Identification of cells expressing galectin‐1, a galactose‐binding receptor, in the rat olfactory system

Puche, A.C.; Key, Brian

doi:10.1002/cne.903570403

Cited by 52 publications

(35 citation statements)

References 39 publications

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“…The results observed on adult rat olfactory bulb sections confirm the information previously reported by Puche and Key, 1995. The specificity of the mAb was strengthened by the superposable staining patterns obtained by mAb and cRNA probe.…”

Section: Discussionsupporting

confidence: 80%

Production and characterization of a monoclonal antibody able to discriminate galectin-1 from galectin-2 and galectin-3

Cornillot¹,

Pontet²,

Dupuy

et al. 1998

Glycobiology

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Antisera raised against galectin-1 exhibit crossreactivities with other galectins or related molecules. In order to overcome this problem, a monoclonal antibody to human brain galectin-1 was obtained by selecting clones without reactivity toward galectin-3. This mAb specifically bound galectin-1 of various animal origins but neither galectin-2 nor galectin-3. Westernblotting analysis of soluble human brain extracts after 2D gel electrophoresis revealed only the two most acidic isoforms of galectin-1. The ability of this mAb to bind galectin-1/asialofetuin complexes indicates that its epitope is not localized in the carbohydrate recognition domain of galectin-1. This particularity induces with efficiency its monospecificity.

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Section: Discussionsupporting

confidence: 80%

Production and characterization of a monoclonal antibody able to discriminate galectin-1 from galectin-2 and galectin-3

Cornillot¹,

Pontet²,

Dupuy

et al. 1998

Glycobiology

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“…Galectin-1 mRNA becomes abundant in sensory neurons and motoneurons in the spinal cord and brainstem soon after neuronal differentiation [23]. Galectin-1 is also expressed in the developing brain [26] and olfactory system [25,27]. It has also been proposed to function as a lectin in neuronal pathfinding [27], contributing to fasciculation or the guidance of axons by acting as a substrate.…”

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confidence: 99%

Oxidized galectin-1 promotes axonal regeneration in peripheral nerves but does not possess lectin properties

Inagaki¹,

Sohma²,

Horie³

et al. 2000

Eur J Biochem

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Galectin-1 has recently been identified as a factor that regulates initial axonal growth in peripheral nerves after axotomy. Although galectin-1 is a well-known b-galactoside-binding lectin, its potential to promote axonal regeneration as a lectin has not been reported. It is essential that the process of initial repair in peripheral nerves after axotomy is well clarified. We therefore undertook to investigate the relation between the structure and axonal regeneration-promoting activity of galectin-1. Recombinant human galectin-1 secreted into the culture supernatant of transfected COS1 cells (rhGAL-1/COS1) was purified under nonreducing conditions and subjected to structural analysis. Mass spectrometric analysis of peptide fragments from rhGAL-1/COS1 revealed that the secreted protein exists as an oxidized form containing three intramolecular disulfide bonds (Cys2±Cys130, Cys16±Cys88 and Cys42±Cys60). Recombinant human galectin-1 (rhGAL-1) and a galectin-1 mutant in which all six cysteine residues were replaced by serine (CSGAL-1) were expressed in and purified from Escherichia coli for further analysis; the purified rhGAL-1 was subjected to oxidation, which induced the same pattern of disulfide linkages as that observed in rhGAL-1/COS1. Oxidized rhGAL-1 enhanced axonal regeneration from the transected nerve sites of adult rat dorsal root ganglion explants with associated nerve stumps (5.0±5000 pg´mL 21 ), but it lacked lectin activity. In contrast, CSGAL-1 induced hemagglutination of rabbit erythrocytes but lacked axonal regeneration-promoting activity. These results indicate that galectin-1 promotes axonal regeneration only in the oxidized form containing three intramolecular disulfide bonds, not in the reduced form which exhibits lectin activity.Keywords: axonal regeneration; dorsal root ganglion; lectin; oxidized galectin-1; structure/activity relationship.Successful nerve regeneration requires the concerted interplay of non-neuronal cells, growth factors, cell adhesion molecules, extracellular matrix materials, regenerating axons and recruiting macrophages [1±3]. However, although various neurotrophins have been investigated to promote axonal regeneration in vivo, it is still unclear what factor initiates axonal regeneration response to nerve injury. We found one of these factors from the culture supernatant of COS1 cells in a previous study [4]. The factor enhanced axonal regeneration in the in vitro nerve regeneration model employed, allowing for initial axon outgrowth from the proximal nerve stump to be monitored, which is comparable with the initial stages of nerve repair. Analysis of the purified protein indicated that it was identical to galectin-1. Recombinant human galectin-1 (rhGAL-1) confirmed that the protein promotes axonal regeneration not only in the in vitro experiment, but also in two other types of in vivo acellular nerve regeneration model. Furthermore, antibodies to galectin-1 clearly inhibited axonal regeneration in vivo as well as in vitro. These observations suggest that galectin-1 mi...

