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Cell Growth and Development

Profilaggrin is a Major Epidermal Calcium-Binding Protein

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Pages 613-625 | Received 30 Jun 1992, Accepted 02 Oct 1992, Published online: 01 Apr 2023

REFERENCES

  • Andresen, K., T. D. Tom, and Μ. Strand. 1991. Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni. J. Biol. Chem. 266:15085–15090.
  • Ausubel, F. Μ., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl. 1991. Current protocols in molecular biology. John Wiley & Sons, New York.
  • Blessing, Μ., J. L. Jorcano, and W. W. Franke. 1989. Enhancer elements directing cell-type-specific expression of Cytokeratin genes and changes of the epithelial cytoskeleton by transfections of hybrid Cytokeratin genes. EMBO J. 8:117–126.
  • Bucher, P., and E. Trifonov. 1986. Compilation and analysis of eukaryotic POL II promoter sequences. Nucleic Acids Res. 14:10009–10026.
  • Chodosh, L. A., A. S. Baldwin, R. W. Carthew, and P. A. Sharp. 1988. Human CCAAT-binding proteins have heterologous subunits. Cell 53:11–24.
  • Dale, B. A., A. Μ. Gown, P. Fleckman, J. R. Kimball, and K. A. Resing. 1987. Characterization of two monoclonal antibodies to human epidermal keratohyalin: reactivity with filaggrin and related proteins. J. Invest. Dermat. 88:306–313.
  • Dale, B. A., K. A. Holbrook, J. R. Kimball, Μ. Hoff, and T.-T. Sun. 1983. Expression of epidermal keratins and filaggrin during human fetal skin development. J. Cell Biol. 101:1257–1269.
  • Dale, B. A., K. A. Holbrook, and P. Μ. Steinert. 1978. Assembly of stratum corneum basic protein and keratin filaments in macrofibrils. Nature (London) 276:729–731.
  • Dale, B. A., K. A. Resing, and P. V. Haydock. 1990. Filaggrins, p. 393–412. In R. D. Goldman and P. Μ. Steinert (ed.), Cellular and molecular biology of intermediate filaments. Plenum Press, New York.
  • Deveroux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387–395.
  • Dlugosz, A., and S. Yuspa. Coordinate changes in gene expression which mark the spinous to granular cell transition in epidermis are regulated by protein kinase C. J. Cell Biol., in press.
  • Dorin, J. R., E. Emslie, and V. van Heyningen. 1990. Related calcium-binding proteins map to the same subregion of chromosome 1q and to an extended region of synteny on mouse chromosome 3. Genomics 8:420–426.
  • Dorin, J. R., Μ. Novak, R. E. Hill, D. J. H Brock, D. D. Secher, and V. van Heyningen. 1987. A clue to the basic defect in cystic fibrosis from cloning the CF antigen. Nature (London) 326:614–617.
  • Eckert, R., and H. Green. 1986. Structure and evolution of the human involucrin gene. Cell 46:583–589.
  • Fairley, J. 1991. Calcium: a second messenger, p. 314–328. In L. A. Goldsmith (ed.), Physiology, biochemistry, and molecular biology of the skin. Oxford University Press, New York.
  • Ferrari, S., B. Calabretta, J. DeRiel, R. Battini, F. Ghezzo, E. Lauret, C. Griffin, B. Emanuel, F. Gurrieri, and R. Beserga. 1987. Structural and functional analysis of a growth related gene, the human calcyclin. J. Biol. Chem. 262:8325–8332.
  • Frohman, Μ. A. 1990. RACE: rapid amplification of cDNA ends, p. 28–38. In Μ. A. Innis, D. H. Gelfand, J. J. Sninski, and T. J. White (ed.), PCR protocols: a guide to methods and applications. Academic Press, New York.
  • Gan, S.-Q., O. W. McBride, N. Markova, W. W. Idler, and P. Μ. Steinert. 1990. Structure, organization and polymorphisms of the human profilaggrin gene. Biochemistry 29:9432–9440.
  • Gerke, V., and K. Weber. 1985. The regulatory chain in the p36-Kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the SlOO protein of glial cells. EMBO J. 4:2917–2920.
  • Hamilton, E. H., R. E. Payne, Jr., and E. J. O’Keefe. 1991. Trichohyalin: presence in the granular layer and stratum corneum of normal human epidermis. J. Invest. Dermatol. 96:666–672.
  • Hardas, B. D., and J. T. Elder. 1992. Physical linkage of CRABP-II and calcyclin on chromosome 1q21 by yeast artificial chromosome cloning, abstr. 105. J. Invest. Dermat. 58:569.
