Galectin‐3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo

Fowlis, Deborah; Colnot, Céline; Ripoche, Marie‐Anne; Poirier, Françoise

doi:10.1002/aja.1002030211

Cited by 72 publications

(63 citation statements)

References 53 publications

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“…Furthermore, galectin-3 influences cell growth and repair in the nervous system by promoting neural cell adhesion and neurite growth (Pesheva et al, 1998). It is expressed in the developing notochord of embryonic mice, and in the dorsal root ganglion of rats with peripheral nerve injury (Cameron et al, 1993;Fowlis et al, 1995). Because in CP, pancreatic nerves are enlarged and their perineurium is frequently damaged, galectins may also be important for the growth and injury protection of the nerves in CP.…”

Section: Discussionmentioning

confidence: 99%

Galectin-1 and Galectin-3 in Chronic Pancreatitis

Wang

Frieß

Zhu

et al. 2000

Laboratory Investigation

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SUMMARY:Galectin-1 and galectin-3 have important functions in cell-cell interactions, cell adhesion to extracellular matrix, the organization of extracellular matrix, and tissue remodeling. To assess their potential role in chronic pancreatitis (CP), we examined their expression by Northern blot analysis, in situ hybridization, immunohistochemistry, and Western blot analysis in normal and CP pancreatic tissues. Northern blot analysis revealed a 4.5-fold increase of galectin-1 mRNA (p Ͻ 0.01) and a 3.8-fold increase of galectin-3 mRNA (p Ͻ 0.01) in CP samples compared with normal controls. In situ hybridization analysis of normal pancreas indicated low abundance of galectin-1 mRNA in fibroblasts, whereas galectin-3 mRNA was moderately present in ductal cells. CP samples exhibited moderate to intense galectin-1 mRNA signals in fibroblasts, whereas galectin-3 mRNA signals were intense in the cells of ductular complexes and weak in the degenerating acinar cells. In addition, intense galectin-1 and galectin-3 mRNA signals were present in nerves of normal and CP samples. Immunohistochemistry showed a distribution pattern of galectin-1 and galectin-3 similar to that described for in situ hybridization. Relative quantification of galectin-1 and galectin-3 protein by immunoblotting revealed an increase of 3.2-fold and 3.0-fold, respectively, in CP compared with normal controls. There was a significant correlation between galectin-1 and fibrosis and between galectin-3 and fibrosis and the density of ductular complexes. Up-regulation of galectin-1 in fibroblasts and galectin-3 in ductular complexes suggests a role of these lectins in tissue remodeling in CP. Galectin-1 might participate in ECM changes, whereas galectin-3 seems to be involved in both ECM changes and ductular complex formation. (Lab Invest 2000, 80:1233-1241.

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Section: Discussionmentioning

confidence: 99%

Galectin-1 and Galectin-3 in Chronic Pancreatitis

Wang

Frieß

Zhu

et al. 2000

Laboratory Investigation

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“…It is thus clear that the expression of galectin-4 and galectin-6 is much more limited compared with galectin-1 and galectin-3, which are both expressed in many different tissues (26,27). Galectin-1 and galectin-3 are also present in intestine, but their patterns of expression differ.…”

Section: Figmentioning

confidence: 99%

“…The signal is first detected on the 13th day of embryogenesis and is then detected through adulthood. Scale bars, 700 m in A and B and 200 m in C-H. the epithelium of the adult intestine, but galectin-3 is not expressed there before birth (27). Galectin-9 is also expressed in the adult intestine but in many other tissues as well (9).…”

Section: Figmentioning

confidence: 99%

Galectin-4 and Galectin-6 Are Two Closely Related Lectins Expressed in Mouse Gastrointestinal Tract

Gitt¹,

Colnot²,

Poirier³

et al. 1998

Journal of Biological Chemistry

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Galectins are a family of carbohydrate-binding proteins that share a conserved sequence and affinity for ␤-galactosides. Some, such as galectin-1, are isolated as dimers and have a single carbohydrate recognition domain (CRD) in each monomer, whereas others, such as galectin-4, are isolated as monomers and have two CRDs in a single polypeptide chain. In the course of studying mouse colon mRNA for galectin-4, we detected a related mRNA that encodes a new galectin that also has two CRDs in a single peptide chain. The new galectin, galectin-6, lacks a 24-amino acid stretch in the link region between the two CRDs that is present in galectin-4. Otherwise, these two galectins have 83% amino acid identity. Expression of both galectin-4 and galectin-6 is confined to the epithelial cells of the embryonic and adult gastrointestinal tract. Galectin-4 is expressed at about equal levels in colon and small intestine but much less in stomach, whereas galectin-6 is expressed at about equal levels throughout the gastrointestinal tract.