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“…Sense and antisense cRNA were synthesized in vitro from linearized pGEM plasmids using T7 and SP6 polymerases and a transcription system kit (Promega) according to the manufacturer's instructions with additional modifications (21). Staining was visualized using diaminobenzidine and cultures were temporarily coverslipped for counting.…”

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confidence: 99%

Lineage specification of neuronal precursors in the mouse spinal cord.

Richards

Murphy

Dutton

et al. 1995

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

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We have investigated the differentiation potential of precursor cells within the developing spinal cord of mice and have shown that spinal cord cells from embryonic day 10 specifically give rise to neurons when plated onto an astrocytic monolayer, Ast-1. These neurons had the morphology of motor neurons and >83% expressed the motor neuron markers choline acetyltransferase, peripherin, calcitonin gene-related peptide, and L-14. By comparison, <10%o of the neurons arising on monolayers ofother neural cell lines or 3T3 fibroblasts had motor neuron characteristics. Cells derived from dorsal, intermediate, and ventral regions of the spinal cord all behaved similarly and gave rise to motor neuron-like cells when plated onto Ast-1. By using cells that expressed the lacZ reporter gene, it was shown that >93% of cells present on the Ast-1 monolayers were motor neuron-like. Time-lapse analysis revealed that the precursors on the Ast-1 monolayers gave rise to neurons either directly or following a single cell division. Together, these results indicate that precursors in the murine spinal cord can be induced to differentiate into the motor neuron phenotype by factors produced by Ast-I cells, suggesting that a similar factor(s) produced by cells akin to Ast-1 may regulate motor neuron differentiation in vivo.The induction of motor neurons in the spinal cord, one of the first neurons to arise developmentally (1-3), is influenced by epigenetic factors. It has been shown in the chicken that neuronal differentiation (4, 5), and later motor neuron differentiation (6, 7) in the spinal cord, can be regulated by the notochord. Further, conditioned medium from the notochord and floor plate can stimulate motor neuron differentiation in the intermediate zone, a region that does not normally give rise to motor neurons (8). These findings suggest that soluble factors within notochord conditioned medium are responsible for the motor neuron-inducing activity. In addition, these results suggest that precursor cells within the chicken spinal cord are not committed to any particular neuronal pathway. To examine the potential of individual precursors within the spinal cord, and to determine the direct effect of factors on the precursors, we have developed an in vitro assay in which the differentiation of individual precursors from the mouse spinal cord could be monitored.MATERIALS AND METHODS Cell Culture. All mice used in these experiments were of the CBA/CaWEHI strain except for transgenic mice, which were Bl/6 x DBA/2 hybrids (F6). The transgenic mice (line H253) contained a lacZ gene insertion (9). Mice heterozygous for the transgene were mated and embryos containing the lacZ transgene were identified by the 5-bromo-4-chloro-3-indolyl P3-Dgalactoside histochemistry (10) of biopsied material. Spinal cord cells from embryonic day 10 (E10) to E16 mice, where EO was the day a vaginal plug was detected, were prepared as described (11,12).Astrocytes were derived from E18 spinal cord as described (13); in addition, the cells were passed t...

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Identification of cells expressing galectin‐1, a galactose‐binding receptor, in the rat olfactory system

Cited by 52 publications

References 39 publications

Production and characterization of a monoclonal antibody able to discriminate galectin-1 from galectin-2 and galectin-3

Production and characterization of a monoclonal antibody able to discriminate galectin-1 from galectin-2 and galectin-3

Oxidized galectin-1 promotes axonal regeneration in peripheral nerves but does not possess lectin properties

Lineage specification of neuronal precursors in the mouse spinal cord.

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