Difference between revisions of "Mannose receptor"

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=== Structure ===
 
=== Structure ===
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The mannose receptor is a type I transmembrane protein, with a large extracellular domain containing three types of domain. An N-terminal R-type carbohydrate-recognition domain is followed by a fibronectin type II domain and eight C-type carbohydrate-recognition domains<ref name="Taylor 1990"/>. The short cytoplasmic C-terminal domain contains a di-aromatic motif essential for rapid internalization and endosomal sorting<ref name="Schweizer 2000">Schweizer A, Stahl PD, Rohrer J (2000) A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting.<i>J Biol Chem</i> <b>275</b>, 29694-29700</ref>. Three other endocytic receptors, DEC-205, Endo-180 and the phospholipase A2 receptor, share the same domain organization as the mannose receptor<ref name="Taylor 1997">Taylor, ME (1997) Evolution of a family of receptors containing multiple C-type carbohydrate-recognition domains. <i>Glycobiology</i> <b>7</b>, v-viii</ref>. Of these, only Endo-180 has been shown to bind carbohydrate ligands.
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=== Biological roles of GBP-ligand interaction ===
 
=== Biological roles of GBP-ligand interaction ===
  

Revision as of 17:50, 13 June 2010

The mannose receptor represents a paradigm for the involvement of C-type lectins in clearance of circulating glycoproteins. The role of glycan-binding receptors as tags for uptake and turnover was one of the first established functions for endogenous sugar-binding proteins and provides a key model for how glycans can modulate communication between cells in a physiological context. While the asialoglycoprotein receptor would be considered the founder member of this group of receptors, the in vivo evidence for its function is less compelling than the results for the mannose receptor, which has well defined roles in clearance of sulfated glycoprotein hormones and mannose-bearing glycoproteins released at sites of inflammation.

The mannose receptor represents a paradigm for the involvement of C-type lectins in clearance of circulating glycoproteins. The role of glycan-binding receptors as tags for uptake and turnover was one of the first established functions for endogenous sugar-binding proteins and provides a key model for how glycans can modulate communication between cells in a physiological context. While the asialoglycoprotein receptor would be considered the founder member of this group of receptors, the in vivo evidence for its function is less compelling than the results for the mannose receptor, which has well defined roles in clearance of sulfated glycoprotein hormones as well as mannose-bearing glycoproteins released at sites of inflammation[1].


In addition to the mannose receptor and the asialoglycoprotein receptor, the scavenger receptor C-type lectin may also be involved in clearance of serum glycoproteins. The asialoglycoprotein receptor and the scavenger receptor C-type lectin have different domain organisations and ligand binding specificities compared to the mannose receptor.


PIs working with the mannose receptor include: Ten Feizi; Reiko Lee; Yuan Lee; Michel Nussenzweig; Maureen Taylor; Kurt Drickamer; Chi-Huey Wong; Bill Weis; Pauline Rudd; Nathalie Scholler

Progress toward understanding this GBP paradigm

As in the case of the selectins, much of the evidence for functions of the mannose receptor pre-dates the consortium. However, there have been some further developments for this receptor and other members of the group. PIs have generated and characterized knockout mice, defined the sugar-binding specificities, demonstrated clearance in vivo and endocytosis in tissue culture, and performed structural analysis.

Carbohydrate ligands

The multiple domains in the extracellular region of the mannose receptor allow recognition of a diverse range of glycoconjugate ligands[2]. Several of the eight C-type carbohydrate-recognition domains are involved in Ca2+-dependent recognition of terminal mannose, GlcNAc or fucose residues on the oligosaccharides of endogenous glycoproteins or the surfaces of microorganisms [3][4], while the R-type carbohydrate-recognition domain binds sulfated GalNAc and sulfated galactose residues[5]. Biological ligands for the mannose receptor include lysosomal hydrolases, the pro-collagen peptides of type I and type III collagens and tissue plasminogen activator – proteins that bear high mannose oligosaccharides and are released from cells at sites of inflammation[6]. The main biological ligands recognized by the R-type carbohydrate-recognition domain are the pituitary hormones lutropin and thyrotropin which bear oligosaccharides terminating in GalNAc-4-SO4[5][7]. The CFG contributed to defining specificity for oligosaccharides through screening of glycan arrays[8].

Cellular expression

The mannose receptor was first identified in the liver on sinusoidal endothelial cells and Kupffer cells[9]. The receptor has since been found on most types of tissue macrophages, including those in the placenta and the brain, but not on circulating monocytes[1]. The mannose receptor is also expressed in the retinal pigmented epithelium[10] and on CD1-positive dendritic cells[11]. The CFG contributed to defining expression of the mannose receptor by glycogene microarray analysis[12].

Structure

The mannose receptor is a type I transmembrane protein, with a large extracellular domain containing three types of domain. An N-terminal R-type carbohydrate-recognition domain is followed by a fibronectin type II domain and eight C-type carbohydrate-recognition domains[2]. The short cytoplasmic C-terminal domain contains a di-aromatic motif essential for rapid internalization and endosomal sorting[13]. Three other endocytic receptors, DEC-205, Endo-180 and the phospholipase A2 receptor, share the same domain organization as the mannose receptor[14]. Of these, only Endo-180 has been shown to bind carbohydrate ligands.