  • Harding, C. R., and I. R. Scott. 1983. Histidine-rich proteins (filaggrins): structural and functional heterogeneity during epidermal differentiation. J. Mol. Biol. 170:651–673.
  • Harper, J. F., Μ. R. Sussman, G. E. Schaller, C. Putnam-Evans, H. Charbonneau, and A. C. Harmon. 1991. A calcium-dependent protein kinase with a regulatory domain similar to calmodulin. Science 252:951–954.
  • Hohl, D., U. Lichti, D. Breitkreutz, P. Steinert, and D. Roop. 1991. Transcription of the human loricrin gene in vitro is induced by calcium and cell density and suppressed by retinoic acid. J. Invest. Dermatol. 96:414–418.
  • Hohl, D., T. Mehrel, U. Lichti, Μ. L. Turner, D. R. Roop, and P. Μ. Steinert. 1991. Characterization of human Ioricrin. Structure and function of a new class of cell envelope proteins. J. Biol. Chem. 266:6626–6636.
  • Jensen, R., D. R. Marshak, C. Anderson, T. J. Lukas, and D. Μ. Watterson. 1985. Characterization of human grain S100 protein fraction: amino acid sequence of S100β. J. Neurochem. 45:700–705.
  • Kawasaki, H., H. Kasai, and T. Okuyama. 1985. Protein analysis and reagents: microscale assay of calcium-binding activity of proteins and peptides using a nitrocellulose membrane. Anal. Biochem. 148:297–302.
  • Kligman, D., and D. Hilt. 1988. The S100 protein family. Trends Biochem. Sci. 13:437–443.
  • Kretsinger, R. H. 1980. Structure and evolution of calcium-modulated proteins. Crit. Rev. Biochem. 8:119–174.
  • Krisinger, J., H. Darwish, N. Maeda, and H. F. De Luca. 1988. Structure and nucleotide sequence of the rat intestinal vitamin D-dependent calcium-binding protein gene. Proc. Natl. Acad. Sci. USA 85:8988–8992.
  • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685.
  • Lagasse, E., and R. Clerc. 1988. Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation. Mol. Cell. Biol. 8:2402–2410.
  • Leask, A., C. Byrne, and E. Fuchs. 1991. Transcription factor AP2 and its role in epidermal-specific gene expression. Proc. Natl. Acad. Sci. USA 88:7948–7952.
  • Leask, A., Μ. Rosenberg, R. Vassar, and E. Fuchs. 1990. Regulation of a human epidermal keratin gene: sequences and nuclear factors involved in keratinocyte-specific transcription. Genes Dev. 4:1985–1998.
  • Lee, S.-C., I.-G. Kim, O. W. McBride, J. G. Compton, E. J. O’Keefe, and P. Μ. Steinert. 1992. The human trichohyalin gene, abstr. 448. J. Invest. Dermatol. 98:626.
  • Lonsdale-Eccles, J. D., J. A. Haugen, and B. A. Dale. 1980. A phosphorylated keratohyalin-derived precursor of epidermal stratum corneum basic protein. J. Biol. Chem. 255:2235–2238.
  • Mack, J. W., and P. Μ. Steinert. The mechanism of interaction of filaggrin with intermediate filaments: the ionic zipper hypothesis. Submitted for publication.
  • Markova, N. G., S.-Q. Gan, and P. Μ. Steinert. Unpublished data.
  • Markova, N. G., and P. Μ. Steinert. Unpublished data.
  • Martensen, T. Μ. 1984. Chemical properties, isolation and analysis of O-phosphates in proteins. Methods Enzymol. 107:3–23.
  • McKinley-Grant, L. G., W. W. Idler, I. A. Bernstein, D. A. D Parry, L. Cannizzaro, C. Μ. Croce, K. Huebner, S. R. Lessin, and P. Μ. Steinert. 1990. Characterization of a cDNA clone encoding human filaggrin and localization of the gene to chromosome region 1q21. Proc. Natl. Acad. Sci. USA 86:4848–4852.
  • Pontremoli, S., and E. Melloni. 1986. Extralysosomal protein degradation. Annu. Rev. Biochem. 55:455–481.
  • Resing, K. A., and B. A. Dale. 1991. Proteins of keratohyalin, p. 148–167. In L. A. Goldsmith (ed.), Physiology, biochemistry, and molecular biology of the skin. Oxford University Press, New York.
  • Resing, K. A., B. A. Dale, and K. A. Walsh. 1985. Multiple copies of phosphorylated filaggrin in epidermal profilaggrin demonstrated by analysis of tryptic peptides. Biochemistry 24:4167–4175.
  • Resing, K. A., K. A. Walsh, and B. A. Dale. 1984. Identification of two intermediates during processing of profilaggrin to filaggrin in neonatal mouse epidermis. J. Cell Biol. 99:1372–1378.
