Epidermal structural proteins in skin disorders

Journal of Dermatological Science

Volumn 15, Issue 3, 1997, Pages 143-165

  Manabe, Motomu ^a   Mizoguchi, Masayuki ^a   Suto, Hajime ^a   Ogawa, Hideoki ^a  

^a JUNTENDO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIBODY; CYSTATIN; ELAFIN; ENVELOPE PROTEIN; FILAGGRIN; INTERMEDIATE FILAMENT PROTEIN; INVOLUCRIN; KERATIN; KERATOHYALIN; LORICRIN; PROLINE; STRUCTURAL PROTEIN; TRICHOHYALIN; UNCLASSIFIED DRUG;

EPIDERMOLYSIS BULLOSA SIMPLEX; GENE EXPRESSION REGULATION; GENODERMATOSIS; HUMAN; ICHTHYOSIS; KERATINOCYTE; KERATOSIS PALMOPLANTARIS; MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PSORIASIS; REVIEW; SKIN DISEASE;

ANIMALS; EPIDERMIS; HUMANS; INTERMEDIATE FILAMENT PROTEINS; MEMBRANE PROTEINS; PROTEINS; SKIN DISEASES;

EID: 0030841583     PISSN: 09231811     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0923-1811(97)00618-X     Document Type: Review

References (167)

1. Fuchs E: Epidermal differentiation: the bare essentials. J Cell Biol 111: 2807-2814, 1990.
2. Fuchs E: Intermediate filaments and disease: mutations that cripple cell strength. J Cell Biol 125: 511-516, 1994.
3. McLean WHI, Lane EB: Intermediate filaments in disease. Curr Opin Cell Biol 7: 118-125, 1995.
4. Rothnagel JA: The role of keratin mutations in disorders of the skin. Curr Opin Dermatol 3: 127-136, 1996.
5. O'Guin WM, Manabe M: The role of trichohyalin in hair follicle differentiation and its expression in nonfollicular epithelia. In The Molecular and Structural Biology of the Hair. Ann NY Acad Sci 642: 51-63, 1992.
6. Manabe M, O'Guin WM: Keratohyalin, trichohyalin and keratohyalin-trichohyalin hybrid granules: an overview. J Dermatol 19: 749-755, 1992.
7. Fuchs E, Weber K: Intermediate filaments: structure, dynamics, function, and disease. Annu Rev Biochem 63: 345-382, 1994.
8. Klymkowsky MW: Intermediate filaments: new proteins, some answers, more questions. Curr Opin Cell Biol 7: 46-54, 1995.
9. Galvin S, Loomis C, Manabe M, Dhouailly D, Sun T-T: The major pathways of keratinocyte differentiation as defined by keratin expression: an overview. Adv Dermatol 4: 277-300, 1988.
10. O'Guin WM, Schermer A, Lynch M, Sun T-T: Differentiation-specific expression of keratin pairs. In Cellular and Molecular Biology of Intermediate Filaments. Edited by RD Goldman, PM Steinert. Plenum Publishing Co., 1990, pp. 301-334.
11. Bowden PE: Keratins and other epidermal proteins. In Molecular Aspect of Dermatology. Edited by GC Priestley. John Wiley and Sons Ltd., Chichester, 1993, pp. 19-54.
12. Steinert PM: Structure, function, and dynamics of keratin intermediate filaments. J Invest Dermatol 100: 729-734, 1993.
13. Steinert PM, North ACT, Parry DAD: Structural features of keratin intermediate filaments. J Invest Dermatol 103: 19S-24S, 1994.
14. Yasser R, Coulombe PA, Degenstein L, Albers K, Fuchs E: Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease. Cell 64: 365-380, 1991.
15. Bonifas JM, Rothman AL, Epstein EH: Epidermolysis bullosa simplex: evidence in two families for keratin gene abnormalities. Science 254: 1202-1205, 1991.
16. Coulombe PA, Hutton ME, Letai A, Hebert A, Paller ASS, Fuchs E: Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: genetic and functional analysis. Cell 66: 1301-1311, 1991.
17. Goldsmith LA: Mutations in epidermolysis bullosa simplex. J Invest Dermatol 105: 529-531, 1995.
18. Rothnagel JA, Dominey AM, Dempsey LD, Longley MA, Greenhalg DA, Gagne TA, Huber M, Frenk E, Hohl D, Roop DR: Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis. Science 257: 1128-1130, 1992.
19. Chen J, Syder AJ, Yu Q-C, Letai A, Paller A, Fuchs E: The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes. Cell 70: 811-819, 1992.
20. Rothnagel JA, Traupe H, Wojcik S, Huber M, Hohl D, Pittelkow MR, Saeki H, Ishibashi Y, Roop DR: Mutations in the rod domains of keratin 2e in patients with ichthyosis bullosa of Siemens. Nature Genet 7: 485-490, 1994.
