BMC Biophys 2013 Sep 5;6(1):12. Epub 2013 Sep 5.
Unilever R&D Port Sunlight, Quarry Road East, Bebington, Wirral, CH63 3JW, UK.
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J Invest Dermatol 2004 Oct;123(4):715-32
Group of Applied Physics-Biomedical, Department of Physics, University of Geneva, Geneva, Switzerland.
A new model for stratum corneum keratin structure, function, and formation is presented. The structural and functional part of the model, which hereafter is referred to as "the cubic rod-packing model", postulates that stratum corneum keratin intermediate filaments are arranged according to a cubic-like rod-packing symmetry with or without the presence of an intracellular lipid membrane with cubic-like symmetry enveloping each individual filament. The new model could account for (i) the cryo-electron density pattern of the native corneocyte keratin matrix, (ii) the X-ray diffraction patterns, (iii) the swelling behavior, and (iv) the mechanical properties of mammalian stratum corneum. Read More
J Mol Biol 1993 Jul;232(1):50-66
Skin Biology Branch, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892.
Filaggrins of mammalian epidermis represent archetypical examples of intermediate filament-associated proteins that can bind large numbers of intermediate filaments in vitro (and keratin filaments in vivo) into macrofibrils. To explore the mechanism of this interaction, the secondary structures of filaggrins were analyzed. As much as 80% of mouse and human filaggrins consist of multiple repeating elements. Read More
J Cell Biol 1990 Dec;111(6 Pt 2):3049-64
Howard Hughes Medical Institute, Departments of Molecular Genetics, Chicago, Illinois.
To investigate the sequences important for assembly of keratins into 10-nm filaments, we used a combined approach of (a) transfection of mutant keratin cDNAs into epithelial cells in vivo, and (b) in vitro assembly of mutant and wild-type keratins. Keratin K14 mutants missing the nonhelical carboxy- and amino-terminal domains not only integrated without perturbation into endogenous keratin filament networks in vivo, but they also formed 10-nm filaments with K5 in vitro. Surprisingly, keratin mutants missing the highly conserved L L E G E sequence, common to all intermediate filament proteins and found at the carboxy end of the alpha-helical rod domain, also assembled into filaments with only a somewhat reduced efficiency. Read More
J Invest Dermatol 2001 Jan;116(1):157-66
Department of Animal Science, University of Adelaide, Adelaide, South Australia.
A unique type I keratin intermediate filament group, comprising three highly related proteins and expressed in the inner root sheath of hair follicles, has been identified in both sheep and human. The first members from these species are named oIRSa1 and hIRSa1 and each encodes a protein of 450 amino acids, with compositional characteristics intermediate between those of previously described hair keratin and epidermal cytokeratin type I intermediate filaments. Detection of abundant mRNA transcripts derived from the sheep and human genes by cRNA in situ hybridization only in the inner root sheath and not in the medulla concurs with the findings of earlier ultrastructural analyses that have reported intermediate filaments only in the inner root sheath. Read More