scholarly journals Human cell surface glycoprotein related to cell proliferation is the receptor for transferrin.

1981 ◽  
Vol 78 (5) ◽  
pp. 3039-3043 ◽  
Author(s):  
I. S. Trowbridge ◽  
M. B. Omary
Keyword(s):  
Cell Proliferation ◽  
Cell Surface ◽  
Human Cell ◽  
Surface Glycoprotein ◽  
Cell Surface Glycoprotein

Human cell-surface glycoprotein with unusual properties

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

scholarly journals A Monoclonal Antibody Recognizes a Human Cell Surface Glycoprotein Involved In Measles Virus Binding

1992 ◽  
Vol 73 (10) ◽  
pp. 2617-2624 ◽  
Author(s):  
D. Naniche ◽  
T. F. Wild ◽  
C. Rabourdin-Combe ◽  
D. Gerlier
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Human Cell ◽  
Measles Virus ◽  
Surface Glycoprotein ◽  
Virus Binding ◽  
Cell Surface Glycoprotein

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

2017 ◽  
Vol 8 (1) ◽  
pp. 268-277 ◽  
Author(s):  
Haopeng Xiao ◽  
Ronghu Wu
Keyword(s):  
Cell Surface ◽  
Human Cell ◽  
Surface Glycoprotein ◽  
Quantitative Investigation ◽  
Cell Surface Glycoprotein

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

scholarly journals Rat Parotid Gland Acinar Cell Proliferation: Signal Transduction at the Plasma Membrane

1993 ◽  
Vol 4 (3) ◽  
pp. 537-543 ◽  
Author(s):  
K.R. Purushotham ◽  
Y. Nakagawa ◽  
M.G. Humphreys-Beher ◽  
N. Maeda ◽  
C.A. Schneyer
Keyword(s):  
Signal Transduction ◽  
Cell Proliferation ◽  
Cell Surface ◽  
Acinar Cell ◽  
Intracellular Signaling ◽  
Plasma Membranes ◽  
Surface Glycoprotein ◽  
Dependent Manner ◽  
Intact Cells ◽  
Cell Surface Glycoprotein

Galactosyltransferase (Gal Tase) is involved in a "receptor-ligand-type" interaction at the cell surface that mediates signal transduction following isoproterenol (ISO) treatment leading to acinar cell proliferation. Evidence is presented herein for the identification of the cell-surface glycoprotein signaling component. Using intact cells or isolated plasma membranes, the EGF-receptor (EGF-R) was specifically radiolabeled with [14C]-Galactose following ISO treatment. Injection of a polyclonal antibody monospecific for rat EGF-R also inhibited proliferation in a dose-dependent manner. The immunoaffinity purified receptor demonstrated altered lectin binding and increased in vitro Gal Tase substrate capacity following β-agonist treatment when compared with EGF-R isolated from control animals. When acinar cells were incubated in the presence of EGF, plasma membranes from control and ISO-treated animals showed autophosphorylation of EGF-R tyrosine moieties, transient increases in membrane associated phospholipase Cy, and increased cellular levels of cAMP. These properties of the tyrosine phosphate signaling pathway could be duplicated by the exogenous addition of bovine Gal Tase to ISO-treated cells but not control cells. The results suggest that cell surface Gal Tase interacts with a form of the EGF-R, having altered carbohydrate moieties to promote intracellular signaling for acinar cell proliferation.

scholarly journals Expression and function of a putative cell surface receptor for fibronectin in hamster and human cell lines.

1986 ◽  
Vol 103 (4) ◽  
pp. 1595-1603 ◽  
Author(s):  
P J Brown ◽  
R L Juliano
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Lines ◽  
Human Cell ◽  
Mammalian Cells ◽  
Surface Glycoprotein ◽  
Cell Surface Receptor ◽  
Human Cell Lines ◽  
Cell Surface Glycoprotein ◽  
Fibronectin Receptor

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.

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