21. McLean WHI, Morley SM, Lane EB, Eady RAJ, Griffiths WAD, Paige DG, Happer JI, Higgins C, Leigh IM: Ichthyosis bullosa of Siemens: a disease involving keratin 2e. J Invest Dermatol 103: 277-281, 1994.
22. Kremer H, Zeuwen P, McLean WHI, Mariman ECM, Lane EB, Van der Kerkhof PCM, Ropers H-H, Steijlen PM: Ichthyosis bullosa of Siemens is caused by mutations in the keratin 2e gene. J Invest Dermatol 103: 286-289, 1994.
23. Reis A, Hennies HC, Langbein L, Digweed M, Mischke D, Drechsler M, Schrock E, Royer-Pokora B, Franke WW, Sperling K, Kunster W: Keratin 9 gene mutation in epidermolytic palmoplantar keratoderma (EPPK). Nature Genet 6: 174-179, 1994.
24. Kimonis V, DiGiovanna JJ, Yang J-M, Doyle SZ, Bale SJ, Compton JG: A mutation in the V1 end domain of keratin 1 in non-epidermolytic palmar-plantar keratoderma. J Invest Dermatol 103: 764-769, 1994.
25. Kouklis PD, Hutton E, Fuchs E: Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins. J Cell Biol 127: 1049-1060, 1994.
26. Risk JM, Field EA, Field JK, Whittaker J, Freyer A, Ellis A, Shaw JM, Friedmann PS, Bishop DT, Bodmer J et al. Tylosis oesophageal cancer mapped. Nature Genet 8: 319-321, 1994.
27. Stevens HP, Kelsell DP, Bryant SP, Bishop T, Spurr NK, Weissenbach J, Marger D, Marger R, Leigh IR: Linkage of an American pedigree with palmoplantar keratoderma and malignancy (palmoplantar ectodermal dysplasia type III) to 17q24: literature survey and proposed updated classification of the keratodermas. Arch Dermatol 132: 640-651, 1996.
28. McLean WHI, Rugg EL, Lunny DP, Morley SM, Lane EB, Swensson O, Dopping-Hepenstal PJC, Griffiths WAD, Eady RAJ, Higgins C, Navsaria HA, Leigh IM, Strachan T, Kunkeler L, Munro CS: Keratin 16 and keratin 17 mutations cause pachyonychia congenita. Nature Genet 9: 273-278, 1995.
29. Bowden PE, Haley JL, Kansky A, Rothnagel JA, Jones DO, Turner RJ: Mutation of a type II keratin gene (K6a) in pachyonychia congenita. Nature Genet 10: 363-365, 1995.
30. Rugg EL, McLean WHI, Allison WE, Lunny DP, Macleod RI, Felix DH, Lane EB, Munro CS: A mutation in the mucosal keratin K4 is associated with oral white sponge nevus. Nature Genet 11: 450-452, 1995.
31. Richard G, De Laurenzi V, Didona B, Bale SJ, Compton J: Keratin 13 point mutation underlies the hereditary mucosal epithelia disorder white sponge nevus. Nature Genet 11: 453-455, 1995.
32. Dale BA, Presland RB, Fleckman P, Kam E, Resing KA: Phenotypic expression and processing of filaggrin in epidermal differentiation. In Molecular Biology of the Skin, Vol. 1. The Keratinocyte. Edited by M Darmon, M Blumenberg. Academic Press, New York, 1993, pp. 79-106.
33. Resing KA, Johnson RS, Walsh KA: Mass spectrometric analysis of 21 phosphorylation sites in the internal repeat of rat profilaggrin, precursor of an intermediate filament associated protein. Biochemistry 34: 9477-9487, 1995.
34. Kam E, Resing KA, Lim SK, Dale BA: Identification of rat epidermal profilaggrin phosphatase as a member of the protein phosphatase 2A family. J Cell Sci 106: 219-226, 1993.
35. 2+ in the second stage. J Biol Chem 268: 25139-25145, 1993.
36. Resing KA, Thulin C, Whiting K, Al-Alaw N, Mostad S: Characterization of profilaggrin endoproteinase 1: a regulated cytoplasmic endoproteinase of epidermis. J Biol Chem 270: 28193-28198, 1985.
37. Resing KA, Walsh KA, Haugen SJ, Dale BA: Identification of proteolytic cleavage sites in the conversion of profilaggrin to filaggrin in mammalian epidermis. J Biol Chem 264: 1837-1845, 1989.
38. Resing KA, Johnson RS, Walsh KA: Characterization of protease processing sites during conversion of rat profilaggrin to filaggrin. Biochemistry 32: 10036-10045, 1993.
39. 2+ in the second stage. J Biol Chem 268: 25139-25145, 1993.
