Oxidation and chemical modification of lung β-galactoside-specific lectin

Whitney, Philip L.; Powell, Janet T.; Sanford, Gary L.

doi:10.1042/bj2380683

Cited by 78 publications

(61 citation statements)

References 23 publications

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“…Galectin-1 exists in either a reduced or oxidized form, and only the reduced form possesses carbohydrate-binding activity (38). The infusion of CS-Galectin-1, a reduced form in which all of the cysteines responsible for its oxidation have been converted to serine (39), significantly increased the number of slowly dividing cells (Fig.…”

Section: Infusion Of Galectin-1 Protein Increases the Slowly Dividingmentioning

confidence: 97%

A carbohydrate-binding protein, Galectin-1, promotes proliferation of adult neural stem cells

Sakaguchi

Shingo

Shimazaki³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

143

150

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In the subventricular zone of the adult mammalian forebrain, neural stem cells (NSCs) reside and proliferate to generate young neurons. We screened factors that promoted the proliferation of NSCs in vitro by a recently developed proteomics technique, the ProteinChip system. In this screen, we identified a soluble carbohydrate-binding protein, Galectin-1, as a candidate. We show herein that Galectin-1 is expressed in a subset of slowly dividing subventricular zone astrocytes, which includes the NSCs. Based on results from intraventricular infusion experiments and phenotypic analyses of knockout mice, we demonstrate that Galectin-1 is an endogenous factor that promotes the proliferation of NSCs in the adult brain.lectin ͉ mobilization ͉ stem cell niche

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Section: Infusion Of Galectin-1 Protein Increases the Slowly Dividingmentioning

confidence: 97%

A carbohydrate-binding protein, Galectin-1, promotes proliferation of adult neural stem cells

Sakaguchi

Shingo

Shimazaki³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

143

150

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“…To stabilize Gal-1, Gal-1 was treated with 100 mM iodoacetamide in 100 mM lactose/ PBS for 12 h at 4°C, similar to the method used previously (41). iGal-1 remained stable over prolonged periods of incubation at 37°C (at least up to 4 days).…”

Section: Preparation Of Recombinant Forms Of Human Gal-1 and Gal-3mentioning

confidence: 99%

Differential Roles of Galectin-1 and Galectin-3 in Regulating Leukocyte Viability and Cytokine Secretion

Stowell

Qian

Karmakar

et al. 2008

The Journal of Immunology

223

189

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Galectin-1 (Gal-1) and galectin-3 (Gal-3) exhibit profound but unique immunomodulatory activities in animals but their molecular mechanisms are incompletely understood. Early studies suggested that Gal-1 inhibits leukocyte function by inducing apoptotic cell death and removal, but recent studies show that some galectins induce exposure of the common death signal phosphatidylserine (PS) independently of apoptosis. In this study, we report that Gal-3, but not Gal-1, induces both PS exposure and apoptosis in primary activated human T cells, whereas both Gal-1 and Gal-3 induce PS exposure in neutrophils in the absence of cell death. Gal-1 and Gal-3 bind differently to the surfaces of T cells and only Gal-3 mobilizes intracellular Ca2+ in these cells, although Gal-1 and Gal-3 bind their respective T cell ligands with similar affinities. Although Gal-1 does not alter T cell viability, it induces IL-10 production and attenuates IFN-γ production in activated T cells, suggesting a mechanism for Gal-1-mediated immunosuppression in vivo. These studies demonstrate that Gal-1 and Gal-3 induce differential responses in T cells and neutrophils, and identify the first factor, Gal-3, capable of inducing PS exposure with or without accompanying apoptosis in different leukocytes, thus providing a possible mechanism for galectin-mediated immunomodulation in vivo.

