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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Lectin, galactoside-binding, soluble, 8

galectin-8, Gal-8, Po66-CBP, PCTA-1
This gene encodes a member of the galectin family. Galectins are beta-galactoside-binding animal lectins with conserved carbohydrate recognition domains. The galectins have been implicated in many essential functions including development, differentiation, cell-cell adhesion, cell-matrix interaction, growth regulation, apoptosis, and RNA splicing. This gene is widely expressed in tumoral tissues and seems to be involved in integrin-like cell interactions. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: galectin-1, galectin-3, CAN, ACID, HAD
Papers on galectin-8
Molecular characterization of Galectin-8 from Nile tilapia (Oreochromis niloticus Linn.) and its response to bacterial infection.
New
Areechon et al., Bangkok, Thailand. In Mol Immunol, Dec 2015
We isolated and characterized the cDNA of galectin-8 (OnGal-8) in Nile tilapia (Oreochromis niloticus).
Fetal gender specific expression of tandem-repeat galectins in placental tissue from normally progressed human pregnancies and intrauterine growth restriction (IUGR).
New
Jeschke et al., München, Germany. In Placenta, Dec 2015
We identified a significantly lower expression of gal-4 and gal-9 in villous trophoblast tissue of IUGR placentas with male fetuses and a downregulation of gal-4 and gal-8 in extravillous trophoblast (EVT) from IUGR and male fetuses.
Glycodendrimersomes from Sequence-Defined Janus Glycodendrimers Reveal High Activity and Sensor Capacity for the Agglutination by Natural Variants of Human Lectins.
New
Percec et al., Philadelphia, United States. In J Am Chem Soc, Nov 2015
Three naturally occurring forms of the human adhesion/growth-regulatory lectin galectin-8, Gal-8S and Gal-8L, which differ by the length of linker connecting their two active domains, and a single amino acid mutant (F19Y), were used as probes to study activity and sensor capacity.
NMR assignments of the C-terminal domain of human galectin-8.
New
Hsu et al., Taipei, Taiwan. In Biomol Nmr Assign, Oct 2015
Human galectin 8 plays an important role in numerous cancer and immune responses.
Combining Crystallography and Hydrogen-Deuterium Exchange to Study Galectin-Ligand Complexes.
New
Gabius et al., Madrid, Spain. In Chemistry, Oct 2015
Cell binding by using glycosylation mutants reveals binding of the N-terminal domain of chicken galectin-8 (CG-8N) to α-2,3-sialylated and galactose-terminated glycan chains.
Comparison of galectin expression signatures in rejected and accepted murine corneal allografts.
New
Panjwani et al., Boston, United States. In Cornea, Jun 2015
Although in both accepted and rejected grafts, expression levels of the 5 lectins were upregulated compared with normal corneas, there were distinct differences in the expression levels of galectins-8 and 9 between accepted and rejected grafts, as both the Western blot and immunofluorescence staining revealed that galectin-8 is upregulated, whereas galectin-9 is downregulated in the rejected grafts compared with the accepted grafts.
Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface.
New
Percec et al., München, Germany. In Proc Natl Acad Sci U S A, Jun 2015
Alteration of the linker length in human galectin-8 and single-site mutation (F19Y) are used herein to illustrate the potential of glycodendrimersomes with programmable glycan displays as a model system to reveal the functional impact of natural sequence variations in trans recognition.
The mammalian lectin galectin-8 induces RANKL expression, osteoclastogenesis, and bone mass reduction in mice.
Zick et al., Israel. In Elife, 2014
In this study, we show that mice overexpressing galectin-8, a secreted mammalian lectin of the galectins family, exhibit accelerated osteoclasts activity and bone turnover, which culminates in reduced bone mass, similar to cases of postmenopausal osteoporosis and cancerous osteolysis.
Heterologous expression of newly identified galectin-8 from sea urchin embryos produces recombinant protein with lactose binding specificity and anti-adhesive activity.
