Unique sequence and expression profiles of rat galectins-5 and -9 as a result of species-specific gene divergence

Lensch, M. William; Lohr, Michaela; Russwurm, Roland; Vidal, Michel; Kaltner, Herbert; André, Sabine; Gabius, Hans‐Joachim

doi:10.1016/j.biocel.2006.04.004

Cited by 47 publications

(35 citation statements)

References 64 publications

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“…Anti-galectin-2, -4, and -5 antibodies were raised against recombinant proteins and controlled for specificity and absence of cross-reactivity by enzyme-linked immunosorbent assay and Western blotting. 28,36 To generate polyclonal antiserum, a rabbit was immunized with galectin-5 purified from rat erythrocytes as described in the next section. Anti-galectin-5 antibody was purified from the serum by affinity chromatography by the use of recombinant galectin-5, tagged with glutathione-S-transferase (GSTGal-5) immobilized on glutathione-Sepharose beads (GE Healthcare).…”

Section: Antibodiesmentioning

confidence: 99%

“…12,16 Galectin-5 stands out from the group of prototype galectins because of its exceptionally low propensity for dimer formation in the absence of multivalent ligands and its strict cell-type-specific expression pattern. 28,29 Furthermore, the galectin-5 gene has exclusively been found in rat, likely resulting from duplication of an ancestral gene encoding for the C-terminal domain of galectin-9. 28,30 Considering these features, it was of interest to investigate the functional relevance of this rat-specific galectin expression, which will then prompt respective analysis in other mammals.…”

Section: Introductionmentioning

confidence: 99%

“…28,29 Furthermore, the galectin-5 gene has exclusively been found in rat, likely resulting from duplication of an ancestral gene encoding for the C-terminal domain of galectin-9. 28,30 Considering these features, it was of interest to investigate the functional relevance of this rat-specific galectin expression, which will then prompt respective analysis in other mammals. We show in this study that galectin-5, although mainly cytosolic, is also present on the cell surface of reticulocytes and mature red cells.…”

Section: Introductionmentioning

confidence: 99%

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Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages

Barrès

Blanc

Bette‐Bobillo

et al. 2010

Blood

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Reticulocytes release small membrane vesicles termed exosomes during their maturation into erythrocytes. Exosomes are intraluminal vesicles of multivesicular endosomes released into the extracellular medium by fusion of these endosomal compartments with the plasma membrane. This secretion pathway contributes to reticulocyte plasma membrane remodeling by eliminating certain membrane glycoproteins. We show in this study that galectin-5, although mainly cytosolic, is also present on the cell surface of rat reticulocytes and erythrocytes. In addition, in reticulocytes, it resides in the endosomal compartment. We document galectin-5 translocation from the cytosol into the endosome lumen, leading to its secretion in association with exosomes. Galectin-5 bound onto the vesicle surface may function in sorting galactosebearing glycoconjugates. Fittingly, we found that Lamp2, a major cellular glycoprotein presenting galectin-reactive poly-N-acetylactosamine chains, is lost during reticulocyte maturation. It is associated with released exosomes, suggestive of binding to galectin-5. Finally, we reveal that the uptake of rat reticulocyte exosomes by macrophages is dependent on temperature and the mechanoenzyme dynamin and that exosome uptake is decreased by adding galectin-5. These data imply galectin-5 functionality in the exosomal sorting pathway during rat reticulocyte maturation. (Blood. 2010;115: 696-705) IntroductionExosomes are membrane vesicles secreted by various cells and represent intraluminal vesicles of multivesicular endosomes (MVEs) released into the extracellular medium upon fusion of MVE with the plasma membrane. 1 Exosomal release during reticulocyte maturation is part of a cellular program resulting in remodeling of the plasma membrane by removal of a distinct set of (glyco)proteins. 2 We have previously shown that exosomal segregation of internalized membrane (glyco)proteins can occur by different routes, such as a natural enrichment in membrane domains (eg, lipid rafts), 3 antibody-or lectin-induced clustering on the cell surface, 4 or via the endosomal sorting complex required for transport (ie, ESCRT) cytosolic machinery. 5 During an earlier stage of mammalian erythroid differentiation, ie, when the erythroblast expels its nucleus, some components of the erythroblast plasma membrane are already specifically sorted to either the nascent reticulocyte or the expelled nucleus. For example, it has been shown by the use of mouse erythroblasts that proteins such as erythroblast-macrophage protein and ␤1-integrin partitioned predominantly to the plasma membrane surrounding the expelled nucleus, whereas glycophorin A localized to the plasma membrane of the nascent reticulocyte. 6 Both erythroblastmacrophage protein and ␤1-integrin have been identified as adhesion molecules involved in erythroblast retention by central macrophages within erythroblastic islands. [7][8][9] Thus, it has been suggested that their segregation to expelled nuclei favors their engulfment by macrophages while enabling reticulocytes to de...

