Sialoadhesin - Revision history

S�rge Kelm: /* Biosynthesis of ligands */

2012-01-27T21:02:38Z

Biosynthesis of ligands

S�rge Kelm: /* Biosynthesis of ligands */

2012-01-27T20:57:36Z

Biosynthesis of ligands

S�rge Kelm: /* Biosynthesis of ligands */

2012-01-27T18:29:43Z

Biosynthesis of ligands

S�rge Kelm: /* Biosynthesis of ligands */

2012-01-27T18:27:56Z

Biosynthesis of ligands

S�rge Kelm at 18:22, 27 January 2012

2012-01-27T18:22:18Z

S�rge Kelm: /* Biosynthesis of ligands */

2012-01-27T18:20:04Z

Biosynthesis of ligands

S�rge Kelm at 18:15, 27 January 2012

2012-01-27T18:15:35Z

S�rge Kelm: /* Biosynthesis of ligands */

2012-01-27T18:03:41Z

Biosynthesis of ligands

Anna Crie: /* Acknowledgements */

2012-01-21T05:48:39Z

Acknowledgements

Carole Weaver at 23:30, 30 March 2011

2011-03-30T23:30:48Z

@@ Line 18: / Line 18: @@
 === Biosynthesis of ligands ===
-Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans.<ref name="Crocker1991">Crocker PR, Kelm S, Dubois C, Martin B, McWilliam AS, Shotton DM, Paulson JC, Gordon S. (1991) Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages. EMBO J. 1991, 10, 1661-1669</ref> <ref name="Kelm1994">S. Kelm, A. Pelz, R. Schauer, M. T. Filbin, S. Tang, M.-E. de Bellard, R. L. Schnaar, J. A. Mahoney, A. Hartnell, P. Bradfield, P. R. Crocker (1994) Sialoadhesin, MAG and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. Curr. Biol. 4, 965-972</ref> Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Neu5Ac hydroxylase ''O''-acetyltransferases or sialate esterases, negtively control the biosynthesis of ligands for Sialoadhesin.<ref name="Kelm1994a">Kelm S, Schauer R, Manuguerra JC, Gross HJ, Crocker PR. (1994)Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22.Glycoconj J. 1994 11, 576-85</ref> <ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>
+Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans.<ref name="Crocker1991">Crocker PR, Kelm S, Dubois C, Martin B, McWilliam AS, Shotton DM, Paulson JC, Gordon S. (1991) Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages. EMBO J. 1991, 10, 1661-1669</ref> <ref name="Kelm1994">S. Kelm, A. Pelz, R. Schauer, M. T. Filbin, S. Tang, M.-E. de Bellard, R. L. Schnaar, J. A. Mahoney, A. Hartnell, P. Bradfield, P. R. Crocker (1994) Sialoadhesin, MAG and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. Curr. Biol. 4, 965-972</ref> Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Neu5Ac hydroxylase ''O''-acetyltransferases or 9-''O''-acetylsialate esterases, negtively control the biosynthesis of ligands for Sialoadhesin.<ref name="Kelm1994a">Kelm S, Schauer R, Manuguerra JC, Gross HJ, Crocker PR. (1994)Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22.Glycoconj J. 1994 11, 576-85</ref> <ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>
 <br>

@@ Line 18: / Line 18: @@
 === Biosynthesis of ligands ===
-Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans. Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Neu5Ac hydroxylase ''O''-acetyltransferases or sialate esterases, negtively control the biosynthesis of ligands for Sialoadhesin.<ref name="Kelm1994a"">Kelm S, Schauer R, Manuguerra JC, Gross HJ, Crocker PR. (1994)Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22.Glycoconj J. 1994 11, 576-85</ref> <ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>
+Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans.<ref name="Crocker1991">Crocker PR, Kelm S, Dubois C, Martin B, McWilliam AS, Shotton DM, Paulson JC, Gordon S. (1991) Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages. EMBO J. 1991, 10, 1661-1669</ref> <ref name="Kelm1994">S. Kelm, A. Pelz, R. Schauer, M. T. Filbin, S. Tang, M.-E. de Bellard, R. L. Schnaar, J. A. Mahoney, A. Hartnell, P. Bradfield, P. R. Crocker (1994) Sialoadhesin, MAG and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. Curr. Biol. 4, 965-972</ref> Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Neu5Ac hydroxylase ''O''-acetyltransferases or sialate esterases, negtively control the biosynthesis of ligands for Sialoadhesin.<ref name="Kelm1994a">Kelm S, Schauer R, Manuguerra JC, Gross HJ, Crocker PR. (1994)Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22.Glycoconj J. 1994 11, 576-85</ref> <ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>
 <br>

