Cloning, Expression, and Chromosome Mapping of Human Galectin-7

Madsen, Peder; Rasmussen, Hanne H.; Flint, T; Gromov, Pavel; Kruse, Torben A.; Honoré, Bent; Vorum, Henrik; Celis, Julio E.

doi:10.1074/jbc.270.11.5823

Cited by 135 publications

(126 citation statements)

References 41 publications

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“…Xgalectin-Va and/or -Vb is the most abundant protein in skin (5% of the total protein) (26). In mammals, a proto-type galectin, galectin-7, is abundantly expressed in skin keratinocytes (12,37,38), but its amino acid sequence is dissimilar from that of either xgalectin-Va or -Vb. Thus, galectin(s) distributed in skin may have evolved independently in various animal species.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

confidence: 99%

Characterization of the Xenopus Galectin Family

Shoji

Nishi

Hirashima

et al. 2003

Journal of Biological Chemistry

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“…22 Galectin-7 was originally identified in the human epidermis and later found to be expressed in all types of stratified epithelial cells in the skin, tongue, esophagus, and Hassal's corpuscles in the thymus. 20,21,25 In skin keratinocytes, its expression is rapidly induced following exposure to UV irradiation in association with p53 stabilization, and an increased level of the protein was mainly found in sunburned apoptotic keratinocytes. 24 Indeed, Kuwabara et al 46 have shown that stable transfectants of Hela cells expressing galectin-7 exhibit enhanced sensitivity to apoptosis.…”

Section: Figurementioning

confidence: 99%

“…Among those genes whose expression were significantly altered, we further investigated the unexpected and strongly upregulated galectin-7. This gene, originally identified as a keratinocyte marker, 20,21 has previously been associated with the development of chemically induced mammary carcinoma 22 and is one of the 14 genes previously shown to be under the control of p53. 23 …”

Section: Introductionmentioning

confidence: 99%

Upregulation of galectin-7 in murine lymphoma cells is associated with progression toward an aggressive phenotype

et al. 2003

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We have previously shown that ICAM-1-deficient mice were resistant to lymphoma dissemination of intravenously injected 164T2 lymphoma cells. Highly aggressive variants of this cell line, however, could overcome this resistance. To discern the complex pattern of gene expression involved in the evolution of aggressiveness in lymphoma cells, we compared the transcriptome of 164T2 cells with that of their aggressive variants using cDNA arrays. We identified several genes that were differentially expressed in nonmetastatic lymphoma cells and their metastatic variants. Galectin-7, associated with the development of chemically induced mammary carcinoma, was one such gene whose expression was significantly upregulated. We showed that it was constitutively expressed in aggressive variants, at both mRNA and protein levels. Galectin-7 expression in aggressive lymphoma cells was induced upon in vivo selection in several organs, including the thymus, the spleen and kidneys. We also showed that treatment of nonaggressive lymphoma cells with 5-aza-2 0 -deoxycytidine was sufficient to induce galectin-7 gene expression. This report is the first to show that galectin-7 is expressed in aggressive lymphoma.

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“…Galectin-7 is expressed in stratified epithelial cells (8,9), but its expression is down-regulated in transformed keratinocytes and squamous cell carcinoma cells (8,10). Its gene was reported to be one of those highly induced by the tumor suppressor p53 in the human colon carcinoma cell line DLD-1, thus designated as p53-induced gene 1 (PIG1), and the protein has been suggested to play a role in the proapoptotic function of p53 (11).…”

Section: Introductionmentioning

confidence: 99%

Suppression of Tumor Growth by Galectin-7 Gene Transfer

2004

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Galectin-7 is a ␤-galactoside-binding animal lectin specifically expressed in stratified epithelia. Its expression is inducible by p53 and is down-regulated in squamous cell carcinomas. Other investigators previously showed that galectin-7 is a proapoptotic protein, and we showed that ectopic expression of galectin-7 in HeLa cells renders the cells more sensitive to a variety of apoptotic stimuli. In the present study, we showed that ectopic expression of galectin-7 in the human colon carcinoma cell line DLD-1 also made the cells more sensitive to apoptosis under various conditions. We also found that galectin-7-transfected DLD-1 (DLD-1-Gal7) cells grew significantly more slowly than control transfectants (DLD-1-V) under normal culture conditions in the absence of apoptosis. Moreover, a significantly lower number of colonies were formed from DLD-1-Gal7 cells than from DLD-1-V cells under anchorage-independent cell growth conditions. Most importantly, tumor formation from DLD-1-Gal7 cells was dramatically reduced compared with DLD-1-V cells when these cells were inoculated s.c. into severe combined immunodeficient mice. DLD-1-Gal7 tumors showed a significantly lower proliferation rate than DLD-1-V tumors as determined by in vivo 5-bromo-2-deoxyuridine incorporation. DLD-1-Gal7 tumors also contained a lower density of blood vessels than DLD-1-V tumors, suggesting that ectopic expression of galectin-7 suppresses angiogenesis. This may partially account for the greater suppressive effect of galectin-7 on tumor growth in vivo than in vitro. Our results show that galectin-7 has a suppressive effect on tumor growth, suggesting that galectin-7 gene transfer or other means of specifically inducing galectin-7 expression may be a new approach for management of cancers.

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Cloning, Expression, and Chromosome Mapping of Human Galectin-7

Cited by 135 publications

References 41 publications

Characterization of the Xenopus Galectin Family

Characterization of the Xenopus Galectin Family

Upregulation of galectin-7 in murine lymphoma cells is associated with progression toward an aggressive phenotype

Suppression of Tumor Growth by Galectin-7 Gene Transfer

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