• Interaction

    AccNo. 22418 Score 0.86
    Name ACAPG_ather Environment ex vivo
    Kd 1.0 Organism Homo sapiens (human)

    Peptide

    AccNo. 22302
    Name ACAPG
    Organism N/A
    Constraint disulfide
    Sequence ACAPGPSKSCGGSYK
    22302_small
    Origin phage display
    Form synthetic
    Internalized no
    Unnatural C-terminal K is conjugated to biotin
    Imaging no
    Is Motif no

    Interactor

    AccNo. 22154
    Name ather
    Description atherosclerotic lesions from iliac artery
    Organism Homo sapiens (human)
    Type tissue

    Experiment

    AccNo. 22373
    Classification incorrect?
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    is used to improve the automatic classification.
    Voting_motivation
    CA CVD DM APO ANG MI BD
    0.48 0.67 0.50 0.47 0.83 0.43 0.33 Vote
    plus plus plus plus plus plus plus Yes
    minus minus minus minus minus minus minus No
    Name PD_4
    Detection light microscopy, MI:0426
    Source PDF Text Id 4
    Journal Am J Pathol. 2003 Nov;163(5):1859-71.
    Title In vivo interrogation of the molecular display of atherosclerotic lesion surfaces.
    Authors Liu C, Bhattacharjee G, Boisvert W, Dilley R, Edgington T
    Text The endothelial surface of atherosclerotic lesions of ApoE knockout mice was interrogated by in vivo biopanning with a phage-displayed constrained peptidyl library. Through repeated biopanning, 103 peptidyl sequences were identified, many are homologous to known proteins. The sequence CAPGPSKSC contains motifs that are shared by 9.7% of selected peptides. On phage or as a synthetic peptide, this constrained peptide selectively bound to atherosclerotic lesion surfaces of ApoE knockout mice in vivo and of human atherosclerotic lesions ex vivo. A cell-surface protein of approximately 82 kd recognized by this peptide was affinity-purified and determined by mass spectrometry analysis as glucose-regulated protein 78 (Grp78), indicating the surprising presence of this endoplasmic reticulum chaperone on the endothelial cell surface of atherosclerotic lesions. Peptides that mimicked binding functions of their homologues were demonstrated with three peptides homologous to tissue inhibitor of metalloproteinase-2 (TIMP-2), ie, CNHRYMQMC, CNQRHQMSC, and CNNRSDGMC. Phage carrying CNHRYMQMC bound to atherosclerotic lesion endothelium of ApoE knockout mice in vivo. The three peptides bound to endothelial cells in a dose-dependent manner and were inhibited by TIMP-2 protein. These peptides provide a set of probes to interrogate the cell surface repertoire associated with atherogenesis and thrombotic complications.
    Mesh Terms Amino Acid Sequence; Animals; Apolipoproteins E/genetics; Arteriosclerosis/metabolism; Arteriosclerosis/pathology; Blotting, Western; Carrier Proteins/analysis; Carrier Proteins/metabolism; Chromatography; Endothelium, Vascular/chemistry; Endothelium, Vascular/metabolism; Endothelium, Vascular/pathology; Flow Cytometry; Heat-Shock Proteins; Humans; Immunohistochemistry; Mass Spectrometry; Mice; Mice, Knockout; Molecular Chaperones/analysis; Molecular Chaperones/metabolism; Peptide Library; Peptides/metabolism; Precipitin Tests; Tissue Inhibitor of Metalloproteinase-2/analysis; Tissue Inhibitor of Metalloproteinase-2/metabolism
    References
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