Status
Please wait ...

Details for messenger / hormone: alpha-AGP

EndoNet ID: ENH00215

To link to the content of EndoNet use the EndoNet ID that is given on the detail pages in the format ENX0000, where X is a place holder for the type of the component (e. g. R for receptor or C for anatomical structure).
As URL for the linking append this ID to the detail page for this type of component.
For an hormone that would be: 

http://endonet.bioinf.med.uni-goettingen.de/hormone/ENH00000

It is also possible to use the search of EndoNet to link to the right detail page. The URL should look like 

http://endonet.bioinf.med.uni-goettingen.de/search/ENC00000
If the search pattern is unambigious the user is directed to the corresponding detail page.

Synonyms

  • ORM
  • alpha-1-acid glycoprotein 1
  • alpha-AGP
  • orosomucoid 1
  • ORM1
  • glycoprotein, alpha-1-acid, of serum
  • alpha-1-acid glycoprotein
  • alpha-1-AGP
  • AGP1
  • AGP 1
  • OMD1
  • OMD 1
  • orosomucoid-1
  • alpha AGP
  • alpha 1 acid glycoprotein

General information

  • Alpha(1)-acid glycoprotein (AGP), one of the major acute-phase proteins, forms a function-stabilizing complex with plasminogen activator inhibitor 1 (PAI-1). [1]
  • AGP, a highly glycosylated polypeptide chain, is expressed in human liver and in other cells, including human breast epithelial cells, endothelial cells, and cultured human granulocytes and monocytes. [1]
  • The plasma concentration of alpha AGP in humans increases considerably as a consequence of acute infections or inflammations. [2]
  • Human alpha-acid glycoprotein (alpha-AGP) or orosomucoid is a plasma protein synthesized in the liver and secreted into the blood. [2]
  • The human genome contains three alpha 1-glycoprotein genes (AGP-A, AGP-B, and AGP-B') encoding for slightly different forms of the protein. [3]
  • Orosomucoid in urine may be a more informative marker than albumin for inflammation. [4]

Classification

Hormone function

  • immune response
    • activation

    Chemical classification

    Composition

    • Structure of the human alpha 1-acid glycoprotein gene: sequence homology with other human acute phase protein genes. [5]
    • Molecular cloning and nucleotide sequence of human alpha 1 acid glycoprotein cDNA. [6]
    Sequence 
    MALSWVLTV LSLLPLLEA QIPLCANLV 
PVPITNATL DQITGKWFY IASAFRNEE 
YNKSVQEIQ ATFFYFTPN KTEDTIFLR 
EYQTRQDQC IYNTTYLNV QRENGTISR 
YVGGQEHFA HLLILRDTK TYMLAFDVN 
DEKNWGLSV YADKPETTK EQLGEFYEA 
LDCLRIPKS DVVYTDWKK DKCEPLEKQ 
HEKERKQEE GES
    UniProt P02763

    Orosomucoid 1 mature peptide

    Sequence 
    QIPLCANLV PVPITNATL DQITGKWFY 
IASAFRNEE YNKSVQEIQ ATFFYFTPN 
KTEDTIFLR EYQTRQDQC IYNTTYLNV 
QRENGTISR YVGGQEHFA HLLILRDTK 
TYMLAFDVN DEKNWGLSV YADKPETTK 
EQLGEFYEA LDCLRIPKS DVVYTDWKK 
DKCEPLEKQ HEKERKQEE GES

    Links to other resources

    UniProt P02763
    Ensembl ENST00000259396
    KEGG hsa:5004

    • Anatomical structure: breast

      • AGP, a highly glycosylated polypeptide chain, is expressed in human liver and in other cells, including human breast epithelial cells, endothelial cells, and cultured human granulocytes and monocytes. [1]

    • Anatomical structure: epithelial_cell

      • AGP, a highly glycosylated polypeptide chain, is expressed in human liver and in other cells, including human breast epithelial cells, endothelial cells, and cultured human granulocytes and monocytes. [1]

    • Anatomical structure: continuous_vascular_endothelial_cell_of_blood_vessels_and_lymphatics

      • AGP, a highly glycosylated polypeptide chain, is expressed in human liver and in other cells, including human breast epithelial cells, endothelial cells, and cultured human granulocytes and monocytes. [1]

    • Anatomical structure: neutrophil_granulocyte

      • AGP, a highly glycosylated polypeptide chain, is expressed in human liver and in other cells, including human breast epithelial cells, endothelial cells, and cultured human granulocytes and monocytes. [1]

    • Anatomical structure: monocyte

      • AGP, a highly glycosylated polypeptide chain, is expressed in human liver and in other cells, including human breast epithelial cells, endothelial cells, and cultured human granulocytes and monocytes. [1]

    Targets

    CellCCR5Sialic acid-binding Ig-like lectin 5
    lipocyte of liver Present
    Phenotypes
    • hepatic stellate cell migration
    • ERK activation
    • positive regulation of cell proliferation
    Influences
    • ↑ RANTES
    monocyte Present
    Reference