caa a22 4500 397568185 CHVBK 20180308164833.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.3382/ps.0750484 doi (NATIONALLICENCE)oxford-10.3382/ps.0750484 Developmental Changes in Skin Collagen Biosynthesis Pathway in Posthatch Male and Female Chickens [Elektronische Daten] [M. PINES, M. SCHICKLER, S. HURWITZ, M. YAMAUCHI] The developmental changes in skin collagen biosynthesis pathway in male and female chickens were evaluated. Concentration of collagen, levels of mRNA for collagen type I subunits and for lysyl hydroxylase, and the level of three lysyl oxidase-derived cross-links: dehydro-dihydroxylysinonorleucine (DHLNL), dehydro-hydroxylysinonorleucine (HLNL), and dehydro-histidinohydroxymerodesmosine (HHMD) were determined during 4 wk posthatching. Skin collagen content increased with age and was higher in males than in females. In both sexes, the expression of the genes coding for α1 and α2 of collagen type I decreased with age: α1 (I) gene expression decreased from Day 3 onwards, whereas the reduction in α2(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 remained low until Day 16, after which an increase in the enzyme gene expression was observed. An increase in skin HLNL content was observed from 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 females 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 remained at that low level thereafter. The skin content of HHMD in males and females followed an oscillatory behavior with higher peaks in the male skin. The results suggest that the higher tensile strength of male skin than female skin may be due to the elevated skin collagen content that resulted from increased expression in collagen type I genes on the one hand, and from the higher amounts of various collagen cross-links on the other. © 1996 Poultry Science Association, Inc. Metabolism and Nutrition nationallicence broiler chick nationallicence collagen type I nationallicence lysyl hydroxylase nationallicence cross-linking nationallicence skin nationallicence PINES M. Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel aut SCHICKLER M. Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel aut HURWITZ S. Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel aut YAMAUCHI M. Dental Research Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27514-7455 aut Poultry Science Oxford University Press 75/4(1996-04), 484-490 0032-5791 75:4<484 1996 75 ps https://doi.org/10.3382/ps.0750484 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.3382/ps.0750484 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- PINES M. Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel aut NATIONALLICENCE 700 1- SCHICKLER M. Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel aut NATIONALLICENCE 700 1- HURWITZ S. Institute of Animal Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel aut NATIONALLICENCE 700 1- YAMAUCHI M. Dental Research Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27514-7455 aut NATIONALLICENCE 773 0- Poultry Science Oxford University Press 75/4(1996-04), 484-490 0032-5791 75:4<484 1996 75 ps Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford