Dermokine: an extensively differentially spliced gene expressed in epithelial cells.

Studies performed to discover genes overexpressed in inflammatory diseases identified dermokine as being upregulated in such disease conditions. Dermokine is a gene that was first observed as expressed in the differentiated layers of skin. Its two major isoforms, alpha and beta, are transcribed from different promoters of the same locus, with the alpha isoform representing the C terminus of the beta isoform. Recently, additional transcript variants have been identified. Extensive in silico analysis and reverse transcriptase (RT)-PCR cloning has confirmed the existence of these variants in human cells and tissues, identified a new human isoform as well as the gamma isoform in mouse. Recombinant expression and analysis of the C-terminal truncated isoform indicate that the molecule is O-linked glycosylated and forms multimers in solution. In situ hybridization and immunohistochemistry has shown that the gene is differentially expressed in various cells and tissues, other than the skin. These results show that the dermokine gene is expressed in epithelial tissues other than the skin and this expression is transcriptionally and posttranscriptionally complex.

[1]  A. Steven,et al.  Glycine loops in proteins: their occurrence in certain intermediate filament chains, loricrins and single-stranded RNA binding proteins. , 1991, International journal of biological macromolecules.

[2]  C. Lanctôt,et al.  Identification of a conserved cluster of skin-specific genes encoding secreted proteins. , 2004, Gene.

[3]  G. Rubin,et al.  A computer program for aligning a cDNA sequence with a genomic DNA sequence. , 1998, Genome research.

[4]  J. Ramshaw,et al.  Amino acid propensities for the collagen triple-helix. , 2000, Biochemistry.

[5]  S. M. Baker,et al.  Characterization of Protease-activated Receptor-2 Immunoreactivity in Normal Human Tissues , 1998, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[6]  B. Brodsky,et al.  The triple‐lielix motif in proteins , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[7]  K. Hadjiolova,et al.  Corneodesmosin, a Component of Epidermal Corneocyte Desmosomes, Displays Homophilic Adhesive Properties* , 2002, The Journal of Biological Chemistry.

[8]  E. Toulza,et al.  The human dermokine gene: description of novel isoforms with different tissue-specific expression and subcellular location. , 2006, The Journal of investigative dermatology.

[9]  Y. Ono,et al.  Identification of novel keratinocyte-secreted peptides dermokine-α/-β and a new stratified epithelium-secreted protein gene complex on human chromosome 19q13.1 , 2004 .

[10]  R. Dwek,et al.  Concepts and principles of O-linked glycosylation. , 1998, Critical reviews in biochemistry and molecular biology.

[11]  F. Lopez,et al.  Homo-oligomerization of human corneodesmosin is mediated by its N-terminal glycine loop domain. , 2004, The Journal of investigative dermatology.

[12]  C. Turano,et al.  Influence of the carbohydrate moiety on the stability of glycoproteins. , 1996, Biochemistry.

[13]  P. Steinert,et al.  The two size alleles of human keratin 1 are due to a deletion in the glycine-rich carboxyl-terminal V2 subdomain. , 1992, The Journal of investigative dermatology.