High impact information on LOC408038

• The nucleotide and deduced amino acid sequences of the cDNA clone were not identical to any sequence entries in the data bases but revealed significant similarities to avian beta-keratin genes; the highest degree of amino acid sequence identity was 63% [1].
• Specific activation in jun-transformed avian fibroblasts of a gene (bkj) related to the avian beta-keratin gene family [1].
• These patterns of RNA expression correlated well with the appearance of beta-keratin polypeptides, suggesting that beta-keratin synthesis may be controlled at the level of keratin mRNA transcription [2].
• Expression of beta keratin genes during skin development in normal and sc/sc chick embryos [2].
• Here we show that the embryonic layers covering the anterior metatarsal region of the chicken hindlimb (scutate scale forming region) produce several members of the beta keratin family of polypeptides, designated beta (beta) 1-7 [3].

Biological context of LOC408038

• Epidermal-dermal interactions influence morphogenesis and expression of the beta keratin gene family during development of scales in the embryonic chick [4].
• In vivo phosphorylation studies suggested that an additional three beta keratin polypeptides were present as phosphoproteins [4].
• However, the present study of beta keratin gene expression during avian epidermal differentiation contributes new information with which to investigate the role of tissue interactions in this process [4].
• Polyclonal antiserum made against two of the beta keratin polypeptides was used for immunohistochemical and immunogold electron-microscopic analysis of beta keratin tissue distribution [4].

Anatomical context of LOC408038

• Serial cultivation of chicken keratinocytes, a composite cell type that accumulates lipids and synthesizes a novel beta-keratin [5].
• Furthermore, we find that the embryonic layers of the skin overlying the anterior metatarsal region of birds homozygous for the mutation "scaleless" (sc/sc), which completely lack scutate scales, produce the same members of the beta keratin family, beta 1-7, as the embryonic layers and beta strata of normal scutate scales [3].
• The mixed bundles of alpha and beta keratin filaments were closely associated with desmosomes in the lower stratum intermedium and with electron-dense aggregates in the cytoplasm of cells in the outer stratum intermedium [6].
• In late embryonic stages (25-26 to hatching), beta-keratin occurs only in the upper suprabasal cells, in prekeratinized and keratinized layers, whereas alpha-keratin bundles (tonofilaments) remain only in the lowest layers [7].
• While the antibody labels a mature form of beta-keratin incorporated in large filaments, the autoradiographic analysis shows that beta-keratin is produced within the first 30 min in ribosomes, and is later packed into large filaments [8].

Associations of LOC408038 with chemical compounds

• The present observations suggest that both beta-keratin and denser matrix proteins, possibly incorporating histidine, are packed into growing setae [9].
• Proline incorporation occurs mainly in the growing centers, and is more specifically associated with beta-keratin synthesis [10].
• Some evidence suggests that at least some proteins contained within beta-keratin filaments are rich in glycine and resemble some keratin-associated proteins present in mammalian corneous derivatives [11].

Analytical, diagnostic and therapeutic context of LOC408038

• Indirect immunofluorescence microscopy and double-labeling immunogold-electron microscopy confirmed that the stratum germinativum contained alpha keratin but not beta keratin [6].
• In situ hybridization with a beta keratin-specific RNA probe demonstrated that mRNA accumulated in the same regional manner as the polypeptides [4].
• Immunoblotting with the beta-keratin antibody identifies proteic bands according to the isolation method [8].
• The antiserum recognizes beta-cells of lizard epidermis and labels beta-keratin filaments using immunocytochemistry and immunoblotting [11].

References