Elucidation of the mechanism of interaction of sheep spleen galectin-1 with splenocytes and its role in cell-matrix adhesion

Ramkumar, Rajagopal; Podder, Santosh

doi:10.1002/1099-1352(200009/10)13:5<299::aid-jmr504>3.0.co;2-o

Cited by 13 publications

(14 citation statements)

References 35 publications

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“…The VpreB partner is neither directly involved in GAL1 binding nor is it necessary for a conformational imprinting of the SLC-binding site, because SLC and -like bind to GAL1 with close affinities (K a values of 3.12 ϫ 10 6 M Ϫ1 and 1.29 ϫ 10 6 M Ϫ1 , respectively). These affinities are on the same order of magnitude as those measured for GAL1 cell-surface counter- receptors (32). The SLC -like NH 2 -terminal extra loop seems to be the major GAL1-binding element, which points to a clear biological role for this SLC region.…”

Section: Discussionsupporting

confidence: 64%

Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering

Gauthier

Rossi

Roux

et al. 2002

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

228

215

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Although preB cell-receptor (pre-BCR) formation and cell-surface expression is essential for B cell development, pre-BCR generation of signal transduction remains elusive. Here, we report that recombinant pre-BCRs and the surrogate light chain bind specifically to the bone marrow stromal cell galectin-1 (GAL1), an S-type lectin. The surrogate light chain͞GAL1 association is a direct protein-protein interaction (K a ‫؍‬ 2 ؋ 10 6 M ؊1 ), and the NH2 extra loop of -like is the major binding element. Pre-BCR binding to stromal cells depends upon GAL1 anchoring to glycosylated counter-receptors, and these complexes completely relocalize to form a synapse at the contact zone between preB and stromal cells. This immune developmental synapse is accompanied by the initiation of intracellular tyrosine kinase activity and signal transduction from the pre-BCR.

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Section: Discussionsupporting

confidence: 64%

Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering

Gauthier

Rossi

Roux

et al. 2002

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

228

215

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“…Because of their variety and the multiple subcellular localization of galectins, many different functions have been proposed for these proteins including roles in cell-cell adhesion, cell-matrix adhesion, direct effects on cell growth and viability, and potential intracellular functions in regulating metabolism [10][11][12][13][14][15][16][37][38][39][40][41][42][43][44][45][46]. The ubiquitously expressed Galectin-1 is the most extensively studied.…”

Section: Discussionmentioning

confidence: 99%

“…The ubiquitously expressed Galectin-1 is the most extensively studied. The discovery that Galectin-1 binds with high affinity to polylactosamine-containing ligands (such as laminin) and the colocalization of Galectin-1 with laminin in extracellular matrix suggested that its major function could be to promote cell adhesion to glycoconjugates [10][11][12][13][14][15][16].…”

Section: Discussionmentioning

confidence: 99%

“…Galectin-1 is a member of the S-type galactoside-binding animal lectins [7][8][9]. The discovery that Galectin-1 binds with high affinity to polylactosamine-containing ligands (such as laminin) and the colocalization of Galectin-1 with laminin in extracellular matrix suggested that its major function could be to promote cell adhesion to glycoconjugates [10][11][12][13][14][15][16]. To test the possibility that Galectin-1 recognizes Chitlac, we produced recombinant pig Galectin-1 and surveyed its binding capacities on Chitlac and its distribution on chondrocyte aggregates.…”

Section: Introductionmentioning

confidence: 99%

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The role of Galectin-1 in the interaction between chondrocytes and a lactose-modified chitosan

et al. 2005

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“…Similarly, Skrincosky et al [25] found a significant increase in the lactose-inhibitable adhesion of A121 ovarian carcinoma cells to polymerized Gal-1-coated plates, while only 37% of the cells adhered to adsorbed dimeric Gal-1. Further, the adhesion of splenocytes to plates coated with sheep spleen Gal-1 has been reported [26]. Gal-1 promotes the adhesion of normal and cancer cells to ECM glycoproteins such as LN [27 -29].…”

Section: Galectin-1mentioning

confidence: 99%

Galectins: matricellular glycan-binding proteins linking cell adhesion, migration, and survival

Elola

Wolfenstein‐Todel

Troncoso

et al. 2007

Cell. Mol. Life Sci.

325

267

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Galectins are a taxonomically widespread family of glycan-binding proteins, defined by at least one conserved carbohydrate-recognition domain with a canonical amino acid sequence and affinity for beta-galactosides. Because of their anti-adhesive as well as pro-adhesive extracellular functions, galectins appear to be a novel class of adhesion-modulating proteins collectively known as matricellular proteins (which include thrombospondin, SPARC, tenascin, hevin, and disintegrins). Accordingly, galectins can display de-adhesive effects when presented as soluble proteins to cells in a strong adhesive state. In this context, the de-adhesive properties of galectins should be considered as physiologically relevant as the proadhesive effects of these glycan-binding proteins. This article focuses on the roles of mammalian galectins in cell adhesion, spreading, and migration, and the crossregulation of these functions. Although careful attention should be paid when examining individual galectin functions due to overlapping distributions, these intriguing glycan-binding proteins offer promising possibilities for the treatment and intervention of a wide variety of pathological processes, including cancer, inflammation, and autoimmunity.

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Elucidation of the mechanism of interaction of sheep spleen galectin-1 with splenocytes and its role in cell-matrix adhesion

Cited by 13 publications

References 35 publications

Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering

Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering

The role of Galectin-1 in the interaction between chondrocytes and a lactose-modified chitosan

Galectins: matricellular glycan-binding proteins linking cell adhesion, migration, and survival

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