Cloning and characterization of a sialic acid binding lectins (SABL) from Manila clam Venerupis philippinarum

The cellular glycocalyx of vertebrates is frequently decorated with sialic acid residues. These sialylated structures are recognized by sialic acid-binding immunoglobulin-type lectins (Siglecs) of immune cells, which modulate their responsiveness. Fifteen Siglecs are known to be expressed in humans, but only four Siglecs are regularly present in fish: Siglec1, CD22, myelin-associated glycoprotein (MAG), and Siglec15. While several studies have dealt with the physiological roles of these four Siglecs in mammals, little is known about Siglecs in fish. In the present manuscript, the expression landscapes of these Siglecs were determined in the two salmonid species Oncorhynchus mykiss and Coregonus maraena and in the percid fish Sander lucioperca. This gene-expression profiling revealed that the expression of MAG is not restricted to neuronal cells but is detectable in all analyzed blood cells, including erythrocytes. The teleostean MAG contains the inhibitory motif ITIM; therefore, an additional immunomodulatory function of MAG is likely to be present in fish. Besides MAG, Siglec1, CD22, and Siglec15 were also expressed in all analyzed blood cell populations. Interestingly, the expression profiles of genes encoding Siglecs and particular associated enzymes changed in a gene- and tissue-specific manner when Coregonus maraena was exposed to handling stress. Thus, the obtained data indicate once more that stress directly affects immune-associated processes.

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Molecular characterization of limulin, a sialic acid binding lectin from the hemolymph of the horseshoe crab, Limulus polyphemus

Biochemistry ◽

10.1021/bi00638a026 ◽

1977 ◽

Vol 16 (19) ◽

pp. 4297-4303 ◽

Cited By ~ 38

Author(s):

Ruth Kaplan ◽

Steven S. L. Li ◽

J. Michael Kehoe

Keyword(s):

Sialic Acid ◽

Molecular Characterization ◽

Horseshoe Crab ◽

Limulus Polyphemus ◽

Sialic Acid Binding ◽

Binding Lectin

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Cloning and Characterization of Siglec-10, a Novel Sialic Acid Binding Member of the Ig Superfamily, from Human Dendritic Cells

Journal of Biological Chemistry ◽

10.1074/jbc.m100467200 ◽

2001 ◽

Vol 276 (30) ◽

pp. 28106-28112 ◽

Cited By ~ 62

Author(s):

Nan Li ◽

Weiping Zhang ◽

Tao Wan ◽

Jia Zhang ◽

Taoyong Chen ◽

...

Keyword(s):

Dendritic Cells ◽

Sialic Acid ◽

Sialic Acid Binding ◽

Ig Superfamily ◽

Human Dendritic Cells

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Further characterization of the sialic acid-binding lectin from the horseshoe crab Carcinoscorpius rotunda cauda

Archives of Biochemistry and Biophysics ◽

10.1016/0003-9861(81)90288-5 ◽

1981 ◽

Vol 209 (1) ◽

pp. 325-333 ◽

Cited By ~ 23

Author(s):

D.Thambi Dorai ◽

B.K. Bachhawat ◽

S. Bishayee ◽

K. Kannan ◽

D.Rajagopal Rao

Keyword(s):

Sialic Acid ◽

Horseshoe Crab ◽

Sialic Acid Binding ◽

Binding Lectin

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Characterization of Siglec-5, a Novel Glycoprotein Expressed on Myeloid Cells Related to CD33

Blood ◽

10.1182/blood.v92.6.2123 ◽

1998 ◽

Vol 92 (6) ◽

pp. 2123-2132 ◽

Cited By ~ 116

Author(s):

Ann L. Cornish ◽

Sylvie Freeman ◽

Gareth Forbes ◽

Jian Ni ◽

Mei Zhang ◽

...

Keyword(s):

Sialic Acid ◽

Leukemic Cell ◽

Immunoglobulin Superfamily ◽

Tyrosine Residues ◽

Cos Cells ◽

Leukemic Cell Lines ◽

Sialic Acid Binding ◽

Human Igg1 ◽

American Society

Abstract We describe the characterization of siglec-5 (sialic acid-binding Ig-like lectin-5), a novel transmembrane member of the immunoglobulin superfamily, highly related to the myeloid antigen, CD33. A full-length cDNA encoding siglec-5 was isolated from a human activated monocyte cDNA library. Sequencing predicted that siglec-5 contains four extracellular immunoglobulin-like domains, the N-terminal two of which are 57% identical to the corresponding region of CD33. The cytoplasmic tail is also related to that of CD33, containing two tyrosine residues embodied in immunoreceptor tyrosine-based inhibitory motif-like motifs. The siglec-5 gene was shown to map to chromosome 19q13.41-43, closely linked to the CD33 gene. When siglec-5 was expressed on COS cells or as a recombinant protein fused to the Fc region of human IgG1, it was able to mediate sialic acid–dependent binding to human erythrocytes and soluble glycoconjugates, suggesting that it may be involved in cell-cell interactions. By using specific antibodies, siglec-5 was found to have an expression pattern distinct from that of CD33, being present at relatively high levels on neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation. Western blot analysis of neutrophil lysates indicated that siglec-5 exists as a disulfide-linked dimer of approximately 140 kD. © 1998 by The American Society of Hematology.

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