40. Rothnagel JA, Mehrel T, Idler WW, Roop DR, Steinert PM: The gene for mouse epidermal filaggrin precursor. Its partial characterization, expression, and sequence of a repeating filaggrin unit. J Biol Chem 262: 15643-15648, 1987.
41. McKinley-Grant LJ, Idler WW, Bernstein IA, Parry DA, Cannizzaro L, Croce CM, Huebner K, Lessin SR, Steinert PM: 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, 1989.
42. Rothnagel JA, Steinert PM: The structure of the gene for mouse filaggrin and a comparison of the repeating units. J Biol Chem 265: 1862-1865, 1990.
43. Gan S-Q, McBride OW, Idler WW, Markova N, Steinert PM: Organization, structure, and polymorphisms of the human profilaggrin gene. Biochemistry 29: 9432-9440, 1990.
44. Haydock PV, Dale BA: Filaggrin, an intermediate filament-associated protein: structural and functional implication from the sequence of a cDNA from rat. DNA Cell Biol 9: 251-261, 1990.
45. Presland RB, Haydock PV, Fleckman P, Nirunsuksiri W, Dale BA: Characterization of the human epidermal profilaggrin gene: genomic organization and identification of an S100-like calcium binding domain at the aminoterminus. J Biol Chem 267: 23772-23781, 1992.
46. Markova NG, Marekov LN, Chipev CC, Gan S-Q, Idler WW, Steinert PM: Profilaggrin is a major epidermal calcium-binding protein. Mol Cell Biol 13: 613-625, 1993.
47. Presland RB, Bassuk JA, Kimball JR, Dale BA: Characterization of two distinct calcium-binding sites in the amino-terminus of human profilaggrin. J Invest Dermatol 104: 218-223, 1995.
48. Mischke D, Korge BP, Marenholz I, Volz A, Ziegler A: Genes encoding structural proteins of epidermal cornification and S100 calcium-binding proteins from a gene complex ('epidermal differentiation complex') on human chromosome 1q21 (and references therein). J Invest Dermatol 106: 989-992, 1996.
49. Sybert VP, Dale BA, Holbrook KA: Ichthyosis vulgaris: identification of a defect in synthesis of filaggrin correlated with an absence of keratohyalin granules. J Invest Dermatol 84: 191-194, 1985.
50. Manabe M, Sanchez M, Sun T-T, Dale BA: Interaction of filaggrin with keratin filaments during advanced stages of normal human epidermal differentiation and in Ichthyosis vulgaris. Differentiation 48: 43-50, 1991.
51. Nirunsuksiri W, Presland RB, Brumbaugh SG, Dale BA, Fleckman P: Decreased profilaggrin expression in ichthyosis vulgaris is a result of selectively impaired post-transcriptional control. J Biol Chem 270: 871-876, 1995.
52. Young BJJ, Mallya RK, Leslie RDG, Clark CJM, Hamblin TJ: Antikeratin-antibodies in rheumatoid arthritis. Br Med J 2: 97-99, 1979.
53. Quismono FP Jr., Kaufman RL, Beardmore T, Mongan ES: Reactivity of serum antibodies to the keratin layer of rat esophagus in patients with rheumatoid arthritis. Arthritis Rheum 26: 494-499, 1983.
54. Johnson GD, Carvalho A, Holborow EJ, Goddard DH, Russel G: Antiperinuclear factor and keratin antibodies in rheumatoid arthritis. Ann Rheum Dis 40: 263-266, 1981.
55. Simon M, Girbal E, Sebbag M, Gomes-Daudrix V, Vincent C, Salama G, Serre G: The cytokeratin filament-aggregating protein filaggrin is the target of the so-called 'antikeratin antibodies', autoantibodies specific for rheumatoid arthritis. J Clin Invest 92: 1387-1393, 1993.
56. Miossec P, Youinou P, Le Goff P, Moineau MP: Clinical relevance of antikeratin antibodies in rheumatoid arthritis. Clin Rheumatol 1: 185-189, 1982.
57. Ordeig J, Guardia JJ: Diagnostic value of antikeratin antibodies in rheumatoid arthritis. J Rheumatol 11: 602-604, 1984.
58. Hajiroussou VJ, Skingle J, Gillett AP. Webley MJ: Significance of antikeratin antibodies in rheumatoid arthritis. J Rheumatol 12: 57-59, 1985.
59. Vincent C, Serre G, Lapeyre F, Fournié B, Ayrolles C, Fournié A, Soleilhavoup J-P: High diagnostic value in rheumatoid arthritis of antibodies to the stratum corneum of rat oesophagus epithelium, so-called 'antikeratin antibodies'. Ann Rheum Dis 48: 712-722, 1989.
60. Paimela L, Gripenberg M, Kurki P, Leirisalo-Repo M: Anti-keratin antibodies: diagnosis and prognostic markers for early rheumatoid arthritis. Ann Rheum Dis 51: 743-746, 1992.