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Section: Antibodiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages

Barrès

Blanc

Bette‐Bobillo

et al. 2010

Blood

Self Cite

254

211

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“…In rats, the Lgals5 gene derives from a recent duplication of the Lgals9 gene (Houzelstein et al 2004). As for the Lgals4/ Lgals6 genes, the deletion of a large part of one of the duplicates (i.e., Lgals5) seems to be associated with subsequent asymmetrical divergence (Lensch et al 2006) as well as a positive d N /d S (our unpublished data). These data suggest that positive selection has also been involved in their evolution.…”

Section: Discussionmentioning

confidence: 78%

Lgals6, a 2-Million-Year-Old Gene in Mice: A Case of Positive Darwinian Selection and Presence/Absence Polymorphism

et al. 2008

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Duplications of genes are widely considered to be a driving force in the evolutionary process. The fate of such duplicated genes (paralogs) depends mainly on the early stages of their evolution. Therefore, the study of duplications that have already started to diverge is useful to better understand their evolution. We present here the example of a 2-million-year-old segmental duplication at the origin of the Lgals4 and Lgals6 genes in the mouse genome. We analyzed the distribution of these genes in samples from 110 wild individuals and wild-derived inbred strains belonging to eight mouse species from Mus (Coelomys) pahari to M. musculus and 28 laboratory strains. Using a maximum-likelihood method, we show that the sequence of the Lgals6 gene has evolved under the influence of strong positive selection that is likely to result in its neofunctionalization. Surprisingly, despite this selection pressure, the Lgals6 gene is present in some mouse species, but not all. Furthermore, even within the species and populations where it is present, the Lgals6 gene is never fixed. To explain this paradox, we propose different hypotheses such as balanced selection and neutral retention of ancient polymophism and we discuss this unexpected result with regard to known galectin properties and response to infections by pathogens.

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“…The human galectins (homodimeric proto-type galectins-1, -2, and -7; chimera-type galectin-3; tandem-repeat-type galectins-4, -8, and -9) and rat monomeric proto-type galectin-5 (closely related to the C-terminal lectin domain of galectin-9) were purified after recombinant production under optimal conditions by affinity chromatography on lactosylated Sepharose 4B, obtained after divinyl sulfone activation, as crucial step, and routinely checked for purity and correct quaternary structure by one-and two-dimensional gel electrophoresis, nanoelectrospray ionization mass spectrometry, and gel filtration (22)(23)(24)(25)(26). Galectin-3 was further exposed to collagenase treatment to completely remove its N-terminal stalk region by proteolytic truncation, as ascertained by gel electrophoresis (27).…”

Section: Purification and Biotinylation Of Galectinsmentioning

confidence: 99%

Human galectins as sensors for apoptosis/necrosis‐associated surface changes of granulocytes and lymphocytes

et al. 2008

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Changes in the glycomic profile can significantly affect the cells' communication with the environment. Plant lectins have so far been used to address the issue as to whether the courses of apoptosis or necrosis are associated with such alterations. We, here, initiate the study of members of the family of functionally pleiotropic human galectins in this respect. Established protocols for the induction of apoptosis/necrosis of blood cells and for flow cytometry using annexin V/propidium iodide were combined with cell surface staining using biotinylated galectins at a nontoxic concentration. The galectin panel covered members from all three subfamilies. Flow cytometry revealed specific binding of galectins to viable control cells and conspicuous staining differences when testing apoptotic or necrotic cells. Onset and especially progression of cell death led to pronounced reactivity with the proto-type galectins-1, -2, and -7 and tandem-repeattype galectin-4. Extent of staining depended on the nature and stage of cell death, type of dying cell, and type of galectin. Galectins act as sensors for cell-death-associated surface changes. Staining of late-apoptotic polymorphonuclear cells was particularly strong. Examining the functional significance of this result may reveal a new aspect within the surveillance system to protect against autoinflammation. ' 2008 International Society for Analytical Cytology Key terms apoptosis; flow cytometry; galectin; glycosylation; lectin; necrosis; phagocytosis; sialylation THE safe disposal of apoptotic and necrotic cell material will limit the hazard to develop autoimmunity (1). In its initial phase, endogenous safeguard systems trace biochemical deviations on the cell surface, which signal the onset of cell death. Consecutive steps toward late stages are accompanied by further surface alterations. They are supposed to mark dying cells for elimination but their biochemical nature is not yet fully characterized. To explain efficient clearance, probing into distinct surface characteristics is a means to delineate operative routes of dying-self recognition. That said that the analysis of cell surface glycans is an obvious choice, because the glycomic profile is known to undergo disease-associated changes and to present a large panel of sugar-encoded signals to the environment (2-4). Using plant lectins as marker for glycan determinants (5), the hypothesis that their profile and/or mode of presentation are altered by cell death was already tested, and changes of lectin binding to dying and dead leukemic cells had been reported (6-9). These results obtained with plant proteins support the concept that glycan recognition by endogenous receptors can figure as a way to identify and clear nonviable cells. Focusing on spatially accessible branch-end determinants of glycan antennae, case studies with hepatic, and macrophage C-type asialoglycoprotein receptors already illustrated their

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Unique sequence and expression profiles of rat galectins-5 and -9 as a result of species-specific gene divergence

Cited by 47 publications

References 64 publications

Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages

Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages

Lgals6, a 2-Million-Year-Old Gene in Mice: A Case of Positive Darwinian Selection and Presence/Absence Polymorphism

Human galectins as sensors for apoptosis/necrosis‐associated surface changes of granulocytes and lymphocytes

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