scholarly journals Quantitative investigation of human cell surface N-glycoprotein dynamics

2017 ◽  
Vol 8 (1) ◽  
pp. 268-277 ◽  
Author(s):  
Haopeng Xiao ◽  
Ronghu Wu

We designed the first method to systematically investigate cell surface glycoprotein dynamics and measure their half-lives.

Nature ◽  
1980 ◽  
Vol 286 (5776) ◽  
pp. 888-891 ◽  
Author(s):  
M. Bishr Omary ◽  
Ian S. Trowbridge ◽  
Jun Minowada

1992 ◽  
Vol 73 (10) ◽  
pp. 2617-2624 ◽  
Author(s):  
D. Naniche ◽  
T. F. Wild ◽  
C. Rabourdin-Combe ◽  
D. Gerlier

1986 ◽  
Vol 103 (4) ◽  
pp. 1595-1603 ◽  
Author(s):  
P J Brown ◽  
R L Juliano

We have previously reported the use of monoclonal antibodies to identify a 140-kD cell surface glycoprotein in mammalian cells that is specifically involved in fibronectin-mediated cell adhesion. We now report the purification of this molecule using immunoaffinity chromatography and the subsequent generation of polyclonal antibodies that selectively immunoprecipitate 140-kD putative fibronectin receptor glycoprotein (gp140) extracted from rodent or human cells; these antibodies also specifically block fibronectin-mediated cell adhesion but not adhesion mediated by other factors in serum. Expression of gp140-like molecules was detected on the surfaces of several adherent human cell lines (HDF, WISH, and EFC) but not on erythrocytes; however, gp140 was also detected on a nonadherent human lymphoid line (DAUDI). Analysis of gp140 on nonreducing SDS gels revealed two closely migrating bands. Protease digestion and peptide mapping suggests that the two bands are closely related polypeptides.


1995 ◽  
Vol 62 (5) ◽  
pp. 610-618 ◽  
Author(s):  
Mara Fornaro ◽  
Roberta Dell' Arciprete ◽  
Manuela Stella ◽  
Cecilia Bucci ◽  
Michele Nutini ◽  
...  

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