Expression of epidermal keratins and filaggrin during human fetal skin development.

Dale, Beverly A.; Holbrook, Karen A.; Kimball, Janet R.; Hoff, Mary S.; Sun, Tung‐Tien

doi:10.1083/jcb.101.4.1257

Cited by 276 publications

(193 citation statements)

References 56 publications

(78 reference statements)

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“…To elucidate the inheritance characteristics of the K10 polymorphism, we used the same PCR technique to amplify the V2 subdomain of the 17 members from one Centre d'Etude du Polymorphisme Humain family (28). A total of four differently sized alleles (labeled [1][2][3][4] of alleles present in the parents (Fig. 6).…”

Section: Resultsmentioning

confidence: 99%

Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops.

Korge

Gan

McBride

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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Existing data suggest that the human keratin 10 intermediate filament protein is polymorphic in amino acid sequence and in size. To precisely define the nature of the polymorphism, we have used PCR amplification and sequence analyses on DNA from several individuals including five with documented size variations of the keratin 10 protein. We found no variation in the N-terminal or rod domain sequences. However, we observed many variations in the V2 subdomain near the C terminus in glycine-rich sequences with a variation of as much as 114 base pairs (38 amino acids), but all individuals had either one or two variants. Our results show that (i) the keratin 10 system is far more polymorphic than previously realized, (is) the polymorphism is restricted to insertions and deletions of the glycine-rich quasipeptide repeats that form the glycine-loop motif in the C-terminal domain, (iii) the polymorphism can be accounted for by simple allelic variations that segregate by normal Mendelian mechanisms, and (iv) the differently sized PCR products most likely represent different alleles of a single-copy gene per haploid genome.Keratins form a large family of cytoplasmic intermediate filaments (IFs). The more than 30 known keratin chains are differentially expressed along the different pathways of epithelial cell development and differentiation. They are subdivided into acidic type I and neural-basic type II chains. Most epithelial cells express a particular pair of type I and type II chains that assemble into keratin IFs characteristic of that cell type (1-6). For example, terminally differentiating epidermal keratinocytes express keratins 1 (type II) and 10 (K1O; type I).Keratins, like all other IF proteins, have a central a-helical rod domain of conserved secondary structure. The rod domain is flanked on both sides by end domains that display particular patterns that permit their classification into subdomains. These subdomains are the high homology or H subdomains, regions with sequence variation or V subdomains, and highly charged ends or E subdomains (1, 2, 7). For K10, the rod domain is flanked on the N-terminal end by El, Vi, and H1 subdomains and on the C-terminal side by V2 and E2 subdomains (Fig. 1).-Although the principles of the structural organization of the rod domain and its possible function during IF assembly are largely known (9-11), little is known about the structure and function of the end domains of the IFs. In comparison to most other keratins, the E and V subdomains of epidermal keratins 1 and 10 are unusually glycine-rich (8,(12)(13)(14) and, therefore, likely to adopt a distinct configuration and conceivably possess a unique function (15). Notably, solid-state NMR experiments have

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Section: Resultsmentioning

confidence: 99%

Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops.

Korge

Gan

McBride

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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“…Besides CK, filament aggregating protein (filaggrin), a histidine-rich phosphorylated basic protein of major constituents of keratohyaline granules, is a marker of terminal differentiation of epidermis (5). No immunohistochemical study of CK and filaggrin in DC has been reported.…”

Section: Introductionmentioning

confidence: 99%

Cutaneous dermoid cyst: Cytokeratin and filaggrin expression suggesting differentiation towards follicular infundibulum and mature sebaceous gland

Kurokawa

Nishimura²,

Hakamada³

et al. 2006

Oncol Rep

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Abstract. We experienced two cases of cutaneous dermoid cysts (DC). To elucidate the histogenesis of DC, we have studied cytokeratin (CK) expression in DC using ten different anti-keratin antibodies against CK1,7,8,10,14, 15, 16, 17, 18 and 19, antibody. In the cyst wall of DC, CK1 and 10 were expressed in suprabasal layer, and CK14 was limited to the basal layer. In sebaceous gland-like structures, CK14 was detected in sebaceous acinus, and CK17 was detected in sebaceous duct. The other CKs were not detected. Filaggrin was intensely detected in the granular layer in the cyst wall of DC. CK expression profile of DC was similar to follicular infundibulum and sebaceous gland. These results suggested that DC differentiates towards follicular infundibulum and mature sebaceous gland. IntroductionCutaneous dermoid cysts result from the sequestration of cutaneous tissue along lines of embryonic fusion (1). DC in the periorbital area, midline of the neck, nasal root, forehead, mastoid area and the scalp have been reported (2). DCs of the auricle are very rare (3). The histogenesis of DC still remains unclear.CK is an essential marker to evaluate the origin of epithelial tumors (4). Besides CK, filament aggregating protein (filaggrin), a histidine-rich phosphorylated basic protein of major constituents of keratohyaline granules, is a marker of terminal differentiation of epidermis (5). No immunohistochemical study of CK and filaggrin in DC has been reported.To elucidate the histogenesis of DC, we studied CK and filaggrin expression in DC using ten different anti-keratin antibodies against CK1,7,8,10,14, 15, 16, 17, 18 and 19, and anti-filaggrin antibody. Materials and methodsThe patient, a 48-year-old male had DC located on the left postauriclar area from at birth. The other patient, a 31-yearold female developed DC on the right postauriclar area ten years ago. The lesions were surgically excised. Each specimen was formalin-fixed, paraffin-embedded, stained with hematoxylin and eosin, and serially-cut sections were used for the immunohistochemical study. The anti-keratin antibodies used were as follows: 34ßB4 (CK1) (6), LHP1 (CK10) (7), LL002 (CK14) (7), LHK15 (CK15) (8), LL025 (CK16) (7), E3 (CK17) (7), 5D3 (CK18) (7) and b170 (CK19) (9) (all from Novocastra Laboratories Ltd., Newcastle-upon-Tyne, UK).The immunohistochemical study was carried out with the labeled streptoavidin-biotin method (LSAB, Dako, Carpenteria, CA, USA) was performed as previous study (10). Normal skin from the auricle served as controls. ResultsHematoxylin and eosin staining. Histopathological findings of the cases were similar. The cyst wall of DC was located in the deep dermis. Cyst wall was partly ruptured, resulting in the fibrosis with vellus hairs. The cyst wall was formed with keratinizing epithelium in granular layers. The keratinizing epithelium partly projected into the lumen-like crenulation. Thick laminated corneocytes were observed. In the vicinity of the cyst wall, sebaceous gland-like structure was observed (Fig. 1).Immunohistochem...

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“…Cells of the single-layered precursor of the human epidermis produce the same types of CK that are characteristic of simple epithelia, namely CK8, CK18 and CK19 (Dale, Holbrook et al 1985). With the onset of stratification, different cytokeratins are expressed in the basal and suprabasal layers, e.g.…”

Section: Introductionmentioning

confidence: 99%

Cytokeratins of the Liver and Intestine Epithelial Cells During Development and Disease

Chougule¹,

Sumitran–Holgersson²

2012

Cytokeratins - Tools in Oncology

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Expression of epidermal keratins and filaggrin during human fetal skin development.

Cited by 276 publications

References 56 publications

Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops.

Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops.

Cutaneous dermoid cyst: Cytokeratin and filaggrin expression suggesting differentiation towards follicular infundibulum and mature sebaceous gland

Cytokeratins of the Liver and Intestine Epithelial Cells During Development and Disease

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