Matranga et al., Palermo, Italy. In Sci Rep, 2014
Here, we report a tandem-repeat type galectin from the Paracentrotus lividus sea urchin embryo, referred to as Pl-GAL-8.
Galectin-8: a matricellular lectin with key roles in angiogenesis.
Review
Elola et al., Buenos Aires, Argentina. In Glycobiology, 2014
Galectin-8 (gal-8) is a "tandem-repeat"-type galectin, containing two carbohydrate recognition domains connected by a linker peptide.
Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors.
Review
Rabinovich et al., Buenos Aires, Argentina. In Histol Histopathol, 2014
Galectin-8 (Gal-8) is a 'tandem-repeat'-type galectin, which possesses two carbohydrate recognition domains connected by a linker peptide.
Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases.
Impact
Broz et al., Basel, Switzerland. In Nature, 2014
Moreover, recognition of the lysed vacuole by the danger sensor galectin-8 initiates the uptake of bacteria into autophagosomes, which results in a reduction of caspase-11 activation.
Hierarchical and selective roles of galectins in hepatocarcinogenesis, liver fibrosis and inflammation of hepatocellular carcinoma.
Review
Troncoso et al., Buenos Aires, Argentina. In World J Gastroenterol, 2014
On the other hand, the "tandem-repeat-type" lectins galectin-8 and galectin-9 are down-regulated in tumor hepatocytes.
Redundant and antagonistic functions of galectin-1, -3, and -8 in the elicitation of T cell responses.
GeneRIF
Campetella et al., Buenos Aires, Argentina. In J Immunol, 2012
Gal-8 stimulated naive T cells, but had an antiproliferative effect when these cells were activated.A dose of recombinant Gal-8 administered with a suboptimal Ag dose to DO11.10 mice strengthened weak responses in vivo.
Galectin-8 in IgA nephritis: decreased binding of IgA by galectin-8 affinity chromatography and associated increased binding in non-IgA serum glycoproteins.
GeneRIF
Leffler et al., Lund, Sweden. In J Clin Immunol, 2012
This is the first study that relates a galectin, an endogenous lectin family, to IgA nephritis and thus should stimulate new avenues of research into the pathophysiology of the disease.
Novel role for galectin-8 protein as mediator of coagulation factor V endocytosis by megakaryocytes.
GeneRIF
Meijer et al., Amsterdam, Netherlands. In J Biol Chem, 2012
a novel role for the tandem repeat Gal8 in promoting FV endocytosis.
Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion.
Impact
GeneRIF
Randow et al., Cambridge, United Kingdom. In Nature, 2012
results illustrate how cells deploy the danger receptor galectin 8 to combat infection by monitoring endosomal and lysosomal integrity on the basis of the specific lack of complex carbohydrates in the cytosol
Galectins promote the interaction of influenza virus with its target cell.
GeneRIF
Bovin et al., Moscow, Russia. In Biochemistry (mosc), 2011
Galectin 1 and galectin 8 promote influenza virus binding in dose dependent manner.
Use of glycan microarrays to explore specificity of glycan-binding proteins.
Review
Cummings et al., Atlanta, United States. In Methods Enzymol, 2009
We also describe our new approach to normalizing glycan microarray data derived from concentration-dependent analyses of GBP binding, and the application of this approach with the plant lectin Sambucus nigra agglutinin (SNA-I) and human galectin-8.
Tumor galectinology: insights into the complex network of a family of endogenous lectins.
Review
Gabius et al., Heidelberg, Germany. In Glycoconj J, 2003
Furthermore, variants with distinct amino acid substitutions (galectin-8, Po66-CBP, PCTA-1, CocaI/II and galectin-9/ecalectin) and generation of multiple mRNA species, notably those coding for truncated galectin-8 and -9 versions with only one lectin site, justify to portray these two family members not as distinct individuals but as groups.
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