Distribution of extracellular matrix in the migratory pathway of avian primordial germ cells

1989 ◽  
Vol 224 (1) ◽  
pp. 14-21 ◽  
Author(s):  
Lance E. Urven ◽  
Ursula K. Abbott ◽  
Carol A. Erickson
1997 ◽  
Vol 138 (2) ◽  
pp. 471-480 ◽  
Author(s):  
Martín I. García-Castro ◽  
Robert Anderson ◽  
Janet Heasman ◽  
Christopher Wylie

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.


2002 ◽  
Vol 117 (3) ◽  
pp. 265-273 ◽  
Author(s):  
Mauricio Soto-Suazo ◽  
Paulo A. Abrahamsohn ◽  
Jaime Pereda ◽  
Sebastian San Martin ◽  
Helena B. Nader ◽  
...  

1985 ◽  
Vol 211 (3) ◽  
pp. 271-278 ◽  
Author(s):  
Toyoaki Fujimoto ◽  
Kazuya Yoshinaga ◽  
Ichiro Kono

Development ◽  
1991 ◽  
Vol 113 (4) ◽  
pp. 1365-1373 ◽  
Author(s):  
C. Ffrench-Constant ◽  
A. Hollingsworth ◽  
J. Heasman ◽  
C.C. Wylie

The adhesive extracellular matrix glycoprotein fibronectin is thought to play a central role in cell migration during embryogenesis. In order to define this role, we have examined the response to fibronectin in cell culture of mouse primordial germ cells (PGCs) before, during and after their migration from the hindgut into their target tissue, the genital ridges. Using an explant culture system, we show that PGCs will emigrate from tissue fragments containing hindgut, and that fibronectin stimulates this migration. Adhesion assays show that the start of PGC migration is associated with a fall in adhesion to fibronectin. Double-labelling studies using in situ hybridization and histochemistry demonstrate that migrating PGCs do not contain detectable fibronectin mRNA, suggesting that they do not synthesize and secrete the fibronectin within their migratory substratum. Taken together, these findings are consistent with an important role for fibronectin in stimulating PGC migration. In addition, however, they suggest that the interaction between PGCs and fibronectin may be important in timing the start of migration, with the fall in adhesion allowing the PGCs to commence their migration towards the genital ridges.


Author(s):  
David J. Huss ◽  
Sasha Saias ◽  
Sevag Hamamah ◽  
Jennifer M. Singh ◽  
Jinhui Wang ◽  
...  

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