Altered proteoglycan synthesis disrupts feather pattern formation in chick embryonic skin.

Abstract:

:We have tested the role of proteoglycans in the development of feather pattern by culturing 7-day-old embryonic chick skins on medium containing para-nitrophenyl-beta-D-xyloside (2 mM). Xylosides compete with core proteins of proteoglycans by acting as exogenous acceptors for the synthesis of glycosaminoglycans leading to the synthesis of under- or unglycosylated core proteins and free glycosaminoglycans. We have demonstrated that xyloside treatment alters the structure of the proteoglycans synthesized by embryonic skin and disrupts the feather pattern. The altered pattern is seen as the fusion of individual feather rudiments. Fusion can occur diagonally, and in an anteroposterior and mediolateral direction. The effect induced by the disruption of proteoglycan structure takes place during the first 24 hr of culture during which time all the rows of feather rudiments are being established. The effect is reversible if the skins are returned to control medium after 24 hr but not after 48 hr of treatment with xyloside. Once established during the first 24 hr the feather pattern can only be slightly distorted by the xyloside treatment. The results are interpreted to mean that proteoglycans play a developmental role in the establishment of the feather pattern but not in its maintenance, suggesting that the two processes are under different developmental control. The altered feather pattern obtained by disrupting proteoglycan structure is highly similar to that obtained when skins are cultured in the presence of antibodies to L-CAM (W.J. Gallin, C.-M., Chuong, L.H. Finkel, and G.M. Edelman (1986), Proc. Natl. Acad. Sci. USA 83, 8235-8239). This observation suggests that there may be a functional relationship between the extracellular matrix and cell adhesion molecules in the establishment of feather pattern.

journal_name

Dev Biol

journal_title

Developmental biology

authors

Goetinck PF,Carlone DL

doi

10.1016/0012-1606(88)90199-6

subject

Has Abstract

pub_date

1988-05-01 00:00:00

pages

179-86

issue

1

eissn

0012-1606

issn

1095-564X

pii

0012-1606(88)90199-6

journal_volume

127

pub_type

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