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Galectin-1 and immunotherapy for brain cancer

Expert Review of Neurotherapeutics, 2011
The prognosis of patients diagnosed with high-grade glioma continues to be dismal in spite of multimodal treatment. Active specific immunotherapy by means of dendritic cell vaccination is considered to be a new promising concept that aims at generating an anti-tumoral immune response.
Verschuere, Tina   +4 more
openaire   +3 more sources

Characterisation of Oxidized Recombinant Human Galectin-1

Protein & Peptide Letters, 2009
Oxidized human galectin-1 plays a role in the immune response to injured axons. Over-expression of galectin-1 by cancer, in combination with cancer associated oxidative stress suggests oxidized human galectin-1 may also play a role(s) in tumourigenesis.
Scott, Stacy A   +2 more
openaire   +5 more sources

Galectin-1 and HIV-1 Infection

2010
Initial binding of human immunodeficiency virus-1 (HIV-1) to its susceptible CD4(+) cells is the limiting step for the establishment of infection as the avidity of viral envelope gp120 for CD4 is not high and the number of viral envelope spikes on the surface is found to be low compared to highly infectious viruses. Several host factors, such as C-type
Christian, St-Pierre   +3 more
openaire   +2 more sources

Glycoprotein 90K/MAC‐2BP interacts with galectin‐1 and mediates galectin‐1–induced cell aggregation

International Journal of Cancer, 2001
The glycoprotein 90K was originally described as a tumor-secreted antigen and subsequently found to have immunostimulatory activity as well as other possible functions. This protein interacts with an endogenous lectin, galectin-3, and may play a role in tumor metastasis through this interaction. Because 90K is heavily glycosylated, it may also interact
TINARI, Nicola   +5 more
openaire   +3 more sources

Galectin-1 plays essential roles in adult mammalian nervous tissues. Roles of oxidized galectin-1

Glycoconjugate Journal, 2002
Previous data have suggested that galectin-1 is expressed widely in nervous tissues at embryonic stages but becomes restricted mainly to peripheral nervous tissues with maturation. Though the expression is intense in adult mammalian peripheral neurons, there had been no report about functions of galectin-1 there.
Hidenori, Horie, Toshihiko, Kadoya
openaire   +2 more sources

Galectin‐1 production is elevated in hypertrophic scar

Wound Repair and Regeneration, 2020
AbstractUpon healing, burn wounds often leave hypertrophic scars (HTSs) marked by excess collagen deposition, dermal and epidermal thickening, hypervascularity, and an increased density of fibroblasts. The Galectins, a family of lectins with a conserved carbohydrate recognition domain, function intracellularly and extracellularly to mediate a multitude
Liam D. Kirkpatrick   +5 more
openaire   +2 more sources

Structural and Functional Studies of Galectin-1: A Novel Axonal Regeneration-Promoting Activity for Oxidized Galectin-1

Current Drug Targets, 2005
Recently, we discovered oxidized galectin-1 as a factor that regulates initial axonal growth in the peripheral nerve after axotomy. Galectin-1 is a member of the galectins, a family of animal lectins ranging from Caenorhabditis elegans to humans, which is defined by their affinity for beta-galactosides and by significant sequence similarity in the ...
Toshihiko, Kadoya, Hidenori, Horie
openaire   +2 more sources

High glucose‐induced Galectin‐1 in human podocytes implicates the involvement of Galectin‐1 in diabetic nephropathy

Cell Biology International, 2014
Abstract The diabetic milieu is believed to change the activity, or result in damage of podocytes—a key component of the glomerular filtration barrier and known to secrete matrix for glomerular basement membrane. This in turn contributes to diabetic nephropathy.
Yinghong, Liu   +7 more
openaire   +2 more sources

Characterization of the Interaction of Galectin-1 with Sodium Arsenite

Chemical Research in Toxicology, 2006
We previously showed that galectin-1 (GAL1) is an arsenic-binding protein. In the current study, we further characterize the interaction of GAL1 with sodium arsenite (As(III)). The GALl-As(III) complex was prepared from the cell extracts of GAL1-transfected Escherichia coli (E. coli) that were pretreated with As(III).
Lin, C. H.   +7 more
openaire   +2 more sources

Galectin-1: A bifunctional regulator of cellular proliferation

Glycoconjugate Journal, 2002
Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and proliferation. In different circumstances, it acts as a mitogen, as an inhibitor of cell proliferation, and as a promoter of cellular apoptosis. Many of these activities, particularly the mitogenic and apoptotic responses, follow from the interaction of galectin ...
Ken, Scott, Cristina, Weinberg
openaire   +2 more sources

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