GALECTIN-3 IS EXPRESSED IN THE NOTOCHORD, DEVELOPING BONES, AND SKIN OF THE POSTIMPLANTATION MOUSE EMBRYO

被引:76
作者
FOWLIS, D [1 ]
COLNOT, C [1 ]
RIPOCHE, MA [1 ]
POIRIER, F [1 ]
机构
[1] INST COCHIN GENET MOLEC,INSERM,U257,F-75014 PARIS,FRANCE
关键词
GALECTIN-3; MAC-2; MOUSE EMBRYOGENESIS; NOTOCHORD; CARTILAGE; EPIDERMIS;
D O I
10.1002/aja.1002030211
中图分类号
R602 [外科病理学、解剖学]; R32 [人体形态学];
学科分类号
100101 ;
摘要
The galectins are a family of low molecular weight, calcium-independent mammalian carbohydrate binding proteins that exhibit specificity for beta-galactoside derivatives. We have examined the expression pattern of galectin-3 in the developing mouse embryo by in situ hybridisation and immunohistochemistry. In the embryo proper, galectin-3 message and protein are first detected in notochord, starting from 8.5 days post coitum (dpc), and persist until this structure disappears. Galectin-3 is later found in cartilage primordia and in developing skin from 13.5 dpc. This very restricted and dynamic pattern suggests that galectin-3 may participate in the establishment and/or maintenance of notochord as well as the formation of cartilage and differentiation of skin. Finally, we find that galectin-3, which is identical to the macrophage marker Mac-2, is also expressed in embryonic macrophages. (C) 1995 Wiley-Liss, Inc.
引用
收藏
页码:241 / 251
页数:11
相关论文
共 54 条
[1]  
Akhurst R.J., Localisation of growth factor mRNA in tissue sections by in‐situ hybridisation, Growth Factors: A Practical Approach, (1993)
[2]  
Albrandt K., Orida N.K., Liu F.T., An IgE‐binding protein with a distinctive repetitive sequence and homology with an IgG receptor, Proc. Natl. Acad. Sci. U.S.A., 84, pp. 6859-6863, (1987)
[3]  
Atienza-Samols S.B., Razon-Pine P., Sherman M.I., Effects of tumicamycin upon glycoprotein synthesis and development of early mouse embryos, Dev. Biol., 79, pp. 19-32, (1980)
[4]  
Barondes S.H., Soluble lectins: A new class of extracellular proteins, Science, 223, pp. 1259-1264, (1984)
[5]  
Barondes S.H., Castronovo V., Cooper D.N.W., Cummings R.D., Drickamer K., Feizi T., Gitt M.A., Hirabayashi J., Hughes C., Kasai K., Leffler H., Liu F.T., Lotan R., Mercurio A.M., Mon-signy M., Pillai S., Poirier F., Raz A., Rigby P.W.J., Rini J.M., Galectins: A family of animal beta‐galactoside‐binding lectins, Cell, 76, pp. 597-598, (1994)
[6]  
Barondes S.H., Cooper D.N.W., Gitt M.A., Leffler H., Structure and function of a large family of animal lectins, J Biol Chem, 269, pp. 20807-20810, (1994)
[7]  
Bleil J.D., Wasserman P.M., Galactose at the non‐reducing terminus of N‐linked oligosaccharides of mouse egg ZP3 is essential for the glycoprotein's sperm receptor activity, Proc. Natl. Acad. Sci. U.S.A., 85, pp. 6778-6782, (1988)
[8]  
Cerra R.F., Gitt M.A., Barondes S., Three soluble rat beta‐galactoside‐binding‐specific lectins during foetal and neonatal rabbit development, J. Biol. Chem., 260, pp. 10474-10477, (1985)
[9]  
Cherayil B.J., Weiner S.J., Pillai S., The Mac‐2 antigen is a galactose‐specific lectin that binds IgE, J. Exp. Med., 170, pp. 1959-1972, (1989)
[10]  
Cooper D.N.W., Massa S.M., Barondes S.H., Endogenous muscle lectin inhibits myoblast adhesion to laminin, J. Cell Biol., 115, pp. 1681-1691, (1991)