Ficolin M (Ficolin 1) - Revision history

Carole Weaver: /* Glycogene microarray */

2011-03-28T19:07:51Z

Glycogene microarray

Carole Weaver: /* Related GBPs */

2011-03-21T18:44:38Z

Related GBPs

Nicole Thielens at 13:01, 18 March 2011

2011-03-18T13:01:40Z

Kurt Drickamer: /* Glycogene microarray */

2011-03-18T09:17:52Z

Glycogene microarray

Kurt Drickamer: /* Glycan profiling */

2011-03-18T09:17:27Z

Glycan profiling

Kurt Drickamer: /* Biosynthesis of ligands */

2011-03-18T09:16:30Z

Biosynthesis of ligands

Carole Weaver: /* Cellular expression of GBP and ligands */

2010-08-06T17:38:53Z

Cellular expression of GBP and ligands

Carole Weaver: /* Progress toward understanding this GBP paradigm */

2010-08-06T17:38:35Z

Progress toward understanding this GBP paradigm

Nicole Thielens: /* Biological roles of GBP-ligand interaction */

2010-07-19T06:51:05Z

Biological roles of GBP-ligand interaction

Nicole Thielens: /* Related GBPs */

2010-07-19T06:50:36Z

Related GBPs

← Older revision		Revision as of 19:07, 28 March 2011
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	=== Glycogene microarray ===		=== Glycogene microarray ===
		+	No data available.
	<br>		<br>

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 == Related GBPs ==
-This family is characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. Homologs are apparently absent in ''D. melanogaster'' and ''C. elegans''. Several human family members have been described but Ficolin L and M are the best characterized both biochemically and structurally. Ficolin L and H are made in the liver, while Ficolin M and H are produced by the lung. Two ficolins (A and B) are present in mouse. Ficolin B may be the ortholog of Ficolin M.
+This family is characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. Homologs are apparently absent in ''D. melanogaster'' and ''C. elegans''. Several human family members have been described but Ficolin L and M are the best characterized both biochemically and structurally. Ficolin L [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=ficolin+AND+L&maxresults=20 (CFG data)] and H [http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=ficolin+AND+H&maxresults=20 (CFG data)] are made in the liver, while Ficolin M and H are produced by the lung. Two ficolins (A and B) are present in mouse. Ficolin B may be the ortholog of Ficolin M.
 <br>A vertebrate membrane-bound chitin-binding protein, called FIBCD1 (Fibrinogen C domain containing 1) has been identified recently<ref>Schlosser A, Thomsen T, Moeller JB, Nielsen O, Tornoe I, Mollenhauer J, Moestrup SK, and Holmskov U. Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin. J Immunol 183, 3800-3809 (2009)</ref>. The ectodomain of FIBCD1 forms disulfide-linked tetramers assembled from a coiled-coil region, a polycationic region and a C-terminal fibrinogen-related domain. The acetyl-binding site of the fibrinogen-like recognition domain of FIBCD1 is homologous to that of TL5A and M-ficolin<ref> Thomsen T, Moeller JB, Schlosser A, Sorensen GL, Moestrup SK, Palaniyar N, Wallis R, Mollenhauer J, and Holmskov U. The recognition unit of FIBCD1 organizes into a non-covalently linked tetrameric structure and uses a hydrophobic funnel (S1) for acetyl group recognition. J Biol Chem 285, 1229-1028 (2010)</ref>.

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 == Progress toward understanding this GBP paradigm ==
 This section documents what is currently known about Ficolin M, its carbohydrate ligand(s), and how they interact to mediate cell communication.
 === Carbohydrate ligands ===
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 === Biosynthesis of ligands ===
 Pathways for ganglioside biosynthesis have been described ([http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/geMolecule.jsp GT Database]).
-<br>
+<br>O-acetylation at positions C-7,8,9 of sialic acid is catalyzed by O-acetyltransferase enzymes associated with the Golgi membrane in mammals<ref>Higa, H.H., Manzi, A. and Varki, A. O-acetylation and de-O-acetylation of sialic acids. Purification, characterization, and properties of a glycosylated rat liver esterase specific for 9-O-acetylated sialic acids. J Biol Chem 264, 19435-19442 (1989)</ref><ref>Butor, C., Higa, H.H. and Varki, A. Structural, immunological, and biosynthetic studies of a sialic acid-specific O-acetylesterase from rat liver. J Biol Chem 268, 10207-10213 (1993)</ref>. Sialic acid O-acetyltransferases have also been identified in bacteria, but they are not homologous to the vertebrate enzymes<ref>Lewis, A.L., Hensler, M.E., Varki, A. and Nizet, V. The group B streptococcal sialic acid O-acetyltransferase is encoded by neuD, a conserved component of bacterial sialic acid biosynthetic gene clusters. J Biol Chem 281, 11186-11192 (2006)</ref>.
 === Structure ===

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 === Glycogene microarray ===
-<br>not performed
+<br>
 === Knockout mouse lines ===

@@ Line 30: / Line 30: @@
 === Glycan profiling ===
-<br> not performed
+Glycan profiling has not been performed.
 === Glycogene microarray ===

@@ Line 12: / Line 12: @@
 === Cellular expression of GBP and ligands ===
-M-ficolin has been localized at the surface of blood monocytes and in secretory granules of neutrophils, monocytes, and lung epithelial cells )<ref name="Teh 30"/><ref name="Frederiksen 34"/><ref name="Liu 2005"/>. However, two recent studies have reported its detection in serum, with mean concentrations ranging from 0.06 to 1 &mu;g/ml<ref name="Honore 2008"/><ref>Wittenborn, T., Thiel, S., Jensen, L., Nielsen, H. J., and Jensenius, J. C. Characteristics and biological variations of M-ficolin, a pattern recognition molecule, in plasma. J Innate Immun 2, 167-180 (2010)</ref>.
+M-ficolin has been localized at the surface of blood monocytes and in secretory granules of neutrophils, monocytes, and lung epithelial cells<ref name="Teh 30"/><ref name="Frederiksen 34"/><ref name="Liu 2005"/>. However, two recent studies have reported its detection in serum, with mean concentrations ranging from 0.06 to 1 &mu;g/ml<ref name="Honore 2008"/><ref>Wittenborn, T., Thiel, S., Jensen, L., Nielsen, H. J., and Jensenius, J. C. Characteristics and biological variations of M-ficolin, a pattern recognition molecule, in plasma. J Innate Immun 2, 167-180 (2010)</ref>.
 === Biosynthesis of ligands ===
 <br>

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 === Biological roles of GBP-ligand interaction ===
-Soluble M-ficolin has been shown to bind to ''Staphylococcus aureus'' through GlcNAc<ref name="Liu 2005"/>. It is tethered to monocytes and granulocytes through binding of its fibrinogen-like recognition domain to sialic acid on the cell surface<ref>Honore C, Rorvig S, Hummelshoj T, Skjoedt MO, Borregaard N, Garred P.Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain. J Leukoc Biol 88, 145-158 (2010)</ref>.
+Soluble M-ficolin has been shown to bind to ''Staphylococcus aureus'' through GlcNAc<ref name="Liu 2005"/>. It is tethered to monocytes and granulocytes through binding of its fibrinogen-like recognition domain to sialic acid on the cell surface<ref>Honore C, Rorvig S, Hummelshoj T, Skjoedt MO, Borregaard N, and Garred P. Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain. J Leukoc Biol 88, 145-158 (2010)</ref>.
 == CFG resources used in investigations ==