Chapter 3 Expression and Modification of Keratins During Terminal Differentiation of Mammalian Epidermis
January 1987
in “
Current topics in developmental biology/Current Topics in Developmental Biology
”
Research cited in this study
5 / 5 resultsresearch The complement of native α-keratin polypeptides of hair-forming cells: A subset of eight polypeptides that differ from epithelial cytokeratins
research Genes for Hair and Avian Keratins
research Trans glutaminase-mediated cross-linking in mammalian epidermis
research Different keratin polypeptides in epidermis and other epithelia of human skin: a specific cytokeratin of molecular weight 46,000 in epithelia of the pilosebaceous tract and basal cell epitheliomas.
The study analyzed cytokeratin polypeptides in human skin, focusing on the epidermis, pilosebaceous tract, and eccrine sweat glands, using gel electrophoresis and antibody binding. It found that the pilosebaceous tract shared some keratins with interfollicular epidermis but had a unique acidic cytokeratin of molecular weight 46,000. This keratin was also prominent in basal-cell epitheliomas, showing a similarity between these tumors and hair-follicle epithelium. The study concluded that different skin epithelia could be distinguished by their specific cytokeratin patterns, and the cytoskeleton of basal-cell epitheliomas was related to that of the pilosebaceous tract.
research Characterization of the Proteins of Guinea-Pig Hair and Hair-Follicle Tissue
Guinea-pig hair and follicle proteins are mostly similar, but follicles have more group 2 proteins and fewer group 3 and 4 proteins.
Related Research
1 / 1 results
research Keratin and Skin Disorders
Changes in keratin affect skin health and can lead to skin disorders like blistering diseases and psoriasis.