scholarly journals Analysis of COPII Vesicles Indicates a Role for the Emp47-Ssp120 Complex in Transport of Cell Surface Glycoproteins

Traffic ◽  
2016 ◽  
Vol 17 (3) ◽  
pp. 191-210 ◽  
Author(s):  
Neil G. Margulis ◽  
Joshua D. Wilson ◽  
Christine M. Bentivoglio ◽  
Nripesh Dhungel ◽  
Aaron D. Gitler ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Surface Glycoproteins ◽  
Copii Vesicles ◽  
Surface Glycoproteins

Recognition of collagen by fibroblasts through cell surface glycoproteins reactive with Phaseolus vulgaris agglutinin

1992 ◽  
Vol 101 (3) ◽  
pp. 625-633
Author(s):  
H. Asaga ◽  
K. Yoshizato
Keyword(s):  
Phaseolus Vulgaris ◽  
Cell Surface ◽  
Ricinus Communis ◽  
Specific Binding ◽  
Collagen Gel ◽  
Collagen Fibrils ◽  
Pokeweed Mitogen ◽  
Collagen Gel Contraction ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

The role of glycochains of cell surface glycoproteins in the cell to collagen interaction was examined by studying the effect of lectins on the fibroblast-mediated collagen gel contraction. Lectins of Phaseolus vulgaris agglutinin (PHA), concanavalin A (ConA), lentil seed agglutinin (LCA), pea agglutinin (PSA), Ricinus communis agglutinin-60 (RCA), and wheat germ agglutinin (WGA) dose-dependently inhibited gel contraction, while lectins of mushroom agglutinin (ABA), peanut agglutinin (PNA), pokeweed mitogen (PWM), and soybean agglutinin (SBA) did not. Of these lectins, PHA seemed to be worthy of further analysis, because PHA, but not other lectins, inhibited spreading of fibroblasts on collagen fibrils but not on plastic or gelatin, suggesting that cell-surface glycoproteins responsive to the lectin are involved in the specific binding of fibroblasts to native collagen fibrils. The inhibitory effect of PHA-E4, an isolectin of PHA, was more intense than that of PHA-L4, another isolectin of PHA. The collagen gel contraction was also inhibited by tunicamycin and monensin in a concentration-dependent and reversible manner. These results strongly suggest that PHA-E4-reactive glycoproteins of the fibroblast surface play an important role in cell to collagen binding during the gel contraction. Five membrane proteins including beta 1 subunits of the integrin family were obtained by affinity chromatography with PHA-E4.

scholarly journals Cell surface oligosaccharides on Dictyostelium during development

1991 ◽  
Vol 99 (3) ◽  
pp. 485-495
Author(s):  
SUPAVADEE AMATAYAKUL-CHANTLER ◽  
MICHAEL A. J. FERGUSON ◽  
RAYMOND A. DWEK ◽  
THOMAS W. RADEMACHER ◽  
RAJ B. PAREKH ◽  
...  
Keyword(s):  
Cell Surface ◽  
Time Frame ◽  
Protein Glycosylation ◽  
Developmental Studies ◽  
Plant Glycoproteins ◽  
Chemical Technique ◽  
Cell Surface Glycoproteins ◽  
Oligosaccharide Structures ◽  
Surface Glycoproteins

Developmental studies of the changes in protein glycosylation are useful in elucidating the role of oligosaccharides in biological events. We have used the chemical technique, hydrazinolysis, to release oligosaccharides from cell surface glycoproteins of Dictyostelium discoideum. Oligomannose type, xylose- and fucose-containing oligosaccharides were found to be present. The charged oligosaccharides contained sulphate and mannose 6-phosphate residues; no sialic acid was detected. The charged oligosaccharides also contained significant amounts of xylose, arabinose, fucose and galactose, as well as mannose and N-acetylglucosamine, which were the main constituents of the neutral glycans. By monitoring the chemical characteristics of the liberated oligosaccharides, dramatic changes in both the charge and size distribution of cell surface oligosaccharides were observed throughout the 24 h period of cell development. A comparison, however, between the neutral glycan structures of prestalk and prespore cells, over the same time frame showed no dramatic differences Discoidin, a lectin present on the cell surface of 8 h cells, was found not to be glycosylated. Affinity chromatography using immobilised discoidin was used to probe a sugar library made from the cell surface glycoproteins of 8h cells. Discoidin was found to bind selectively an oligosaccharide with the structure Manα3(Manα6)(Xylβ2)Manβ4GlcNAc. This oligosaccharide lacks a conventional N,N'-diacetylchitobiose core and has only been previously observed in plant glycoproteins. Peptide-N-glycosidase F treatment of horseradish peroxidase released an identical structure, confirming that the oligosaccharide was not a degradation fragment of the hydrazine. The oligosaccharide was found to inhibit discoidinmediated haemagglutination with a Kt of 0.75 mM, a concentration approximately 100 times lower than that for galactose The correlation between changes in the amoebal plasma membrane oligosaccharide structures and the biological events occurring at different stages of development such as cell-cell adhesion and cellsubstratum attachment suggest an important role for sugars in these processes

Interaction ofVicia gramineaAnti-N Lectin with Cell Surface Glycoproteins from Erythrocytes with Rare Blood Group Antigens

1984 ◽  
Vol 365 (1) ◽  
pp. 469-478 ◽  
Author(s):  
Dominique BLANCHARD ◽  
Alain ASSERAF ◽  
Marie José PRiGENT ◽  
John J. MOULDS ◽  
Dasnayanee CHANDANAYINGYONG ◽  
...  
Keyword(s):  
Cell Surface ◽  
Blood Group ◽  
Blood Group Antigens ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

Cell surface glycoproteins of CHO cells

1986 ◽  
Vol 165 (1) ◽  
pp. 92-106 ◽  
Author(s):  
Thomas J. Raub ◽  
R.Michael Roberts
Keyword(s):  
Cell Surface ◽  
Cho Cells ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

Cell-Surface Glycoproteins of Normal and Malignant Rat Liver Cells

1978 ◽  
pp. 412-431
Author(s):  
JAMES J. STARLING ◽  
DOUGLAS C. HIXSON ◽  
SYLVIA C. CAPETILLO ◽  
EDWARD M. DAVIS ◽  
GIOVANNI NERI ◽  
...  
Keyword(s):  
Cell Surface ◽  
Rat Liver ◽  
Liver Cells ◽  
Rat Liver Cells ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins
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