Carbohydrate antigens and lectin receptors of the plasma membrane of carrot cells

PROTOPLASMA ◽  
1989 ◽  
Vol 152 (2-3) ◽  
pp. 123-129 ◽  
Author(s):  
J. P. Knox ◽  
K. Roberts
1984 ◽  
Vol 16 (2) ◽  
pp. 143-152 ◽  
Author(s):  
Prakash C. Misra ◽  
Theodore A. Craig ◽  
Frederick L. Crane

1983 ◽  
Vol 61 (19) ◽  
pp. 941-945 ◽  
Author(s):  
G. H. Farrar ◽  
W. M. Glöckner ◽  
G. Uhlenbruck

1991 ◽  
Vol 99 (3) ◽  
pp. 545-555 ◽  
Author(s):  
LOUISE COLE ◽  
JULIAN COLEMAN ◽  
ANNE KEARNS ◽  
GARETH MORGAN ◽  
CHRIS HAWES

In this paper we report on the uptake of the membrane-impermeant fluorescent probe Lucifer Yellow CH (LY-CH) into the vacuolar system of plant cell suspension cultures. LY-CH is internalised into vacuoles of maize cells at a faster ‘rate’ than carrot cells and in each case, the probe is also trapped at the cell wall. In the presence of the uricosuric drug probenecid, the vacuolar uptake of LY-CH by carrot and maize cells is inhibited and in some cells internalisation of probe is blocked at the plasma membrane. In electroporated carrot cells, LY-CH is sequestered slowly from the cytoplasm into vacuoles by a probenecid-inhibitable transport process. These results are compared with the effects of probenecid on the sequestration of LY-CH from the cytoplasm into the lysosomal system of fibroblasts. In view of the above findings and recent evidence for the putative uptake of LY-CH by fluid-phase endocytosis in plant cells, the possibility that LY-CH is transported across plant membranes via probenecidinhibitable organic anion transporters is discussed


1980 ◽  
Vol 41 (1) ◽  
pp. 89-104
Author(s):  
R. Hellio ◽  
A. Ryter

The disappearance of Wheat Germ Agglutinin (WGA) receptors from the membrane of yeast-engulfing-phagocytic cups in Dictyostelium suggested that these receptors could play a role in yeast adsorption or ingestion. This problem was approached by comparing the fate of WGA, Concanavalin A (Con A) and cationized ferritin (CF) and their effects on the phagocytosis of yeast, bacteria and latex beads. It can be concluded that CF capped in about 30 min and inhibited phagocytosis of any kind of particles for about 15 min. Con A capped in 20–60 min and inhibited phagocytosis of all particles for 1 h 30 min. The time at which phagocytosis started to occur corresponded approximately to the moment at which large areas of plasma membrane were totally devoid of marker. WGA did not cap but induced the formation of large and tight aggregates. The surface of the peripheral cells progressively released WGA in 1 h 30 min. Afterwards, the cells were able to ingest latex beads and bacteria but did not phagocytoze yeast. The latter started to be adsorbed onto the cells and to be ingested only 1 h later. Double labelling experiments showed that CF and Con A receptors were still absent in the plasma membrane, when phagocytosis of any kind of particles started to occur. WGA-labelled cells ingested latex beads and bacteria when their plasma membrane was still devoid of WGA receptors but were able to ingest yeast only after their regeneration. These observations strongly suggest that WGA receptors may correspond to specific receptors for yeast phagocytosis.


1997 ◽  
Vol 3 (S2) ◽  
pp. 119-120
Author(s):  
A.M. Argayosa ◽  
F.F. Natividad ◽  
R.R. Matias ◽  
G.L. Enriquez

Distribution of glucose and mannose moieties of Acanthamoeba sp. (W4) Philippine isolate was detected using fluorescem isothiocyanate (FITC)- labeled Concannavalin A (Con A) lectin. Green fluorescent patches around the plasma membrane of agglutinated trophozoites (Fig.1) were observed. Isolated Acanthamoeba cyst exhibited strong fluorescence on the cyst wall Brighter fluorescence was detected on the site of adherence between the Acanthamoeba (W4) cysts and trophozoites (Fig. 1,3). These lectin receptors were concentrated at the uroidal region of the trophozoite. The fluorescence, however, was absent in the newly forming hyaline cap (Fig.4). Upon addition of α -methyl-mannoside (0.5 M), Con A binding to sugar moieties in cyst and trophozoites was blocked and no fluorescence was observed.The binding specificity of Con A-FITC and Acanthamoeba cell surface mannose moieties demonstrate topographical distribution of lectin receptor sites. Ultrastructurally, ferritin-labeled Con A at cell adhesion sites showed clustering of lectin receptors. Occurrence of fluorescence in Naegleria sp. using Con A-FITC has been shown to concentrate at the uroidal region but no fluorescence was seen at the anterior of newly formed pseudopodia.


Biochemistry ◽  
1983 ◽  
Vol 22 (16) ◽  
pp. 3969-3975 ◽  
Author(s):  
Thomas N. Metcalf ◽  
John L. Wang ◽  
Karel R. Schubert ◽  
Melvin Schindler

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