61. Kurki P, Aho K, Palosuo T, Heliüvaara MP: Immunopathology of rheumatoid arthritis: antikeratin antibodies precede the clinical disease. Arthritis Rheum 35: 914-917, 1992.
62. Manabe M, O'Guin WM: Keratohyalin, trichohyalin and keratohyalin-trichohyalin hybrid granules: an overview. J Dermatol 19: 749-755, 1992.
63. Fietz MJ, McLaughlan CJ, Campbell MT, Rogers GE: Analysis of the sheep trichohyalin gene: potential structural and calcium-binding roles of trichohyalin in the hair follicle. J Cell Biol 121: 855-865, 1993.
64. Lee S-C, Kim I-G, Marekov LN, O'Keefe EJ, Parry DAD, Steinert PM: The structure of human trichohyalin. Potential multiroles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein. J Biol Chem 268: 12164-12176, 1993.
65. O'Guin WM, Sun T-T, Manabe M. Interaction of trichohyalin with intermediate filaments: three immunologically defined stages of trichohyalin maturation. J Invest Dermatol 98: 24-32, 1992.
66. Holbrook KA. Biologic structure and function: perspectives on morphologic approaches to the study of the granular layer keratinocyte. J Invest Dermatol 92: 84s-104s, 1989.
67. Manabe M, O'Guin WM. Existence of trichohyalin-keratohyalin hybrid granules in non-follicular epithelia: the co-localization of two major intermediate filament-associated proteins. Differentiation 58: 65-67, 1994.
68. Manabe M, Yaguchi H, Butt KI, O'Guin WM, Sun T-T, Ogawa H: Expression of keratohyalin-trichohyalin hybrid granules in molluscum contagiosum. Int J Dermatol 35: 106-108, 1996.
69. Manabe M, Yaguchi H, Butt KI, O'Guin WM, Loomis CA, Sun T-T, Ogawa H: Trichohyalin expression in skin tumors: retrieval of trichohyalin antigenicity in formalin-fixed, paraffin-embedded tissues by microwave irradiation. Int J Dermatol 35: 325-329, 1996.
70. Shamsher MK, Navsaria HA, Stevens HP, Ratnavel RC, Purkis PE, Kelsell DP, McLean WHI, Cook LJ, Griffiths WAD, Gschmeissner S, Spurr N, Leigh IM: Novel mutations in keratin 16 gene underly focal nonepidermolytic palmoplantar keratoderma (NEPPK) in two families. Hum Mol Genet 4: 1875-1881, 1995.
71. Hosokawa K, Hosokawa H, Futamura S, Baden PH: Proteins of the cornified envelope. J Dermatol 19: 744-748, 1992.
72. Steinert PM, Marekov LN: The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope. J Biol Chem 270: 17702-17711, 1995.
73. Mehrel T, Hohl D, Rothnagel JA, Longley MA, Bundman D, Cheng C, Lichti U, Bisher ME, Steven AC, Steinert PM, Yuspa SH, Roop DR: Identification of a major keratinocyte cell envelope protein, loricrin. Cell 61: 1103-1112, 1990.
74. Steven AC, Bisher ME, Roop DR, Steinert PM: Biosynthetic pathways of filaggrin and loricrin - two major proteins expressed by terminally differentiated epidermal keratinocytes. J Struct Biol 104: 150-162, 1990.
75. Hohl D, Mehrel T, Lichti U, Truner ML, Roop DR, Steinert PM: Characterization of human loricrin, structure and function of a new class of epidermal cell envelope proteins. J Biol Chem 266: 6626-6636, 1991.
76. Yoneda K, Hohl D, McBrider W, Wang M, Cehrs KU, Idler WW, Steinert PM: The human loricrin gene. J Biol Chem 267: 18060-18066, 1992.
77. Ishida-Yamamoto A, Hohl D, Roop DR, Iizuka H, Eady RAJ: Loricrin immunoreactivity in human skin: localization to specific granules (L-granules) in acrosyringia. Arch Dermatol Res 285: 491-498, 1993.
78. Ishida-Yamamoto A, Eady RAJ, Watt FM, Roop DR, Hohl D, Iizuka H: Immunoelectron microscopic analysis of cornified cell envelope formation in normal and psoriatic epidermis. J Histochem Cytochem 44: 167-175, 1996.
79. DiSepio D, Jones A, Longley MA, Bundmant D, Rothnagel JA, Roop DR: The proximal promoter of the mouse loricrin gene contains a functional AP-1 element and directs keratinocyte specific but not differentiationspecific expression. J Biol Chem 270: 10792-10799, 1995.
80. Steinert PM, Mack JW, Korge BP, Gan SQ, Haynes SR, Stevens AC: Glycine loops in proteins: their occurrence in certain intermediate filament chains, loricrin and single-stranded RNA binding proteins. Int J Biol Macromol 13: 130-139, 1991.
