Hair fibre production by human hair follicles in whole-organ culture.

Abstract

We have used both pulse-chase radiolabelling and morphometric techniques to investigate the ability of whole-organ cultures of human hair follicles to synthesize hair fibre. Anagen hair follicles were obtained from human facial skin by microdissection. Follicles were pulse-labelled with 3H-leucine, and radioactivity in alkali-soluble protein (ASP) and alkali-insoluble hair fibre protein (HFP) fractions was determined by differential extraction. There was a slow decline in ASP radioactivity over 7 days of culture, with a half-life of 4 days. In contrast, leucine incorporation into HFP increased linearly from day 1 to day 5, following an initial delay of 17 h. Morphometric analysis revealed that hair follicles and hair fibres grew at the same rate (0.25 mm/day) for 4 days in culture, after which the rate of hair follicle growth declined progressively, whereas fibre growth continued at the initial rate for a further 3 days. Concurrent with the onset of the decline in follicle growth, the base of the hair fibre began to descend towards the follicle base, until hair fibre occupied almost the full length of the hair follicle at day 15. The decline in follicle growth was preceded by a decline in the rate of follicular 3H-thymidine incorporation, with a delay of approximately 1 day. Overall, these data demonstrate that human hair follicles in whole-organ culture are capable of the production of hair fibre, and suggest that cessation of hair growth in vitro results from depletion of the pool of differentiated follicular keratinocytes, secondary to a loss of matrix cell proliferative activity.