Short CommunicationGene Characterization of Sciellin (SCEL) and Protein Localization in Vertebrate Epithelia Displaying Barrier Properties☆
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Structural and Immunocytochemical Characterization of Keratinization in Vertebrate Epidermis and Epidermal Derivatives
2006, International Review of CytologyCitation Excerpt :Sciellin is a 75‐ to 82‐kDa protein consisting of 668 amino acids, pI 8.0–9.4, and rich in glutamine and lysine. This protein is relatively different from the other proteins of the CCE (Champliaud et al., 2000; Kvedar et al., 1992). Keratins (especially K1/K10) and filaggrin interact with the other proteins of the CCE.
The Expression of Vitamin D-Upregulated Protein 1 in Skin and its Interaction with Sciellin in Cultured Keratinocytes
2003, Journal of Investigative DermatologyCitation Excerpt :In one experiment confocal microscopy was used. Using a cDNA library previously prepared from human keratinocyte RNA by RT-PCR (Champliaud et al, 2000) and primers based on the published VDUP1 sequence (Chen and DeLuca, 1994), the sequence of the cDNA was determined. Thirty-eight positive clones derived from the yeast two-hybrid screening were sequenced.
Sciellin promotes the development and progression of thyroid cancer through the JAK2/STAT3 signaling pathway
2024, Molecular Carcinogenesis
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Sequence data from this article have been deposited with the EMBL/GenBank Data Libraries under Accession No. (BankIt 323690) AF245700.
- 1
The first two authors contributed equally to this work.
- 2
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