@@ Line 18: / Line 18: @@
 === Biosynthesis of ligands ===
-Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans. Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Neu5Ac hydroxylase<ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>, negtively control the biosynthesis of ligands for Sialoadhesin.<ref name="Kelm1994a"">Kelm S, Schauer R, Manuguerra JC, Gross HJ, Crocker PR. (1994)Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22.Glycoconj J. 1994 11, 576-85
+Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans. Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Neu5Ac hydroxylase ''O''-acetyltransferases or sialate esterases, negtively control the biosynthesis of ligands for Sialoadhesin.<ref name="Kelm1994a"">Kelm S, Schauer R, Manuguerra JC, Gross HJ, Crocker PR. (1994)Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22.Glycoconj J. 1994 11, 576-85</ref> <ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>
 <br>

@@ Line 18: / Line 18: @@
 === Biosynthesis of ligands ===
-Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans. Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Ne5Ac hydroxylase<ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>, negtively control the biosynthesis of ligands for Sialoadhesin.
+Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans. Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Neu5Ac hydroxylase<ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>, negtively control the biosynthesis of ligands for Sialoadhesin.<ref name="Kelm1994a"">Kelm S, Schauer R, Manuguerra JC, Gross HJ, Crocker PR. (1994)Modifications of cell surface sialic acids modulate cell adhesion mediated by sialoadhesin and CD22.Glycoconj J. 1994 11, 576-85
 <br>

@@ Line 18: / Line 18: @@
 === Biosynthesis of ligands ===
-Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans. Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Ne5Ac hydroxylase<ref name"Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>, negtively control the biosynthesis of ligands for Sialoadhesin.<ref name"Crocker1998">May, AP, Robinson, RC, Vinson, M, Crocker, PR and Jones, EY (1998) Crystal structure of the N-terminal domain of sialoadhesin in complex with 3  sialyllactose at 1.85 Å Resolution. Molecular Cell 1, 719-728</ref>
+Due to the relatively wide specificity of Sialoadhesin, several enzymes can synthezise suitable glycans. Of particular importance are 2,3-sialyltransferases sialylating ''N''- and ''O''-glycans. Furthermore, it is important to note that sialic acid modifying enzymes, such as CMP-Ne5Ac hydroxylase<ref name="Brinkman-Van der Linden2000">Brinkman-Van der Linden EC, Sjoberg ER, Juneja LR, Crocker PR, Varki N, Varki A. (2000) Loss of N-glycolylneuraminic acid in human evolution. Implications for sialic acid recognition by siglecs. J. Biol. Chem. 2000, 275, 8633-8640</ref>, negtively control the biosynthesis of ligands for Sialoadhesin.
 <br>

← Older revision		Revision as of 05:48, 21 January 2012
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	== Acknowledgements ==		== Acknowledgements ==
−	The CFG is grateful to the following PIs for their contributions to this wiki page: Paul Crocker, James Paulson	+	The CFG is grateful to the following PIs for their contributions to this wiki page: Paul Crocker, Sorge Kelm, James Paulson

← Older revision		Revision as of 23:30, 30 March 2011
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−	Sialoadhesin (Sn) is an atypical siglec, due to the presence of an unusually large number of Ig domains (17) and the absence of tyrosine-based intracellular signaling motifs. Sn is expressed uniquely by macrophage subsets in vivo and the 17 Ig domains are thought to be important for its ability to mediate sialic acid-dependent adhesive functions. This contrasts with most other siglecs which are much shorter and masked by cis binding to co-expressed sialic acids.	+	Sialoadhesin (Sn), also known as Siglec-1, is an atypical siglec, due to the presence of an unusually large number of Ig domains (17) and the absence of tyrosine-based intracellular signaling motifs. Sn is expressed uniquely by macrophage subsets in vivo and the 17 Ig domains are thought to be important for its ability to mediate sialic acid-dependent adhesive functions. This contrasts with most other siglecs which are much shorter and masked by cis binding to co-expressed sialic acids.

	== CFG Participating Investigators contributing to the understanding of this paradigm ==		== CFG Participating Investigators contributing to the understanding of this paradigm ==