Structure of the cumulus matrix and zona pellucida in the golden hamster: A new view of sperm interaction with oocyte-associated extracellular matrices

1988 ◽  
Vol 251 (3) ◽  
pp. 555-564 ◽  
Author(s):  
AshleyI. Yudin ◽  
GaryN. Cherr ◽  
DavidF. Katz
Author(s):  
Jennifer D. Cohen ◽  
Jessica G. Bermudez ◽  
Matthew C. Good ◽  
Meera V. Sundaram

AbstractZona Pellucida domain (ZP) proteins are critical components of the body’s external-most protective layers, apical extracellular matrices (aECMs). Although their loss or dysfunction is associated with many diseases, it remains unclear how ZP proteins assemble in aECMs. Current models suggest that ZP proteins polymerize via their ZPn subdomains, while ZPc subdomains modulate ZPn behavior. Using the model organism C. elegans, we investigated the aECM assembly of one ZP protein, LET-653, which shapes several tubes. Contrary to prevailing models, we find that LET-653 localizes and functions via its ZPc domain. Furthermore, the ZPc domain is inhibited by the ZPn domain and cleavage of the LET-653 C-terminus relieves this inhibition. In vitro, the ZPc, but not ZPn, domain formed crystalline aggregates. These data offer a new model for ZP function whereby the ZPc domain is primarily responsible for matrix incorporation and tissue shaping.


PLoS Genetics ◽  
2020 ◽  
Vol 16 (11) ◽  
pp. e1009188
Author(s):  
Jennifer D. Cohen ◽  
Jessica G. Bermudez ◽  
Matthew C. Good ◽  
Meera V. Sundaram

Zona Pellucida domain (ZP) proteins are critical components of the body’s external-most protective layers, apical extracellular matrices (aECMs). Although their loss or dysfunction is associated with many diseases, it remains unclear how ZP proteins assemble in aECMs. Current models suggest that ZP proteins polymerize via their ZPn subdomains, while ZPc subdomains modulate ZPn behavior. Using the model organism C. elegans, we investigated the aECM assembly of one ZP protein, LET-653, which shapes several tubes. Contrary to prevailing models, we find that LET-653 localizes and functions via its ZPc domain. Furthermore, we show that ZPc domain function requires cleavage at the LET-653 C-terminus, likely in part to relieve inhibition of the ZPc by the ZPn domain, but also to promote some other aspect of ZPc domain function. In vitro, the ZPc, but not ZPn, domain bound crystalline aggregates. These data offer a new model for ZP function whereby the ZPc domain is primarily responsible for matrix incorporation and tissue shaping.


Development ◽  
1968 ◽  
Vol 19 (3) ◽  
pp. 341-345
Author(s):  
M. P. Young ◽  
J. T. Whicher ◽  
D. M. Potts

Previous work on the early development of the golden hamster includes the investigation of Ochs (1908), Graves (1945) and Ward (1948), all at the level of the light microscope. Austin (1963) has examined the ultrastructure of the oocytes of the golden hamster while Enders & Schlafke (1965) have observed the pre-implantation stages of pregnancy. The ultrastructure of implantation has been studied in two other species of myomorph rodents: the mouse (Potts, 1966a; Reinius, 1967) and the rat (Enders & Schlafke, 1967). Implantation is taken as beginning when the zona pellucida is lost and the trophoblast is in contact with the uterine epithelium throughout its circumference. This takes place at between 80–100 h post coitum. Previous studies have been made on specimens embedded in paraffin, and the shrinkage which occurs with this method of preservation has caused implantation to appear to begin considerably later than this:Graves (1945) gives it as beginning at 5 days, Ward(1948) as 4 days 8 h.


1987 ◽  
Vol 11 (3) ◽  
pp. 193-208 ◽  
Author(s):  
Yoshihiko Araki ◽  
Shoichiro Kurata ◽  
Taneaki Oikawa ◽  
Takao Yamashita ◽  
Masahiko Hiroi ◽  
...  

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