81. Candi E, Melino G, Mei G, Tarcsa E, Chung S-II, Marekov LN, Steinert PM: Biochemical, structural, and transglutaminase substrate properties of human loricrin, the major epidermal cornified cell envelope protein. J Biol Chem 270: 26382-26390, 1995.
82. Roop DR: Defects in the barrier. Science 267: 474-475, 1995.
83. Yoneda K, Steinert PM: Overexpression of human loricrin in transgenic mice produces a normal phenotype. Proc Natl Acad Sci USA 90: 10754-10758, 1993.
84. Maestrini E, Monaco AP, McGrath JA, Ishida-Yamamoto A, Camisa C, Hovnanian A, Weeks DE, Lathrop M, Uitto J, Christiano AM: A molecular defect in loricrin, the major component of the cornified cell envelope, underlies Vohwinkel's syndrome. Nature Genet 13: 70-77, 1996.
85. Barrett AJ: The cystatins: a new class of peptidase inhibitors. Trends Biol Sci 12: 193-196, 1987.
86. Turk V, Bode W: The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett 285: 213-219, 1991.
87. Calkins CC, Sloane BF: Mammalian cysteine protease inhibitors: biochemical properties and possible roles in tumor progression. Biol Chem Hoppe-Seyler 376: 71-80, 1995.
88. Barrett AJ, Fitz H, Grubb A, Isemura S, Järvinen M, Katsunuma N, Machleidt W, Müller-Esterl W, Sasaki M, Turk V: Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin. Biochem J 236: 312, 1986.
89. Rawings ND, Barrett AJ: Evolution of proteins of the cystatin superfamily. J Mol Evol 30: 60-71, 1990.
90. Bode W, Engh R, Musil D, Thiele U, Huber R, Karshikov A, Brzin J, Kos J, Turk V: The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J 7: 2593-2599, 1988.
91. Machleidt W, Thiele U, Laber B, Assfalg-Machleidt I, Esterl A, Wiegand G, Kos J, Turk V, Bode W: Mechanism of inhibition of papain by chicken egg white cystatin. FEBS Lett 243: 234-238, 1989.
92. Takeda A, Kaji H, Nakaya K, Nakamura Y, Samejima T: Amino acid sequence of derivative of newborn rat epidermal thiol proteinase inhibitor. Biochem Int 11: 557-564, 1985.
93. 2-terminal region of the cystatin proteinase inhibitor is essential for expression of its inhibitory activity. Biochemistry 34: 12185-12192, 1995.
94. Takahashi M, Tezuka T, Towatari T, Katunuma N: Properties and nature of a cysteine proteinase inhibitor located in keratohyalin granules of rat epidermis. FEBS Lett 267: 261-264, 1990.
95. Takahashi M, Tezuka T, Towatari T, Katunuma N: Identification of hematoxylin-stainable protein in epidermal keratohyalin granules as phosphorylated cystatin χ by protein kinase C. FEBS Lett 287: 178-180, 1991.
96. Takahashi M, Tezuka T, Katunuma N: Phosphorylated cystatin χ is a natural substrata of epidermal transglutaminase for formation of skin cornified envelope. FEBS Lett 308: 79-82, 1992.
97. Takahashi M, Tezuka T, Katunuma N: Filaggrin linker segment peptide and cystatin alpha are part of a complex of the cornified envelope of epidermis. Arch Biochem Biophys 329: 123-126, 1996.
98. Rinne A, Räsänen O, Järvinen M, Demmert K, Kallioinen M, Hopsu-Havu VK: Occurrence of acidic and neutral cysteine proteinase inhibitors in epidermal malignancies: immunohistochemical study. Acta Histochem 74: 75-79, 1984.
99. Howley-Nelson P, Roop DR, Cheng CK, Krieg TM, Yuspa SH: Molecular cloning of mouse epidermal cystatin A and detection of regulated expression in differentiation and tumorigenesis. Mol Carcinogen 1: 202-211, 1988.
100. Lah TT, Clifford JL, Heimer KM, Day NA, Moin K, Honn KV, Crissman JD, Sloane BF: Inhibitory properties of low molecular mass cysteine proteinase inhibitors from human sarcoma. Biochem Biophys Acta 993: 67-73, 1989.
101. Ghiso J, Jensson O, Frangione B: Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of g-trace basic protein (cystatin C). Proc Natl Acad Sci USA 83: 2974-2978, 1986.
102. Hiwasa T, Yokoyama S, Ha J-M, Noguchi S, Sakiyama S: c-Ha-ras gene products are potent inhibitors of cathepsins B and L. FEBS Lett 211: 23-26, 1987.
103. Hiwasa T, Sakiyama S, Noguchi S, Ha J-M, Yokoyama S: Degradation of a cAMP-binding protein is inhibited by human c-Ha-ras gene products. Biochem Biophys Res Commun 146: 731-738, 1987.