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“…The expression of some members is temporally and spatially regulated during embryogenesis (13)(14)(15)(16); galectin-1 regulates the axonal growth of neural cells in mouse and rat (17)(18)(19); a proto-type galectin of chicken affects the differentiation of cultured mesonephroi (20); a null mutant mouse of galectin-3 has subtle but significant defects in bones and inflammatory responses (21)(22)(23), etc. Other evidence that galectins might contribute to developmental regulation has been obtained for Xenopus.…”

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confidence: 99%

Characterization of the Xenopus Galectin Family

Shoji

Nishi

Hirashima

et al. 2003

Journal of Biological Chemistry

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We have isolated six novel galectin cDNAs from a Xenopus laevis kidney cDNA library. The newly identified X. laevis galectins (xgalectins) comprise one proto type (xgalectin-Vb), one chimera type (xgalectin-VIIa), and four tandem repeat types (xgalectin-IIb, -IIIb, -VIa, and -VIIIa). Thus, together with those mentioned in our previous work (Shoji, H., Nishi, N., Hirashima, M., and Nakamura, T. (2002) Glycobiology 12, 163-172), the 12 xgalectins are classified into three types based on their domain structures, as in mammals. The xgalectins whose counterparts in other species have not been identified (xgalectin-IVa, -Vb, and -VIa) were confirmed to possess lactose-binding activity by expression of their recombinant forms. This shows that they truly function as animal lectins. The protein purification study revealed that the major xgalectins in kidney are xgalectinIb, -IIa, -IIb, -IIIa, and -VIIa. The mRNAs of xgalectin-IIb, -IIIb, -Vb, and -VIa were localized to specific adult tissues, whereas those of xgalectin-VIIa and -VIIIa were broadly distributed. The temporal expression patterns of the mRNAs of the 12 xgalectins during embryogenesis were analyzed and categorized into three groups: 1) mRNA observed to exist throughout embryogenesis, i.e. maternal mRNA also exists (xgalectin-Ia, -IIa, -IIIa, -IIIb, -Va, -VIIa, and -VIIIa); 2) mRNA observed from the gastrula stage (xgalectin-VIa); and 3) mRNA observed from the tail bud or the tadpole stage (xgalectin-Ib, -IIb, -IVa, and -Vb). The mRNA of the most abundant xgalectin in embryos, xgalectin-VIIa, was localized to the surface layer of embryos, the epidermis, the cement gland, and various placodes. Xgalectin-VIIa protein was also observed to exist throughout embryogenesis by Western blot analysis with specific antiserum. These results show that the expression of each member is spatiotemporally regulated from eggs to adulthood, suggesting that galectins play multiple roles not only in adults, but also in development.Galectins comprise a family of animal lectins that bind to ␤-galactoside-containing carbohydrate moieties of glycoconjugates (1, 2). Fourteen galectins have been isolated from mammals and are classified into the proto, chimera, and tandem repeat types based on their structures (3-8). Proto-type galectins contain one carbohydrate recognition domain (CRD), 1 a structurally conserved domain that specifically recognizes a ␤-galactoside-containing carbohydrate; and chimera-type galectins consist of one CRD and an N-terminal elongating protein domain. Mammalian galectin-1 (proto type) and -3 (chimera type) are the most extensively studied galectins (9). They have been proposed to play roles in tissue organization, development, immunity, and cancer growth and metastasis by regulating such processes as cell adhesion and apoptosis. Tandem repeat-type galectins contain two CRDs covalently linked through a unique link peptide. Tandem repeat-type galectins are less well understood, but they have been shown to be expressed in a tissue-specific manner in adult animals ...

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Galectin‐3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo

Cited by 72 publications

References 53 publications

Galectin-1 and Galectin-3 in Chronic Pancreatitis

Galectin-1 and Galectin-3 in Chronic Pancreatitis

Galectin-4 and Galectin-6 Are Two Closely Related Lectins Expressed in Mouse Gastrointestinal Tract

Characterization of the Xenopus Galectin Family

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