scholarly journals Localized surface antigens of guinea pig sperm migrate to new regions prior to fertilization.

1984 ◽  
Vol 99 (5) ◽  
pp. 1634-1641 ◽  
Author(s):  
D G Myles ◽  
P Primakoff

We have previously defined distinct localizations of antigens on the surface of the guinea pig sperm using monoclonal antibodies. In the present study we have demonstrated that these antigen localizations are dynamic and can be altered during changes in the functional state of the sperm. Before the sperm is capable of fertilizing the egg, it must undergo capacitation and an exocytic event, the acrosome reaction. Prior to capacitation, the antigen recognized by the monoclonal antibody, PT-1, was restricted to the posterior tail region (principle piece and end piece). After incubation in capacitating media at 37 degrees C for 1 h, 100% of the sperm population showed migration of the PT-1 antigen onto the anterior tail. This redistribution of surface antigen resulted from a migration of the surface molecules originally present on the posterior tail. It did not occur in the presence of metabolic poisons or when tail-beating was prevented. It was temperature-dependent, and did not require exogenous Ca2+. Since the PT-1 antigen is freely diffusing on the posterior tail before migration, the mechanism of redistribution could involve the alteration of a presumptive membrane barrier. In addition, we observed the redistribution of a second surface antigen after the acrosome reaction. The antigen recognized by the monoclonal antibody, PH-20, was localized exclusively in the posterior head region of acrosome-intact sperm. Within 7-10 min of induction of the acrosome reaction with Ca2+ and A23187, 90-100% of the acrosome-reacted sperm population no longer demonstrated binding of the PH-20 antibody on the posterior head, but showed binding instead on the inner acrosomal membrane. This redistribution of the PH-20 antigen also resulted from the migration of pre-existing surface molecules, but did not appear to require energy. The migration of PH-20 antigen was a selective process; other antigens localized to the posterior head region did not leave the posterior head after the acrosome reaction. These rearrangements of cell surface molecules may act to regulate cell surface function during fertilization.

1981 ◽  
Vol 13 (6) ◽  
pp. 547-554 ◽  
Author(s):  
Shoji Kimura ◽  
Nobuhiko Tada ◽  
Yen Liu ◽  
Ulrich H�mmerling

Development ◽  
1983 ◽  
Vol 75 (1) ◽  
pp. 259-270
Author(s):  
Stephen J. Gaunt

The rat sperm surface antigen 2D6, located over the entire surface of the spermatozoon, is shown by use of a monoclonal antibody in indirect immunofluorescence experiments to spread laterally over the surface of the egg after fusion of sperm and egg plasma membranes at fertilization. Freshly fertilized eggs, obtained from superovulated rats 14h after hCG injection, showed the 2D6 antigen to have spread in a gradient over a discrete fan-shaped area of the egg surface anterior to the protruding sperm tail. Eggs at a later stage of sperm incorporation, obtained 20 h after hCG injection, snowed that the spread of antigen had extended to cover most or all of their surfaces. By 40 h after hCG injection, the approximate time that fertilized eggs cleaved to form 2-cell embryos, most of the 2D6 antigen had been lost from the cell surface. Fertilized eggs, but not unfertilized eggs or 2-cell embryos, were lysed by 2D6 monoclonal antibody in the presence of guinea pig complement. A model for sperm-egg fusion is presented to account for the observed pattern of spreading shown by the 2D6 antigen. The possible role of sperm antigens on the egg surface is discussed.


1978 ◽  
Vol 32 (1) ◽  
pp. 153-164
Author(s):  
D.P. Green

The divalent metal cation ionophore A23187 rapidly induces a normal acrosome reaction in a population of guinea-pig sperm suspended in calcium medium. In the course of the acrosome reaction, proacrosin, the zymogen precursor of the protease acrosin, is activated. Although the acrosome reaction causes exocytosis of the acrosomal contents, ‘soluble’ acrosin is not released in significant amounts until well after the sperm population as a whole has undergone an acrosome reaction. This suggests that proacrosin is stored within the acrosome in an insoluble form and that exocytosis of the acrosomal contents in the acrosome reaction is insufficient, by itself, to cause its immediate dissolution. Electron micrographs of sperm undergoing an A23187-induced acrosome reaction in the presence of the acrosin inhibitors benzamidine, p-amino-benzamidine and phenylmethylsulphonyl fluoride show that the acrosome reaction proceeds normally but that dispersal of the acrosomal contents is inhibited. These morphological changes are, for the most part, below the limit of resolution of the light microscope and using light microscopy to assess whether an acrosome reaction has taken place, it can be mistakenly inferred that the reaction itself is inhibited by the acrosin inhibitors. The inhibition of the dispersal of the acrosomal contents by acrosin inhibitors suggests that acrosin activity is important in solubilizing acrosin. These experimental observations, taken with the evidence that the acrosome reaction is a response to an increase in intracellular free calcium, have been taken as the basis of a proposal for the mechanism of proacrosin activation in the acrosome reaction.


1994 ◽  
Vol 9 (1) ◽  
pp. 47 ◽  
Author(s):  
Doo Hyun Chung ◽  
Young Mee Bae ◽  
Hee Young Shin ◽  
Hyo Seop Ahn ◽  
Hyung Geun Song ◽  
...  

2002 ◽  
Vol 30 (6) ◽  
pp. 537-545 ◽  
Author(s):  
Reiner Lammers ◽  
Christina Giesert ◽  
Frank Grünebach ◽  
Anke Marxer ◽  
Wichard Vogel ◽  
...  

1993 ◽  
Vol 11 (4) ◽  
pp. 738-750 ◽  
Author(s):  
E Oosterwijk ◽  
N H Bander ◽  
C R Divgi ◽  
S Welt ◽  
J C Wakka ◽  
...  

PURPOSE To define the imaging and biodistribution characteristics of iodine 131-labeled monoclonal antibody (mAb) G250 (131I-mAbG250), which recognizes a cell-surface antigen expressed by human renal cell carcinoma (RCC). PATIENTS AND METHODS G250 is a cell-surface antigen recognized by mAbG250 expressed by RCC but not detected in normal kidney. Clear-cell RCC, the most frequent form of RCC, shows homogeneous expression of G250, whereas non-clear-cell RCC and cancers derived from other organs generally do not express G250. Expression in normal tissues is highly restricted and limited to large bile ducts and gastric epithelium. 131I-mAbG250 was administered intravenously (IV) to 16 patients with RCC 7 to 8 days before surgery at five dose levels, with at least three patients entered at each dose level. RESULTS Clear tumor images were observed in 12 patients with G250-positive tumors and in one of three patients with G250-negative tumors. Imaged lesions in the peritoneal cavity were confirmed at surgery. The smallest lesion visualized was 8 mm in diameter. The specificity of 131I-mAbG250 localization to tumor tissue was established by radioactivity measurements, autoradiography, and immunohistochemistry of biopsied tissues, and technetium 99-human serum albumin blood-flow studies. The fraction of the injected 131I-mAbG250 dose per gram tumor (%ID/g tumor) localized in G250-positive tumors showed a broad range, but reached levels as high as 0.02% to 0.12%. CONCLUSION 131I-mAbG250 localized specifically to G250 antigen-positive RCC and seems to have considerable potential as an imaging agent in RCC patients. 131I-mAbG250 uptake in the tumors, relative as well as absolute, are among the highest reported for tumor biopsies obtained 8 days after IV mAb administration. Based on the specific localization and high accumulation, mAb G250 may have therapeutic potential.


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