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Mannose receptor: Wikis


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mannose receptor, C type 1
Symbol MRC1
Alt. symbols CD206
Entrez 4360
HUGO 7228
OMIM 153618
RefSeq NM_002438
UniProt P22897
Other data
Locus Chr. 10 p13
mannose receptor, C type 2
Symbol MRC2
Alt. symbols CD280
Entrez 9902
HUGO 16875
RefSeq NM_006039
UniProt Q9UBG0
Other data
Locus Chr. 17 q23

The mannose receptor is a C-type lectin. It has been researched as a target for vaccines.[1]. This gene works to recognize complex carbohydrates that are located on glycoproteins that are a part of many different biological processes. Some of those processes include cell-cell recognition, serum glycoprotein turnover, and neutralization of pathogens. [2] The gene also encodes a protein that is a type 1 membrane receptor that mediates the endocytosis of gycoproteins by macrophages. [3]The structure of this proteins allows it to bind to high mannose structures on the surface of potentially pathogenic viruses, bacteria, and fungi so that they can be engulfed by the cell[4]. The gene is in close proximity to MRC1L1 and has a gene loci that includes the gene, MRC1L1, as well as LOC340843 and LOC340893[5]. The gene also consist of nearly two identical regions, some think that they are duplicated regions[6]. Recombinant proteins produced in yeast may be subject to increased addition of mannose, in patterns different from those of a human cell[7] Dendritic cells take of the immune system possess a mannose receptor that enables them to take up mannosylated proteins, and utilize fragments of them for antigen presentation[8]



The most common function is found during the cell cycle when mutations occur that are involved with either replication initiation or replication elongation. MRC1 works with the activation of Cds1 during replication fork arrest but it is not required to activate Chk1. MRC1 does interact with Chk1 when working to fix replication initiation mutations and if MRC1 is removed from the system during this process the amount of DNA damage is increased.[9]. MRC1 and Cds1 work together to stall replication forks by interacting with the forkhead-association domain located on Cds1 and the Rad3-phosphorylation site on MRC1.[10]. This connection explains that the Rad3 from the MRC1 is what activates the Cds1. If a mutation in MRC1 occurs it will affect the targeted site for Rad3 kinase and the sequence will change to have a series of serine and threonine residues to alanine, changing the SQ cluster and TQ repeats on the Mid7 group and blocking phosphorylation of these sites.[11]. These structural changes also effect the checkpoint activity of MRC1 and thus the activation of the Cds1 kinase. The information known about how MRC1 works with the cell cycle is now being used to find drugs that can help these interactions and block tumor growth.

This gene also interacts with HIV proteins. These interactions affect the gp120 and its ability to bind to the B cells through MRC1 receptors and an increase production of matrix mannose receptors. [12] The protein, Nef interacts with MRC1 by down regulating the receptors on the surface of macrophages and dendritic cells. The tat protein represses the transcription of MRC1 promoters by down regulating the expression of MRC1. [13]All of these proteins interact with MRC1 so that the virus can continue to spread and more research is being conducted trying to understand how stop there interactions from occurring.

More is going to be understood of this gene as more research is done looking at using it to fight tumor growth and HIV.

See also


  1. ^ Keler T, Ramakrishna V, Fanger M (2004). "Mannose receptor-targeted vaccines". Expert Opin Biol Ther 4 (12): 1953–62. doi:10.1517/14712598.4.12.1953. PMID 15571457.  
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  7. ^ Vlahopoulos S, Gritzapis AD, Perez SA, Cacoullos N, Papamichail M, Baxevanis CN.Mannose addition by yeast Pichia Pastoris on recombinant HER-2 protein inhibits recognition by the monoclonal antibody herceptin.Vaccine. 2009 Jun 8. [Epub ahead of print]PMID: 19520203
  8. ^ Shimizu K, Fujii S. An adjuvant role of in situ dendritic cells (DCs) in linking innate and adaptive immunity. Front Biosci. 2008 May 1;13:6193-201. Review. PMID: 18508653
  9. ^ Yin L., Locovei A. M., D’Urso G. (2008). "Activation of the DNA Damage Checkpoint in Mutants Defective in DNA Replication Initiation". Molecular Biology of the Cell 19: 4374-4382.  
  10. ^ Yin L., Locovei A. M., D’Urso G. (2008). "Activation of the DNA Damage Checkpoint in Mutants Defective in DNA Replication Initiation". Molecular Biology of the Cell 19: 4374-4382.  
  11. ^ Yin L., Locovei A. M., D’Urso G. (2008). "Activation of the DNA Damage Checkpoint in Mutants Defective in DNA Replication Initiation". Molecular Biology of the Cell 19: 4374-4382.  
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