104. Hiwasa T, Sakiyama S, Yokoyama S, Ha J-M, Fujita J, Noguchi S, Bando Y, Kominami E, Katunuma N: Inhibition of cathepsin L-induced degradation of epidermal growth factor receptors by c-Ha-ras gene products. Biochem Biophys Res Commun 151: 78-85, 1988.
105. Hisawa T, Fujita-Yoshigaki J, Shirouzu M, Koide H, Sawada T, Sakiyama S, Yokoyama S: c-Ha-ras mutants with point mutations in Gln-Val-Val region have reduced inhibitory activity toward cathepsin B. Cancer Lett 69: 161-165, 1993.
106. Björck J, Åkesson P, Bohus M, Trojnar J, Abrahamson M, Olafsson I, Grubb A: Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor. Nature 337: 385-386, 1989.
107. Takahashi M, Tezuka T, Katunuma N: Inhibitory of growth and cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin A in skin cornified envelope. FEBS Lett 355: 275-278, 1994.
108. Eckert RL, Yaffe MB, Crish JF, Murthy S, Rorke EA, Welter JF: Involucrin - structure and role in envelope assembly. J Invest Dermatol 100: 613-617, 1993.
109. Yaffe MB, Murthy S, Eckert RL: Evidence that involucrin is a covalently linked constituent of highly purified cultured keratinocyte cornified envelopes. J Invest Dermatol 100: 3-9, 1993.
110. Rice RH, Green H: Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: activation of the cross-linking by calcium ions. Cell 18: 681-694, 1979.
111. Warhol MJ, Antonioli DA, Pinkus GS, Burke L, Rice RH: Immunoperoxidase staining for involucrin: a potential diagnostic aid in cervicovaginal pathology. Hum Pathol 13: 1095-1099, 1982.
112. Banks-Schlegel S, Green H: Involucrin synthesis and tissue assembly by keratinocytes in natural and cultured human epithelia. J Cell Biol 90: 732-737, 1981.
113. Banks-Schlegel S, Green H: Formation of epidermis by serially cultivated human epidermal cells transplanted as an epithelium to athymic mice. Transplantation 29: 308-313, 1980.
114. Simon M, Green H: Participation of membrane-associated proteins in the formation of the cross-linked envelope of the keratinocyte. Cell 36: 827-834, 1984.
115. Simon M, Green H: Enzymatic cross-linking of involucrin and other proteins by keratinocyte particulates in vitro. Cell 40: 677-683, 1985.
116. Simon M, Green H: The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin. J Biol Chem 263: 18093-18098, 1988.
117. Eckert RL, Green H: Structure and evolution of the human involucrin gene. Cell 46: 583-589, 1986.
118. Yaffe MB, Beegen H, Eckert RL: Biophysical characterization of involucrin reveals a molecule ideally suited to function as an intermolecular cross-bridge of the keratinocyte cornified envelope. J Biol Chem 267: 12233-12238, 1992.
119. Tseng H, Green H: Remodelling of the involucrin gene during primate evolution. Cell 54: 491-496, 1988.
120. Teumer J, Green H: Divergent evolution of part of the involucrin gene in the hominoids: unique intragenic duplications in the gorilla and human. Proc Natl Acad Sci USA 86: 1283-1286, 1989.
121. Green H, Dijian P: Consecutive actions of different gene-altering mechanisms in the evolution of involucrin. Mol Biol Evol 9: 977-1017, 1992.
122. Critsh JF, Howard JM, Zaim TM, Murthy S, Eckert RL: Tissue-specific and differentiation-appropriate expression of the human involucrin gene in transgenic mice: an abnormal epidermal phenotype. Differentiation 53: 191-200, 1993.
123. Kartasova T, Van de Putte P: Isolation, characterization, and UV-stimulated expression of two families of genes encoding polypeptides of related structure in human epidermal keratinocytes. Mol Cell Biol 8: 2195-2203, 1988.
124. Kartasova T, Van Muijen G, Van Pelt-Heersshap H, Van de Putte P: Novel protein in human epidermal keratinocytes: regulation of expression during differentiation. Mol Cell Biol 8: 2204-2210, 1988.
125. An G, Huang T, Tesfaigzi J, Garcia-Heras J, Ledbetter D, Carlson D, Wu R: An unusual expression of a squamous cell marker, small proline-rich protein gene, in tracheobronchial epithelium: differential regulation and gene mapping. Am J Respir Cell Mol Biol 7: 104-114, 1992.
126. Smits H, Floyd E, Jetten A: Molecular cloning of gene sequences regulated during squamous differentiation of tracheal epithelial cells and controlled by retinoic acid. Mol Cell Biol 7: 4017-4023, 1987.
127. Marvin K, George M, Fujimoto W, Saunders N, Bernacki S, Jetten A: Cornifin, a cross-linked envelope precursor in keratinocytes that is down-regulated by retinoids. Proc Natl Acad Sci USA 89: 11026-11030, 1992.
