Interactions between germ cells and extracellular matrix glycoproteins during migration and gonad assembly in the mouse embryo

被引:83
作者
GarciaCastro, MI
Anderson, R
Heasman, J
Wylie, C
机构
[1] UNIV MINNESOTA,SCH MED,INST HUMAN GENET,DEPT PEDIAT,MINNEAPOLIS,MN 55455
[2] UNIV MINNESOTA,SCH MED,INST HUMAN GENET,DEPT CELL BIOL & NEUROANAT,MINNEAPOLIS,MN 55455
[3] WELLCOME CRC INST DEV BIOL & CANC,CAMBRIDGE CB2 1QR,ENGLAND
基金
英国惠康基金;
关键词
D O I
10.1083/jcb.138.2.471
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cells are known to bind to individual extracellular matrix glycoproteins in a complex and poorly understood way, Overall strength of adhesion is thought to be mediated by a combinatorial mechanism, involving adhesion of a cell to a variety of binding sites on the target glycoproteins, During migration in embryos, cells must alter their overall adhesiveness to the substrate to allow locomotion, The mechanism by which this is accomplished is not well understood, During early development, the cells destined to form the gametes, the primordial germ cells (PGCs), migrate from the developing hind gut to the site where the gonad will form, We have used whole-mount immunocytochemistry to study the changing distribution of three extracellular matrix glycoproteins, collagen IV, fibronectin, and laminin, during PGC migration and correlated this with quantitative assays of adhesiveness of PGCs to each of these, We show that PGCs change their strength of adhesion to each glycoprotein differentially during these stages, Furthermore, we show that PGCs interact with a discrete tract of laminin at the end of migration, Closer analysis of the adhesion of PGCs to laminin revealed that PGCs adhere particularly strongly to the E3 domain of laminin, and blocking experiments in vitro suggest that they adhere to this domain using a cell surface proteoglycan.
引用
收藏
页码:471 / 480
页数:10
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