Human hair production by scalp samples grafted onto nude mice. Biochemical data on normal human hair and the genetic defect trichothiodystrophy. 1994

B de Brouwer, and J Föhles, and D J Van Neste
Skin Study Center, Skinterface sprl, Tournai, Belgium.

The authors report on a laboratory model for continuous production of human hair during long periods of time. This study shows that the amino acid composition of hairs collected in situ from human scalp was similar to that of terminal hairs produced by the donors' scalp follicles grafted and maintained onto nude mice. A similar experiment was performed with scalp samples from a foetus with trichothiodystrophy (TTD). The amino acid analysis of TTD lanugo hairs and of the TTD shafts produced by grafted scalp specimens was consistent with findings published in the literature: severe decrease of cys (< 50% of control values) and moderate decrease of thr and pro (80% of control values or less) with an increase of ala-asp-ile-leu-lys-met-phe (120% of control values or more). These changes indicate a decrease of high sulphur proteins (HSP) and consequently a relative increase of keratins. Furthermore, when foetal scalp samples were grafted, the lanugo hairs transformed into terminal hairs along with normal initiation of melanisation. Hence, keratin and HSP gene expression and regulation of melanogenesis in the normal and genetically defective TTD human hair follicle grafts appear to be independent of systemic host-related factors, at least during a 6 months follow-up period after grafting. The present experimental evidence further supports conclusions gained from previous assays with normal and TTD variant scalp grafts, i.e. that the nude mouse bearing human scalp specimens may serve as a clinically relevant laboratory model for evaluating regulation of normal and abnormal gene expression in the hair follicle under well controlled experimental conditions.

UI MeSH Term Description Entries
D007633 Keratins A class of fibrous proteins or scleroproteins that represents the principal constituent of EPIDERMIS; HAIR; NAILS; horny tissues, and the organic matrix of tooth ENAMEL. Two major conformational groups have been characterized, alpha-keratin, whose peptide backbone forms a coiled-coil alpha helical structure consisting of TYPE I KERATIN and a TYPE II KERATIN, and beta-keratin, whose backbone forms a zigzag or pleated sheet structure. alpha-Keratins have been classified into at least 20 subtypes. In addition multiple isoforms of subtypes have been found which may be due to GENE DUPLICATION. Cytokeratin,Keratin Associated Protein,Keratin,Keratin-Associated Proteins,alpha-Keratin,Associated Protein, Keratin,Keratin Associated Proteins,Protein, Keratin Associated,alpha Keratin
D008297 Male Males
D008819 Mice, Nude Mutant mice homozygous for the recessive gene "nude" which fail to develop a thymus. They are useful in tumor studies and studies on immune responses. Athymic Mice,Mice, Athymic,Nude Mice,Mouse, Athymic,Mouse, Nude,Athymic Mouse,Nude Mouse
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D005260 Female Females
D006197 Hair A filament-like structure consisting of a shaft which projects to the surface of the SKIN from a root which is softer than the shaft and lodges in the cavity of a HAIR FOLLICLE. It is found on most surfaces of the body. Fetal Hair,Hair, Fetal,Lanugo,Fetal Hairs,Hairs,Hairs, Fetal
D006201 Hair Diseases Diseases affecting the orderly growth and persistence of hair. Hair Disease
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

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