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Research paper| Volume 14, ISSUE 1, P1-11, January 1997

Isolation and characterization of genomic clones of human sequences presumably coding for hair cysteine-rich proteins

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      Abstract

      The major biochemical components of the mammalian hair are the intermediate filaments or keratins and the keratin associated proteins. Keratin associated proteins are classified into two groups (high-cysteine and high glycine-tyrosine-rich polypeptides) according to the content of these amino acids. Cysteine-rich group contains high sulphur (16–24% cysteine) and ultra-high sulphur (> 30% cysteine) proteins. We report here the identification of a human sequence presumably coding for a new ultra-high sulphur protein (hUHSp21) and the isolation and characterization of four genomic clones containing six related sequences. We also discuss the possibility that all the genes encoding keratin associated proteins are evolutionary related. These human clones should provide useful molecular tools for studies of hair differentiation and understanding of the molecular basis of human trichothiodystrophy.

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      References

        • Powell BC
        • Nesci A
        • Rogers GE
        Regulation of keratin gene expression in hair follicle differentiation.
        Ann NY Acad Sci. 1991; 642: 1-20
        • Marshall RC
        • Orwin DFG
        • Gillespie JM
        Structure and biochemistry of mammalian hard keratin.
        Electron Microsc Rev. 1991; 4: 47-83
        • Rogers GE
        • Fietz MJ
        • Fratini A
        Trichohyalin and matrix proteins.
        Ann NY Acad Sci. 1991; 642: 64-81
        • 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. 1993; 121: 855-865
        • Powell BC
        • Sleigh MJ
        • Ward KA
        • Rogers GE
        Mammalian keratin gene families: organisation of genes coding for the B2 high-sulphur proteins of sheep wool.
        Nucl Acids Res. 1983; 11: 5327-5346
        • Frenkel MJ
        • Powell BC
        • Ward KA
        • Sleigh MJ
        • Rogers GE
        The keratin BIIIB gene family: isolation of cDNA clones and structure of a gene and a related pseudogene.
        Genomics. 1989; 4: 182-191
        • Fratini A
        • Powell BC
        • Hynd PI
        • Keough RA
        • Rogers GE
        Dietary cysteine regulates the levels of mRNAs encoding a family of cysteine-rich proteins of wool.
        J Invest Dermatol. 1994; 102: 178-185
        • Zhumbaeva BD
        • Gening LV
        • Gazarian KG
        Cloning and structural characteristics of human hair keratin genes rich in sulfur.
        Mol Biol (Mosk). 1992; 26: 813-820
        • McNab AR
        • Wood L
        • Theriault N
        • Gierman T
        • Vogeli G
        An ultra-high sulfur keratin gene is expressed specifically during hair growth.
        J Invest Dermatol. 1989; 92: 263-266
        • Wood L
        • Mills M
        • Hatzenbuhler N
        • Vogeli G
        Serine-rich ultra high sulfur protein gene expression in murine hair and skin during the hair cycle.
        J Biol Chem. 1990; 265: 21375-21380
        • MacKinnon PJ
        • Powell BC
        • Rogers GE
        Structure and expression of genes for a class of cystein-rich proteins of the cuticle layers of differentiating wool and hair follicles.
        J Cell Biol. 1990; 111: 2587-2600
        • Jenkins BJ
        • Powell BC
        Differential expression of genes encoding a cysteine-rich keratin family in the hair cuticle.
        J Invest Dermatol. 1994; 103: 310-317
        • Fratini A
        • Powell BC
        • Rogers GE
        Sequence, expression and evolutionary conservation of a gene encoding a glycine/tyrosine-rich keratin-associated protein of hair.
        J Biol Chem. 1993; 268: 4511-4518
        • Kuczek ES
        • Rogers GE
        Sheep wool glycine +tyrosine-rich keratin genes: a family of low sequence homology.
        Eur J Biochem. 1987; 166: 79-85
        • MacKinnon PJ
        • Powell BC
        • Rogers GE
        • Baker EG
        • MacKinnon RN
        • Hyland VJ
        • Callen DF
        • Sutherland GR
        An ultrahigh-sulphur keratin gene of the human hair cuticle is located at 11q13 and cross-hybridizes with sequences at 11p15.
        Mammalian Genome. 1991; 1: 53-56
        • Price VH
        • Odom RB
        • Ward WH
        • Jones FT
        Trichothiodystrophy: Sulfur-deficient brittle hair as a marker for a neurectodermal symptom complex.
        Arch Dermatol. 1980; 116: 1375-1384
        • Gillepsie JM
        • Marshall RC
        A comparison of the proteins of normal and trichothiodystrophic human hair.
        J Invest Dermatol. 1983; 80: 195-202
        • Sambrook J
        • Fritsh EF
        • Maniatis T
        2nd ed. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New-York1989
        • Huh N
        • Kashiwagi M
        • Konishi C
        • Hashimoto Y
        • Kohno Y
        • Nomura S
        • Kuroki T
        Isolation and characterization of a novel hair-follicle-specific gene, hacl-1.
        J Invest Dermatol. 1994; 102: 716-720
        • Rogers GE
        • Powell BC
        Organization and expression of hair follicle genes.
        J Invest Dermatol (suppl). 1993; 101: 50S-55S