| Sequence and expression of human hair keratin genes. | |
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MedLine Citation:
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PMID: 7528047 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Normal hair growth and differentiation requires co-ordinate expression of many hair specific structural protein genes. It has been established that one of the 4 major groups of hair structural proteins, low-sulphur hair keratins, belongs to the intermediate filament (IF) multigene family. Hair keratin IF proteins differ from those of other epithelia as they contain cysteine-rich terminal domains allowing more extensive disulphide bonding to the high-sulphur hair matrix proteins. Until recently, little information concerning the primary sequence of hair keratins was available but cloning of some mouse hair and sheep wool keratins has now been reported. Using these sequences, we have polymerase chain reaction (PCR) amplified genomic fragments of human hair-specific keratin IF genes and isolated cosmid clones containing full length genes. We have sequenced part of these genes and studied their expression in human hair follicles. Hair specific keratin fragments were amplified from placental gDNA by PCR primed with synthetic oligonucleotides. Fragments were cloned and sequenced after ligation into pGEM-3Z and labelled riboprobes were generated for in situ hybridization on human skin sections. A human cosmid library was screened with PCR fragments and clones encoding human hair keratin genes were characterised by southern hybridization and sequencing. The type I human hair-specific keratin clones obtained (HaKA1-b2, 386 bp; hHaKA1-XH1, 1202 bp) encoded 2B helix, C-terminal and 3'nc regions and were 65% homologous to mouse sequences. The type II hair keratin clone (hHaKB2-1, 829 bp) also encoded 2B helix and C-terminal regions and was 95% homologous to mouse. In situ hybridization on human skin sections showed a specific reaction with precortical cells of the hair follicle. One human cosmid clone, isolated with the hHaKB2-1 probe, contained two type II hair keratin genes about 7 kb apart, each of which had 9 exons spanning approximately 6 kb. The coding sequences were homologous to mouse cDNA (77-88%). These human hair-specific keratin clones are useful molecular tools for studies of hair differentiation. |
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Authors:
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P E Bowden; S Hainey; G Parker; M B Hodgins |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of dermatological science Volume: 7 Suppl ISSN: 0923-1811 ISO Abbreviation: J. Dermatol. Sci. Publication Date: 1994 Jul |
Date Detail:
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Created Date: 1995-01-24 Completed Date: 1995-01-24 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 9011485 Medline TA: J Dermatol Sci Country: IRELAND |
Other Details:
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Languages: eng Pagination: S152-63 Citation Subset: IM |
Affiliation:
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Department of Dermatology, University of Wales College of Medicine, Heath Park, Cardiff, UK. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/S75796; S75797 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Base Sequence Cloning, Molecular Cosmids DNA / genetics Gene Expression Hair / growth & development, metabolism* Humans In Situ Hybridization Keratins / chemistry, classification, genetics* Mice Molecular Sequence Data Molecular Structure Polymerase Chain Reaction Sequence Homology, Amino Acid Sheep Species Specificity |
| Chemical | |
Reg. No./Substance:
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68238-35-7/Keratins; 9007-49-2/DNA |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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