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“…Supernatants were applied to a 10-ml lactosyl-Sepharose column (Sigma), unbound proteins were washed, and fusion proteins were eluted with either MEPBS buffer or Tris-DTT buffer containing 200 mM lactose. The elution buffers containing ␤-mercaptoethanol or DTT were always freshly prepared to prevent oxidation of galectins by air (34,35). Fractions of 1 ml were collected, and the protein concentration was determined by the Bradford method, using a Bio-Rad protein assay kit (Bio-Rad Laboratories).…”

Section: Expression Analysis Of Galectins By Reverse Transcriptase (Rmentioning

confidence: 99%

Identification and Characterization of Galectin-9, a Novel β-Galactoside-binding Mammalian Lectin

Wada

Kanwar

1997

Journal of Biological Chemistry

297

224

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A 36-kDa ␤-galactoside mammalian lectin protein, designated as galectin-9, was isolated from mouse embryonic kidney by using a degenerate primer polymerase chain reaction and cloning strategy. Its deduced amino acid sequence had the characteristic conserved sequence motif of galectins. Endogenous galectin-9, extracted from liver and thymus, as well as recombinant galectin-9 exhibited specific binding activity for the lactosyl group. It had two distinct N-and C-terminal carbohydrate-binding domains connected by a link peptide, with no homology to any other protein. Galectin-9 had an alternate splicing isoform, exclusively expressed in the small intestine with a 31-amino acid insertion between the N-terminal domain and link peptide. Sequence homology analysis revealed that the C-terminal carbohydrate-binding domain of mouse galectin-9 had extensive similarity to that of monomeric rat galectin-5. The presence of galectin-5 in the mouse could not be demonstrated by polymerase chain reaction or by Northern or Southern blot genomic DNA analyses. Sequence comparison of rat galectin-5 and rat galectin-9 cDNA did not reveal identical nucleotide sequences in the overlapping C-terminal carbohydrate-binding domain, indicating that galectin-9 is not an alternative splicing isoform of galectin-5. However, galectin-9 had a sequence identical with that of its intestinal isoform in the overlapping regions in both species. Southern blot genomic DNA analyses, using the galectin-9 specific probe derived from the N-terminal carbohydrate-binding domain, indicated the presence of a novel gene encoding galectin-9 in both mice and rats. In contrast to galectin-5, which is mainly expressed in erythrocytes, galectin-9 was found to be widely distributed, i.e. in liver, small intestine, thymus > kidney, spleen, lung, cardiac and skeletal muscle > reticulocyte, brain. Collectively, these data indicate that galectin-9 is a new member of the galectin gene family and has a unique intestinal isoform.There is growing evidence that specific carbohydrate moieties and their putative binding proteins, i.e. lectins, play diverse roles in mammalian physiology and development and in various pathological states (1). The mammalian lectins are classified into four categories, C-type lectins (including selectins), P-type lectins, pentraxins, and galectins; the latter are referred to as S-type or S-Lac lectins (2, 3). Galectins are endowed with two essential biochemical properties: 1) characteristic amino acid homologous sequences; and 2) affinity for ␤-galactoside sugars, i.e. carbohydrate-binding domain. In addition, all the known galectins lack a signal peptide, have a cytoplasmic localization, and are secreted as soluble proteins by a nonclassical secretory pathway (4). Seven mammalian galectins, i.e. galectins-1 (5), -2 (6), -3 (7), -4 (8), -5 (9), -7 (10, 11), and -8 (12), have been cloned and characterized. Structural analyses of various galectins indicate the presence of homodimers of carbohydrate-binding domains in galectin-1 and galectin-2, a monom...

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Oxidation and chemical modification of lung β-galactoside-specific lectin

Cited by 78 publications

References 23 publications

A carbohydrate-binding protein, Galectin-1, promotes proliferation of adult neural stem cells

A carbohydrate-binding protein, Galectin-1, promotes proliferation of adult neural stem cells

Differential Roles of Galectin-1 and Galectin-3 in Regulating Leukocyte Viability and Cytokine Secretion

Identification and Characterization of Galectin-9, a Novel β-Galactoside-binding Mammalian Lectin

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