128. Austin SJ, Fujimoto W, Marvin KW, Vollberg TM, Lorand L, Jetten AM: Cloning and regulation of cornifin b, a new member of the cornifin/spr family. Suppression by retinoic acid receptor-selective retinoids. J Biol Chem 271: 3737-3742, 1996.
129. Phillips SB, Kubilus J, Grassi AM, Goldaber ML, Baden HP: The pancornulins: a group of basic low molecular weight proteins in mammalian epidermis and epithelium that may function as cornified envelope precursors. Comp Biochem Physiol 95B: 781-788, 1990.
130. Greco MA, Lorand L, Lane WS, Baden HP, Parameswaran KNP, Kvedar JC: The pancornulins: a group of small proline rich-related cornified envelope precursors with bifunctional capabilities in isopeptide bond formation. J Invest Dermatol 104: 204-210, 1995.
131. Yaar M, Eller MS, Bhawan J, Harkness DD, DiBenedetto PJ, Gilchrest BA: In vivo and in vitro SPRR1 gene expression in normal and malignant keratinocytes. Exp Cell Res 217: 217-226, 1995.
132. Hohl D, de Viragh PA, Amiguet-Barras F, Gibbs S, Backendorf C, Huber M: The small proline-rich proteins constitute a multigene family of differentially regulated cornified cell envelope precursor proteins. J Invest Dermatol 104: 902-909, 1995.
133. Fujimoto W, Nakanishi G, Arata J, Jetten AM: Differential expression of human cornifin a and b and in squamous differentiating epithelial tissues and several skin lesions. J Invest Dermatol (in press).
134. Owens DM, Zainal TA, Jetten AM, Smart RC: Localization and expression of cornifin-χ/SPRR1 in mouse epidermis, anagen hair follicles, and skin neoplasms. J Invest Dermatol 106: 647-654, 1996.
135. Tesfaigzi J, Wright P, Oreffo V, An G, Wu R. Carlson D: A small proline-rich protein regulated by vitamin A in tracheal epithelial cells is induced in lung tumors. Am J Respir Cell Mol Biol 9: 434-440, 1993.
136. An G, Tesfaigzi J, Chuu Y-J, Wu R: Isolation and characterization of the human spr1 gene and its regulation of expression by phorbol ester and cyclic AMP. J Biol Chem 268: 10977-10982, 1993.
137. Gibbs S, Fijneman R, Wiegant J, van Kessel AG, van de Putte P, Backendorf C: Molecular characterization and evolution of the SPRR family of keratinocyte differentiation markers encoding small proline-rich proteins. Genomics 16: 630-637, 1993.
138. Gibbs S, Lohman F, Teubel WT, van de Putte P, Backendorf C: Characterization of the human spr2 promoter: induction after UV irradiation or TPA treatment and regulation during differentiation of cultured primary keratinocytes. Nucl Acids Res 18: 4401-4407, 1990.
139. Backendorf C, Hohl D: A common origin for cornified envelope precursor proteins? Nature Genet 2: 91, 1992.
140. Volz A, Korge B, Compton J, Ziegler A, Steinert P, Mischke D: Physical mapping of a functional cluster of epidermal differentiation genes on chromosome 1q21. Genomics 18: 92-99, 1993.
141. Fujimoto W, Marvin K, George M, Celli G, Darwiche N, De Luca L, Jetten A: Expression of cornifin in squamous differentiating epithelial tissues, including psoriasis and retinoic acid-treated skin. J Invest Dermatol 101: 268-274, 1993.
142. Chang A, de Jongh G, Mier PD, van de Kerkhof PCM: Enzymatic quantification of polymorphonuclear leukocytes in normal and psoriatic skin following standardized injury. Clin Exp Dermatol 13: 62-66, 1988.
143. Chang A, Schalkwijk J, Happle R, van de Kerkhof PCM: Elastase-inhibiting activity in scaling skin disorders. Acta Dermatol Venereol (Stockh) 70: 147-151, 1990.
144. Wiedow O, Schroder J, Gregory H, Young JA, Christophers E: Elafin: an elastase specific inhibitor of human skin. Purification, characterization and complete amino acid sequence. J Biol Chem 265: 14791-14795, 1990.
145. Schalkwijk J, Chang A, Janssen P, de Jongh GJ, Mier PD: Skin-derived antileucoproteinases (SKALPs): characterization of two new elastase inhibitors from psoriatic epidermis. Br J Dermatol 122: 631-641, 1990.
146. Schalkwijk J, de Roo C, de Jongh GJ: Skin-derived antileukoproteinase (SKALP) an elastase inhibitor from human keratinocytes. Purification and biochemical properties. Biochim Biophys Acta 1096: 148-154, 1991.
147. Sallenave J-M, Ryle AP: Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor. Biol Chem Hoppe-Seyler 372: 13-21, 1991.
