Method for Measuring the Affinity between Carbohydrate Ligands and Certain Proteins

1980 ◽  
pp. 145-149
Author(s):  
CORNELIS P.J. GLAUDEMANS ◽  
MICHAEL E. JOLLEY
Keyword(s):  
1991 ◽  
Vol 2 (3-4) ◽  
pp. (23)231-(30)238
Author(s):  
L. Nagy ◽  
L. Korecz ◽  
I. Kiricsi ◽  
L. Zsikla ◽  
K. Burger

FEBS Letters ◽  
2011 ◽  
Vol 585 (14) ◽  
pp. 2295-2299 ◽  
Author(s):  
Azusa Takahashi-Nakaguchi ◽  
Tsuyoshi Hiraoka ◽  
Kikuo Iwabuchi

2021 ◽  
Vol 28 ◽  
Author(s):  
Javier Rojo ◽  
Pedro M. Nieto ◽  
José Luis de Paz

: Langerin is a C-type Lectin expressed at the surface of Langerhans cells, which play a pivotal role in protecting organisms against pathogen infections. To address this aim, Langerin presents at least two recognition sites, one Ca2+-dependent and another one independent, capable of recognizing a variety of carbohydrate ligands. In contrast to other lectins, Langerin recognizes sulfated glycosaminoglycans (GAGs), a family of complex and heterogeneous polysaccharides present in the cell membrane and the extracellular matrix at the interphase generated in the trimeric form of Langerin but absent in the monomeric form. The complexity of these oligosaccharides has impeded the development of well-defined monodisperse structures to study these interaction processes. However, in the last few decades, an improvement of synthetic developments to achieve the preparation of carbohydrate multivalent systems mimicking the GAGs has been described. Despite all these contributions, very few examples are reported where the GAG multivalent structures are used to evaluate the interaction with Langerin. These molecules should pave the way to explore these GAG-Langerin interactions.


1992 ◽  
Vol 176 (3) ◽  
pp. 639-646 ◽  
Author(s):  
P S Veras ◽  
C de Chastellier ◽  
M Rabinovitch

Leishmania are flagellated protozoan parasites which, in their amastigote stages, survive and multiply within phagolysosome-like parasitophorous vacuoles (PV) of mammalian macrophages (MO). This study develops an earlier ultrastructural, incidental observation that zymosan particles (Z) were transferred to the PV of macrophages infected with Leishmania amazonensis. In the present report, a pulse-chase light microscopic assay was used to delineate several features of the Z transfer. The assay reflects both the movement of internalized particles to a position adjoining a PV, and their delivery to the vacuoles. Transfer was selective, in the sense that Z, beta-glucan or heat-killed yeast particles were transferred, whereas latex beads, aldehyde-fixed, or immunoglobulin G-coated erythrocytes were not. This selectivity may be related to the high density of carbohydrate ligands displayed on the surface of yeast-derived particles, to ligand resistance to lysosomal degradation or to signals encoded in the cytosolic tails of the receptors involved in particle recognition. A few Z particles could be found within PV after 1 h of incubation with infected MO, but chase periods of several hours at 34 degrees C were required for particle transfer to the PV in a substantial proportion of the MO. Ammonium chloride, chloroquine, or monensin, compounds which increase the pH in acidified compartments, substantially enhanced the transfer of Z particles. Finally, transfer was inhibited by cytochalasin D, but was unaffected by the antitubulin nocodazole. Although it is not yet known if particle transfer occurs by fusion of donor vesicles with PV or by interiorization of the former into the latter, the model described should be useful in the study of the interactions between large phagocytic vesicles and the modulation of those interactions by cellular, parasitic, and environmental signals.


2002 ◽  
Vol 337 (7) ◽  
pp. 651-656 ◽  
Author(s):  
Cristina De Castro ◽  
Antonio Molinaro ◽  
Federico Giordano ◽  
Ida Orabona ◽  
Francesco Ruffo

2021 ◽  
Vol 12 ◽  
Author(s):  
Ellen Menkhorst ◽  
Nandor Gabor Than ◽  
Udo Jeschke ◽  
Gabriela Barrientos ◽  
Laszlo Szereday ◽  
...  

Lectin-glycan interactions, in particular those mediated by the galectin family, regulate many processes required for a successful pregnancy. Over the past decades, increasing evidence gathered from in vitro and in vivo experiments indicate that members of the galectin family specifically bind to both intracellular and membrane bound carbohydrate ligands regulating angiogenesis, immune-cell adaptations required to tolerate the fetal semi-allograft and mammalian embryogenesis. Therefore, galectins play important roles in fetal development and placentation contributing to maternal and fetal health. This review discusses the expression and role of galectins during the course of pregnancy, with an emphasis on maternal immune adaptions and galectin-glycan interactions uncovered in the recent years. In addition, we summarize the galectin fingerprints associated with pathological gestation with particular focus on preeclampsia.


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