M. Pines et al., DEVELOPMENTAL-CHANGES IN SKIN COLLAGEN BIOSYNTHESIS PATHWAY IN POSTHATCH MALE AND FEMALE CHICKENS, Poultry science, 75(4), 1996, pp. 484-490
The developmental changes in skin collagen biosynthesis pathway in mal
e and female chickens were evaluated. Concentration of collagen, level
s of mRNA for collagen type I subunits and for lysyl hydroxylase, and
the level of three lysyl oxidase-derived cross-links: dehydro-dihydrox
ylysinonorleucine (DHLNL), dehydro-hydroxylysinonorleucine (HLNL), and
dehydro-histidinohydroxymerodesmosine (HHMD) were determined during 4
wk posthatching. Skin collagen content increased with age and was hig
her in males than in females. In both sexes, the expression of the gen
es coding for alpha 1 and alpha 2 of collagen type I decreased with ag
e: alpha 1 (I) gene expression decreased from Day 3 onwards, whereas t
he reduction in alpha 2(I) gene expression started 1 wk later. At all
ages examined, the expression of both genes was higher in male than in
female skin, Males and females lysyl hydroxylase gene expression rema
ined low until Day 16, after which an increase in the enzyme gene expr
ession was observed. An increase in skin HLNL content was observed fro
m Day 3 in both sexes reaching a peak in males at Day 9 and in females
1 wk later. The DHLNL content, which was higher in males than in fema
les at all ages tested, dramatically decreased in both male and female
skin from 3 d of age, reaching its lowest level at Day 16, and remain
ed at that low level thereafter. The skin content of HHMD in males and
females followed an oscillatory behavior with higher peaks in the mal
e skin. The results suggest that the higher tensile strength of male s
kin than female skin may be due to the elevated skin collagen content
that resulted from increased expression in collagen type I genes on th
e one hand, and from the higher amounts of various collagen cross-link
s on the other.