Response to fibronectin of mouse primordial germ cells before, during and after migration

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.

Development ◽  
1991 ◽  
Vol 113 (4) ◽  
pp. 1451-1457 ◽  
Author(s):  
I. Godin ◽  
C.C. Wylie

Primordial germ cells are the stem cells that provide the functional gametes of adult animals. In many animal groups they are set aside at the earliest stages of development, and migrate from their sites of first appearance to the sites where the gonad will form, the genital ridges. During this migration they proliferate. In the mouse embryo their numbers increase from less than one hundred to approximately four thousand during the period of their migration. In a previous paper we showed that both the proliferation and the direction of migration of mouse PGCs in culture were influenced by soluble factors released from their target tissue, the genital ridges. Studies on other stem cell populations have shown that complex combinations of growth factors control their proliferation, migration and differentiation. In this paper, we show that TGF beta 1 inhibits proliferation of PGCs taken from 8.5 day old embryos and cultured on embryonic fibroblast feeder layers. We also show that the previously reported chemotropic effect of genital ridges in this culture system is mediated by TGF beta 1, or a closely related molecule, released from the genital ridges.


Development ◽  
1990 ◽  
Vol 109 (4) ◽  
pp. 911-923 ◽  
Author(s):  
A. Orr-Urtreger ◽  
A. Avivi ◽  
Y. Zimmer ◽  
D. Givol ◽  
Y. Yarden ◽  
...  

Developmental expression of the c-kit proto-oncogene, a receptor tyrosine kinase encoded by the W locus, was investigated by in situ hybridization in normal mouse embryos. Early after implantation transcripts were detectable only in the maternal placenta (6 1/2-7 1/2 days p.c.). Subsequently (8 1/2 days p.c.) numerous ectodermal (neural tube, sensory placodes) and endodermal (embryonic gut) derivatives expressed c-kit. Later transcripts were detected also in the blood islands of the yolk sac and in the embryonic liver, the main sites of embryonic hemopoiesis. Around midgestation, transcripts accumulated in the branchial pouches and also in primordial germ cells of the genital ridges. This complex pattern of expression remained characteristic also later in gestation, when c-kit was expressed in highly differentiated structures of the craniofacial area, in presumptive melanoblasts and in the CNS. In the adult ovary, maternal c-kit transcripts were detected. They were present in the oocytes of both immature and mature ovarian follicles, but not in the male germ line, where c-kit expression may be down regulated. Thus, c-kit activity is complex and appears in multiple tissues including those that also display defects in mutations at the W locus where c-kit is encoded. Correlation between W phenotypes and c-kit expression, as well as the regulation of the complex and multiple expression of polypeptide growth factors and receptors, is discussed.


Biologicals ◽  
2017 ◽  
Vol 48 ◽  
pp. 114-120 ◽  
Author(s):  
Vahid Mansouri ◽  
Mohammad Salehi ◽  
Mir davood Omrani ◽  
Zahra Niknam ◽  
Abdolreza Ardeshirylajimi

Zoo Biology ◽  
2002 ◽  
Vol 21 (3) ◽  
pp. 287-294 ◽  
Author(s):  
Takaharu Kawashima ◽  
Rika Sakai ◽  
Koichiro Kano ◽  
Yoshinori Tamaki ◽  
Koichiro Hashimoto

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.


1989 ◽  
Vol 224 (1) ◽  
pp. 14-21 ◽  
Author(s):  
Lance E. Urven ◽  
Ursula K. Abbott ◽  
Carol A. Erickson

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