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Target Concepts:
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Query: UNIPROT:P17931 (
galectin-3
)
2,860
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
In previous studies, we documented that
galectin-3
(M(r) approximately 30,000) is a pre-mRNA splicing factor. Recently,
galectin-3
was identified as a component of a nuclear and cytoplasmic complex, the survival of motor neuron complex, through its interaction with Gemin4. To test the possibility that
galectin-3
may shuttle between the nucleus and the cytoplasm, human fibroblasts (LG-1) were fused with mouse fibroblasts (3T3). The monoclonal antibody
NCL
-GAL3, which recognizes human
galectin-3
but not the mouse homolog, was used to monitor the localization of human
galectin-3
in heterodikaryons. Human
galectin-3
localized to both nuclei of a large percentage of heterodikaryons. Addition of the antibiotic leptomycin B, which inhibits nuclear export of
galectin-3
, decreased the percentage of heterodikaryons showing human
galectin-3
in both nuclei. In a parallel experiment, mouse 3T3 fibroblasts, which express
galectin-3
, were fused with fibroblasts derived from a mouse in which the
galectin-3
gene was inactivated. Mouse
galectin-3
localized to both nuclei of a large percentage of heterodikaryons. Again, addition of leptomycin B restricted the presence of
galectin-3
to one nucleus of a heterodikaryon. The results from both heterodikaryon assays suggest that
galectin-3
can exit one nucleus, travel through the cytoplasm, and enter the second nucleus, matching the definition of shuttling.
...
PMID:Shuttling of galectin-3 between the nucleus and cytoplasm. 1207 75
Previous experiments had established that
galectin-3
(Gal3) is a factor involved in cell-free splicing of pre-mRNA. Addition of monoclonal antibody
NCL
-GAL3, whose epitope maps to the NH2-terminal 14 amino acids of Gal3, to a splicing-competent nuclear extract inhibited the splicing reaction. In contrast, monoclonal antibody anti-
Mac-2
, whose epitope maps to residues 48-100 containing multiple repeats of a 9-residue motif PGAYPGXXX, had no effect on splicing. Consistent with the notion that this region bearing the PGAYPGXXX repeats is sequestered through interaction with the splicing machinery and is inaccessible to the anti-
Mac-2
antibody, a synthetic peptide containing three perfect repeats of the sequence PGAYPGQAP (27-mer) inhibited the splicing reaction, mimicking a dominant-negative mutant. Addition of a peptide corresponding to a scrambled sequence of the same composition (27-mer-S) failed to yield the same effect. Finally, GST-hGal3(1-100), a fusion protein containing glutathione-S-transferase and a portion of the Gal3 polypeptide including the PGAYPGXXX repeats, also exhibited a dominant-negative effect on splicing.
...
PMID:Distinct effects on splicing of two monoclonal antibodies directed against the amino-terminal domain of galectin-3. 1845 93