MRC1
MIM.153618 10p13
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[ (||image_reduire{0,60}|inserer_attribut{alt,The macrophage mannose receptor (MRC1)}) ]
Recognition of complex carbohydrate structures plays an important role in a number of biologic processes, including cell-cell recognition, serum glycoprotein turnover, and neutralization of pathogens.
Many of the endogenous animal lectins which mediate these recognition events share a common Ca(2+)-dependent structural motif, which has been designated a C-type carbohydrate-recognition domain (CRD).
The mannose receptor found on macrophages and on endothelial cells of the liver is the only known example of a C-type lectin that contains multiple C-type CRDs.
One function of the receptor is to bind high-mannose structures on the surface of potentially pathogenic viruses, bacteria, and fungi, so that they can be neutralized by phagocytic engulfment (phagocytosis).
The mannose receptor (MRC1) is a 175 kDa type I membrane molecule expressed in the mouse by most tissue macrophages and lymphatic and hepatic endothelia.
References
Burgdorf, S.; Kautz, A.; Bohnert, V.; Knolle, P. A.; Kurts, C. : Distinct pathways of antigen uptake and intracellular routing in CD4 and CD8 T cell activation. Science 316: 612-616, 2007. PubMed ID : #17463291#
Lee, S. J.; Evers, S.; Roeder, D.; Parlow, A. F.; Risteli, J.; Risteli, L.; Lee, Y. C.; Feizi, T.; Langen, H.; Nussenzweig, M. C. : Mannose receptor-mediated regulation of serum glycoprotein homeostasis. Science 295: 1898-1901, 2002. PubMed ID : #11884756#