Investigation of structural proteins in human hair defects using anagen follicles.
An alternative to using hair specimens for the study of inherited hair shaft defects has been to explore protein compositions in the context of hair formation. Hair follicles were obtained from patients with a hair disorder and the presumptive hair shaft (PHS) separated by microdissection for protein solubilization and electrophoretic experiments aimed at providing a new basis to help explain the mechanism of hair shaft defects. Two-dimensional electrophoresis (fluorographs) of labelled extracts was used to examine the major hair structural proteins and other polypeptide(s) found associated with PHS extracts in normal and aberrant specimens. Changes in either the intermediate filaments (IFs) or matrix polypeptides were not normally found in defective PHS specimens. The polypeptides showing greatest variation were associated with a PHS-specific component which was recently found in normal specimens. The variation in this polypeptide was manifested as multiple spots of different molecular weights. An investigation of the role of PHS-associated polypeptides as a likely part of the hair cross-linking mechanisms, involved examination of a PHS extract from a Menkes' patient. The observations suggest that formation of hair fibre shaft defects may be related to the status of PHS-associated polypeptides which could in turn be influenced by the presence of copper in the hair follicle.
Jones
L N
LN
Department of Medical Biophysics, Karolinska Institute, Stockholm, Sweden.
D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006201:Hair Diseases / Q000235:genetics / Q000378:metabolism; D018859:Hair Follicle / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007633:Keratins / Q000032:analysis* / Q000737:chemistry; D008297:Male; D010375:Pedigree
D007633:Keratins