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

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....

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Bibliographic Details
Published in:Journal of dermatological science 1997, Vol.14 (1), p.1-11
Main Authors: Emonet, Nathalie, Michaille, Jean-Jacques, Dhouailly, Danielle
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Animals
Base Sequence
Cloning, Molecular
Cysteine-rich gene
DNA - genetics
Hair - chemistry
HSp
Human genomic clones
Humans
Keratin-associated protein
Keratins - chemistry
Keratins - genetics
Molecular Sequence Data
Nuclear Proteins
Oligonucleotide Probes - genetics
Proteins - chemistry
Proteins - genetics
Proto-Oncogene Proteins c-myc - chemistry
Proto-Oncogene Proteins c-myc - genetics
Repetitive Sequences, Nucleic Acid
Restriction Mapping
UHSp
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Summary: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.
ISSN:0923-1811
1873-569X
DOI:10.1016/S0923-1811(96)00541-5