Hynd, 1996  Title: Inhibition of polyamine synthesis alters
hair follicle function and fiber composition.
Authors: Hynd PI, Nancarrow MJ
Journal:J Invest Dermatol 1996 Feb;106(2):249-53
PMID: 8601724, UI: 96179736
Affiliated institution: Department
of Animal Science, University of Adelaide Waite Campus, Glen Osmond,
South Australia, Australia.
Cited in:
The activities of ornithine decarboxylase and S-adenosylmethionine
decarboxylase, two of the enzymes involved in the synthesis of
the polyamines, were found to be high in follicle-rich homogenates
of sheep skin, and to be responsive to the nutrition of the animal.
Systemic provision of the inhibitor of ornithine decarboxylase,
alpha difluoromethylornithine, markedly altered the length, diameter,
and composition of the fiber, the last being accompanied by an
increase in the proportion of the fiber occupied by paracortical
cells and an increase in the level of mRNA encoding a cysteine-rich
family of keratin proteins. The growth of wool follicles cultured
in media containing alpha-difluoromethylornithine was not inhibited,
even at high concentrations. In contrast, low concentrations of
methylglyoxal (bis)guanylhydrazone, the inhibitor of S-adenosylmethionine
decarboxylase, completely inhibited fiber growth in culture follicles.
Addition of spermidine to the media overcame this inhibition but
spermine had no effect. Further evidence that spermine is not
required for normal follicle function was provided by incubating
follicles with the specific inhibitor of spermine synthase, n-butyl-1,3-diaminopropane.
This inhibitor, even at high concentrations, had no effect on
fiber growth in vitro. Spermidine partially overcame the growth
depression that occurred in follicles cultured in methionine-deficient
media, suggesting that part of the requirement for methionine
is for spermidine synthesis in the follicle. These investigations
provide strong evidence that the polyamines in general , and spermidine
in particular, play a major role in hair growth.
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