  • Rhim, J. S., J. Jay, P. Arnstein, F. Μ. Price, K. K. Sanford, and S. A. Aaronson. 1985. Neoplastic transformation of human epidermal keratinocytes by AD12-SV40 and Kirsten sarcoma virus. Science (Washington, D.C.) 227:1250–1252.
  • Risse, G., K. Jooss, Μ. Neuberg, H. J. Bruller, and R. Muller. 1989. Asymmetrical recognition of the palindromic AP1 binding site (TRE) by Fos protein complexes. EMBO J. 8:3825–3832.
  • Roeder, R. G. 1991. The complexities of eukaryotic transcription initiation: regulation of preinitiation complex assembly. Trends Biochem. Sci. 16:402–408.
  • Rogers, G. E., Μ. J. Fietz, and A. Fratini. 1991. Trichohyalin and matrix proteins. Ann. N.Y. Acad. Sci. 642:64–81.
  • Rothnagel, J. A., D. A. Greenhalgh, T. Gagne, Μ. A. Longley, D. L. Horak, B. Lu, and D. R. Roop. 1992. Identification of the calcium-sensitive regulatory unit of the gene encoding human keratin I, abstr. 097. J. Invest. Dermatol. 98:568.
  • Rothnagel, J. A., and P. Μ. Steinert. 1990. The structure of the gene for mouse filaggrin and a comparison of the repeating units. J. Biol. Chem. 265:1862–1865.
  • Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
  • Saris, C. J. Μ., T. Kristensen, P. D’Eustachio, L. J. Hicks, D. J. Noonan, T. Hunter, and B. F. Tack. 1987. cDNA sequence and tissue distribution of the mRNA for bovine and murine p11, the S100-related light chain of the protein-tyrosine kinase substrate p36 (calpactin). J. Biol. Chem. 262:10663–10671.
  • Scheidtmann, K. H. 1989. Immunological detection of proteins of known sequence, p. 93–115. In J. Creighton (ed.), Protein structure. IRL Press, Oxford.
  • Scott, I. R., and C. R. Harding. 1981. Studies on the synthesis and degradation of a high molecular weight, histidine-rich phosphoprotein from mammalian epidermis. Biochim. Biophys. Acta 669:65–78.
  • Scott, I. R., and C. R. Harding. 1986. Filaggrin breakdown to water binding compounds during development of the rat stratum corneum is controlled by the water environment. Dev. Biol. 115:84–92.
  • Steinert, P. Μ., J. S. Cantieri, D. C. Teller, J. D. LonsdaleEccles, and B. A. Dale. 1981. Characterization of a class of cationic proteins that specifically interact with intermediate filaments. Proc. Natl. Acad. Sci. USA 78:4097–4101.
  • Steinert, P. Μ., and D. R. Roop. 1988. Molecular and cellular biology of intermediate filaments. Annu. Rev. Biochem. 57:593–625.
  • Steinert, P. Μ., R. Zackroff, Μ. Aynardi-Whitman, and R. Goldman. 1982. Isolation and characterization of intermediate filaments. Methods Cell Biol. 24:399–419.
  • Steven, A. C., Μ. E. Bisher, D. R. Roop, and P. Μ. Steinert. 1990. Biosynthetic pathways of filaggrin and Ioricrin—two major proteins expressed by terminally differentiated mouse keratinocytes. J. Struct. Biol. 104:150–162.
  • Strynadka, N., and Μ. James. 1989. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Bio-chem. 58:951–998.
  • Suzuki, K. 1987. Calcium-activated neutral proteases: domain structure and activity regulation. Trends Biochem. Sci. 12:103–105.
  • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350–4354.
  • Van Eldik, L. J., J. G. Zendegui, D. R. Marshak, and D. Μ. Watterson. 1982. Calcium-binding proteins and the molecular basis of calcium action. Int. Rev. Cytol. 77:1–61.
  • Williams, Μ. L., and P. Μ. Elias. 1987. Genetically transmitted, generalized disorders of cornification. The ichthyoses, p. 155–178. In J. C. Alper (ed.), Dermatologic clinics, vol. 5. The genodermatoses. The W. B. Saunders Co., Philadelphia.
  • Wood, L., D. Carter, Μ. Mills, N. Hatzenbuhler, and G. Vogeli. 1991. Expression of calcyclin, a calcium-binding protein, in the keratogenous region of growing hair follicles. J. Invest. Dermat. 56:383–387.
  • Yoneda, K., D. Hohl, O. W. McBride, Μ. Wang, K. Cehrs, W. W. Idler, and P. Μ. Steinert. 1992. The human Ioricrin gene. J. Biol. Chem. 267:18060–18066.
  • Yuspa, S. H., A. E. Kilkenny, P. Μ. Steinert, and D. R. Roop. 1989. Expression of murine epidermal differentiation markers is tightly regulated by restricted extracellular calcium concentrations in vitro. J. Cell Biol. 109:1207–1217.

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