Purified mouse egg zona pellucida glycoproteins polymerize into homomeric fibrils under non-denaturing conditions

2007 ◽  
Vol 214 (1) ◽  
pp. 153-157 ◽  
Author(s):  
Eveline S. Litscher ◽  
William G. Janssen ◽  
Costel C. Darie ◽  
Paul M. Wassarman
Keyword(s):  
PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0129907 ◽  
Author(s):  
Nathan Egge ◽  
Archana Muthusubramanian ◽  
Gail A. Cornwall
Keyword(s):  

1988 ◽  
Vol 128 (2) ◽  
pp. 376-385 ◽  
Author(s):  
Jeffrey D. Bleil ◽  
Jeffrey M. Greve ◽  
Paul M. Wassarman

1984 ◽  
Vol 98 (3) ◽  
pp. 795-800 ◽  
Author(s):  
I J East ◽  
J Dean

Three sulfated glycoproteins (ZP-1, ZP-2, and ZP-3) make up the zona pellucida, an extracellular glycocalyx that surrounds mouse oocytes. We have produced five monoclonal antibodies specific to the zona. All five immunoprecipitated ZP-2, and in addition, two of the antibodies immunoprecipitated ZP-3. This suggests the presence of either a common antigenic site or one made up in part by each of the two glycoproteins. The monoclonal antibodies bound to approximately 1.3 X 10(8) binding sites per ovulated mouse egg which represents 2% of the total number of ZP-2 molecules present in the zona. ZP-2 appeared to be present throughout the zona and indirect immunofluorescence revealed a fibrous pattern with no evidence of localization. Furthermore, this pattern of distribution, which was identical for all five monoclones, remained constant after fertilization at the two-cell embryo stage. Laser photobleaching demonstrated that ZP-2 is stably integrated in the extracellular matrix of the zona pellucida. No mouse tissue other than the ovary contained ZP-2 and ZP-2 is antigenically distinct from other previously described extracellular matrix proteins.


2012 ◽  
Vol 56 (10-11-12) ◽  
pp. 833-839 ◽  
Author(s):  
Paul M. Wassarman ◽  
Eveline S. Litscher
Keyword(s):  

1989 ◽  
pp. 18-37 ◽  
Author(s):  
P. Wassarman ◽  
J. Bleil ◽  
C. Fimiani ◽  
H. Florman ◽  
J. Greve ◽  
...  
Keyword(s):  

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