Biological roles of GBP-ligand interaction


CFG resources used in investigations

The best examples of CFG contributions to this paradigm are described below, with links to specific data sets. For a complete list of CFG data and resources relating to this paradigm, see the CFG database search results for "mannose receptor".

Glycan profiling


Glycogene microarray

The CFG analyzed patterns of mannose receptor expression.

Knockout mouse lines

Before funding for knockout mice was discontinued, the CFG developed the DNA construct to create a mouse line lacking the scavenger receptor. The construct can now be obtained from the Mutant Mouse Regional Resource Center (MMRRC) at the University of California, Davis.

Glycan array

The CFG analyzed the binding specificities of the mannose receptor.

Related GBPs

Asialoglycoprotein receptor, scavenger receptor C-type lectin, Kupffer cell receptor

References

  1. ↑ 1.0 1.1 Taylor PR, Gordon S, Martinez-Pomares L (2005) The mannose receptor: linking homeostasis and immunity through sugar recognition. Trends Immunol 26,104-110
  2. ↑ 2.0 2.1 Taylor, ME, Conary, JT, Lennartz, MR, Stahl, PD, Drickamer, K (1990) Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains.J Biol Chem 265,12156-12162
  3. ↑ Taylor, ME., Bezouska, K, Drickamer, K (1992) Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor.J Biol Chem 267, 1719-1726
  4. ↑ Mullin, NP, Hitchen, PG, Taylor, ME (1997) Mechanism of Ca2+- and monosaccharide-binding to a C-type carbohydrate-recognition domain of the macrophage mannose receptor. J Biol Chem 272, 5668-5681
  5. ↑ 5.0 5.1 Fiete DJ, Beranek MC, Baenziger JU (1998) A cysteine-rich domain of the "mannose" receptor mediates GalNAc-4-SO4 binding. Proc Natl Acad Sci USA95, 2089-2093
  6. ↑ Lee SJ, Evers S, Roeder D, Parlow AF, Risteli J, Risteli L, Lee YC, Feizi T, Langen H, Nussenzweig MC (2002) Mannose receptor-mediated regulation of serum glycoprotein homeostasis. Science 295, 1898-1901
  7. ↑ Liu Y, Chirino AJ, Misulovin Z, Leteux C, Feizi T, Nussenzweig MC, Bjorkman PJ. (2000) Crystal structure of the cysteine-rich domain of the mannose receptor complexed with a sulfated carbohydrate ligand.J Exp Med191,1105-1116
  8. ↑ Hsu TL, Cheng SC, Yang WB, Chin SW, Chen BH, Huang MT, Hsieh SL, Wong CH (2009) Profiling carbohydrate-receptor interaction with recombinant innate immunity receptor-Fc fusion proteins. J Biol Chem 284, 34479-34489
  9. ↑ Schlesinger P, Doebber TW, Mandell BF, White R, DeSchryver C, Rodman JS, Miller MJ, Stahl P (1978) Plasma clearance of glycoproteins with terminal mannose and GlcNAc by liver non-parenchymal cells.Biochem J176,103-109
  10. ↑ Greaton CJ, Lane KB, Shepherd VL, McLaughlin BJ (2003) Transcription of a single mannose receptor gene by macrophage and retinal pigment epithelium.Opthalmic Res35,42-47
  11. ↑ Sallusto F, Cella M, Danieli C, Lanzavecchia A (1995) Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major hitocompatibility complex class II compartment: downregulation by cytokines and bacterial products.J Exp Med182, 389-400
  12. ↑ Comelli, EM, Head, SR, Gilmartin, T, Whisenant, T, Haslam, SM, North SJ, Wong, N-K, Kudo, T, Narimatsu, H, Esko, JD, Drickamer, K, Dell, A, Paulson, JC (2006) A focused microarray approach to functional glycomics: transcriptional regulation of the glycome.Glycobiology16, 117-131
  13. ↑ Schweizer A, Stahl PD, Rohrer J (2000) A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting.J Biol Chem 275, 29694-29700
  14. ↑ Taylor, ME (1997) Evolution of a family of receptors containing multiple C-type carbohydrate-recognition domains. Glycobiology 7, v-viii
  • Coombs PJ, Taylor ME, Drickamer K (2006) Two categories of mammalian galactose-binding receptors distinguished by glycan array profiling. Glycobiology 16, 1C-7C.
  • Feinberg H, Taylor ME, Weis WI (2007) Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis x by a novel mechanism. J Biol Chem 282, 17250-17258.
  • Coombs PJ, Graham SA, Drickamer K, Taylor ME (2005) Selective binding of the scavenger receptor C-type lectin to Lewisx trisaccharide and related glycan ligands. J Biol Chem 280, 22993-22999.

Acknowledgements

The CFG is grateful to the following PIs for their contributions to this wiki page: Kurt Drickamer, Maureen Taylor, Yvette van Kooyk

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