Disease relevance of SCEL

• MATERIALS AND METHODS: The coding region and intron-exon junctions of SCEL were sequenced in 13 esophageal squamous cell cancers and matching normal esophageal samples to detect mutations [1].
• Analysis of Sciellin (SCEL) as a candidate gene in esophageal squamous cell carcinoma [1].
• BACKGROUND: The aim of this study was to investigate whether a candidate gene, Sciellin (SCEL), mapping to the chromosome 13q21-q31 is mutated in esophageal cancer [1].

High impact information on SCEL

• We have cloned the cDNA encoding sciellin by screening a human keratinocyte expression library with a sciellin-specific monoclonal antibody [2].
• Radiation hybrid mapping demonstrated that sciellin is linked to the sequence tagged site marker WI-457 with a logarithm of the odds score of 7.77 [2].
• Immunofluorescent staining with a polyclonal rabbit antibody made to a recombinant sciellin protein showed peripheral cytoplasmic localization in the upper cell layers of epidermis and in stratified squamous epithelia such as the oral cavity, esophagus, and vagina [2].
• In this study we used the yeast two-hybrid system to find proteins interacting with sciellin and identified vitamin D-upregulated protein 1 (VDUP1) [3].
• Nuclear staining in all layers of human epidermis and bovine stratified epithelium was observed with an antibody to TLS, whereas peripheral staining of the upper layers of these tissues was observed with the antibody to sciellin [4].

Biological context of SCEL

• CONCLUSION: Single nucleotide polymorphisms were detected in both matching tumor and normal esophageal tissues but no disease-associated mutations suggesting that SCEL is not a major factor in esophageal squamous cell carcinogenesis [1].
• cDNA cloning and characterization of sciellin, a LIM domain protein of the keratinocyte cornified envelope [2].
• During embryonic development, the accumulation of sciellin transcript and the accumulation of sciellin protein in the epidermis correlated with the activation of markers of terminal differentiation in epidermis [5].
• This paper describes a protein with amino acid sequence homology to TLS that was isolated from bovine tongue epithelium using an affinity column made with an antibody to the cornified envelope precursor sciellin [4].
• Stem reptiles evolved a multilayered stratum corneum based on a programmed cell death, intensified the production of matrix proteins (e.g., HRPs), corneous cell envelope proteins (e.g., loricrine-like, sciellin-like, and transglutaminase), and complex lipids to limit water loss [6].

Anatomical context of SCEL

• The expression of vitamin D-upregulated protein 1 in skin and its interaction with sciellin in cultured keratinocytes [3].

Associations of SCEL with chemical compounds

• Monoclonal antibodies to the precursor proteins involucrin, pancornulin and sciellin were reacted with frozen section of skin and their localization detected by fluorescein tagged antibodies or the peroxidase technique [7].

Other interactions of SCEL

• Immunoblotting however shows loricrin-, sciellin-, and trasnsglutaminase-positive bands in the corneous layers containing beta-keratin [8].

Analytical, diagnostic and therapeutic context of SCEL

• In situ hybridization of human foreskin tissue sections demonstrated that sciellin is expressed in the stratum granulosum [2].
• Sciellin cDNA probes hybridize to bands of 3.4 and 4.4 kilobase pairs on Northern blots of cultured human keratinocyte RNA [2].
• Using immunoelectron microscopy, the staining by the sciellin antibody was at the cell periphery, but this technique did not work with the antibody to pancornulin [9].
• Western blots of extracts of human and bovine keratinocytes using TLS and sciellin antibodies showed that the two proteins shared at least one epitope, but that they were different [4].

References