. We show that a key factor is the presence of another keratin, K15, which was hitherto unappreciated as a basal cell component. We show that the levels of K15 relative to K14 vary dramatically among stratified squamous epithelial tissues, and with neonatal development. In the absence of K14, K15 makes a bona fide, but ultrastructurally distinct, keratin filament network with K5. In the epidermis of neonatal mutant mice, K15 levels are low and do not compensate for the loss of K14. In contrast, the esophagus is unaffected in the neonatal mutant mice, but does appear to be fragile in the adult. Parallel to this phenomenon is that esophageal K14 is expressed at extremely low levels in the neonate, but rises in postnatal development. Finally, despite previous conclusions that the formation of suprabasal keratin filaments might depend upon K5/K14, we find that a wide variety of suprabasal networks composed of different keratins can form in the absence of K14 in the basal layer.

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Retinoids Strongly and Selectively Correlate With Keratin 13 and Not Keratin 19 Expression in Cutaneous Warts of Renal Transplant Recipients

Blokx¹,

Smit²,

Jong³

et al. 2002

Arch Dermatol

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To compare the expression of keratin (K) 13 and K19 in cutaneous warts of renal transplant recipients (RTRs) and immunocompetent individuals (ICIs). Design: Retrospective, nonrandomized immunohistochemical study. Patients and Methods: Specimens from cutaneous warts of RTRs and ICIs were retrieved from the archives of the Department of Pathology, University Medical Center St Radboud, Nijmegen, the Netherlands. Twentyone warts from RTRs and 21 from ICIs were examined. Nine RTRs (10 specimens) received either systemic acitretin or topical all-trans retinoic acid, and their effect on both keratins was assessed. Main Outcome Measures: Frequency and expression patterns of K13 and K19 in warts of RTRs vs ICIs and the effect of retinoids. Results: A significantly higher percentage of warts of RTRs expressed K13 compared with warts of ICIs (86% vs 14%, 18 vs 3 cases, respectively; PϽ.001). In warts of RTRs, retinoid treatment correlated significantly with a particularly strong, segmental K13 expression pattern, which we termed zebroid. Without use of retinoids, K13 was mostly restricted to suprabasal single cells. Keratin 19 was absent in all warts of both patient groups.

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Changes in the Pattern of Cytokeratin Polypeptides in Epidermis and Hair Follicles During Skin Development in Human Fetuses

Cited by 224 publications

References 35 publications

Distribution of Cytokeratin Polypeptides Detected by Monoclonal Antibodies K8.13 and K8.12 in the Fetal Bovine Ruminal Epithelium.

Distribution of Cytokeratin Polypeptides Detected by Monoclonal Antibodies K8.13 and K8.12 in the Fetal Bovine Ruminal Epithelium.

The basal keratin network of stratified squamous epithelia: defining K15 function in the absence of K14.

Retinoids Strongly and Selectively Correlate With Keratin 13 and Not Keratin 19 Expression in Cutaneous Warts of Renal Transplant Recipients

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