148. Molhuizen HOF, Alkemade HAC, Zeeuwen PLJM, de Jongh GJ, Wieringa B, Schalkwijk J: SKALP/Elafin: an elastase inhibitor from cultured human keratinocytes. Purification, cDNA sequence, and evidence for transglutaminase cross-linking. J Biol Chem 268: 12028-12032, 1993.
149. Tsunemi M, Kato H, Nishiuchi Y, Kumagaya S, Sakakibara S: Synthesis and structure-activity relationships of elafin, an elastase-specific inhibitor. Biochem Biophys Res Commun 185: 967-973, 1992.
150. Ying OL, Simon SR: Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin. Biochemistry 32: 1866-1874, 1993.
151. Wiedow O, Ludemann J, Utecht B: Elafin is a potent inhibitor of proteinase 3. Biochem Biophys Res Commun 174: 6-10, 1991.
152. Wiedow O, Ludemann J, Utecht B: In ANCA-associated Vasculitides: Immunological and Clinical Aspects. Edited by W.L. Gross. Plenum Press, New York, 1993, pp. 61-64.
153. Molhuizen HOF, Schalkwijk J: Structural, biochemical, and cell biological aspects of the serine proteinase inhibitor SKALP/Elafin/ESI. Biol Chem Hoppe-Seyler 376: 1-7, 1995.
154. Schalkwijk J, van Vlijmen IM, Alkemade JA, de Jongh GJ: Immunohistochemical localization of SKALP/elafin in psoriatic epidermis. J Invest Dermatol 100: 390-393, 1993.
155. van de Kerkhof PCM, Kuppens LHCM, van Vlijmen I, Schalkwijk J: Distribution of skin-derived antileucoproteases (SKALP) in the marginal zone of the spreading psoriatic lesion. Br J Dermatol 124: 10-12, 1991.
156. Nonomura K, Yamanishi K, Yasuno H, Nara K, Hirose S: Up-regulation of elafin/SKALP gene expression in psoriatic epidermis. J Invest Dermatol 103: 88-91, 1994.
157. Alkemade JAC, Molhuizen HOF, van Vlijmen-Willems IMJJ, van Haelst UJGM, Schalkwijk J: Differential expression of SKALP/elafin in human epidermal tumors. Am J Pathol 143: 1679-1687, 1993.
158. Alkemade JAC, Molhuizen HOF, Ponec M, Zeeuwen PLJM, de Jongh GJ, van Vlijmen-Willems IMJJ, van Erp PEJ, van de Kerkhof PCM, Schalkwijk J: SKALP/Elafin is an inducible proteinase inhibitor in human epidermal keratinocytes. J Cell Sci 107: 2335-2342, 1994.
159. Zhang M, Zou Z, Maass N, Sager R: Differential expression of elafin in human normal mammary epithelial cells and carcinoma is regulated at the transcriptional level. Cancer Res 55: 2537-2541, 1995.
160. Sallenave J-M, Marsden MD, Ryle AP: Isolation of elafin and elastase-specific inhibitor (ESI) from bronchial secretions. Evidence of sequence homology and immunological cross-reactivity. Biol Chem Hoppe-Seyler 373: 27-33, 1992.
161. Drenth J, Low BW, Richardson JS, Wright CS: The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core. J Biol Chem 255: 2652-2655, 1980.
162. Saheki T, Ito F, Hagiwara H, Saito Y, Kuroki J, Tachibana S, Hirose S: Primary structure of the human elafin precursor preproelafin deduced from the nucleotide sequence of its gene and the presence of unique repetitive sequences in the prosegment. Biochem Biophys Res Commun 185: 240-245, 1992.
163. Molhuizen HOF, Zeeuwen PLJM, Olde Weghuis D, Geurts van Kessel A, Schalkwijk J: Assignment of the human gene encoding the epidermal serine proteinase inhibitor SKALP (P13) to chromosome region 20q12-q13. Cytogenet Cell Genet 66: 129-131, 1994.
164. Fong D, Chan M-Y, Hsieh W-T: Gene mapping of human cathepsins and cystatins. Biomed Biochim Acta 50: 595-598, 1991.
165. Alkemade H, van de Kerkhof P, Schalkwijk J: Demonstration of skin-derived antileukoproteinase (SKALP) in urine of psoriatic patients. J Invest Dermatol 99: 3-7, 1992.
166. Streit V, Wiedow O, Bartels J, Christophers E: Antiprotease activity in urine of patients with inflammatory skin disorders. J Invest Dermatol 105: 562-566, 1995.
167. Alkemade HA, De Jongh GJ, Arnold WP, van de Kerkhof PC, Schalkwijk J: Levels of skin-derived antileukoproteinase (SKALP)/elafin in serum correlate with disease activity during treatment of severe psoriasis with cyclosporin A. J