• Interaction

    AccNo. 22624 Score 0.86
    Name ADPRA_LNCaP Environment in vitro / culture
    Kd 1.0 Organism Homo sapiens (human)

    Peptide

    AccNo. 22504
    Name ADPRA
    Organism N/A
    Constraint none
    Sequence ADPRATPGSDPAKAC
    22504_small
    Origin phage display
    Form synthetic
    Internalized no
    Unnatural no
    Imaging no
    Is Motif no

    Interactor

    AccNo. 22361
    Name LNCaP
    Description LNCaP prostate carcinoma cells
    Organism Homo sapiens (human)
    Type cell

    Experiment

    AccNo. 22579
    Classification incorrect?
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    Voting_motivation
    CA CVD DM APO ANG MI BD
    1.00 1.00 1.00 0.60 0.73 0.40 0.75 Vote
    plus plus plus plus plus plus plus Yes
    minus minus minus minus minus minus minus No
    Name PD_8
    Detection competition binding, MI:0405
    Source PDF Text Id 8
    Journal Prostate. 2001 Jun 1;47(4):239-51.
    Title Phage display selection of peptides that affect prostate carcinoma cells attachment and invasion.
    Authors Romanov VI, Durand DB, Petrenko VA
    Text BACKGROUND: Prostate cancer-specific proteins must be identified to serve as diagnostic and prognostic markers. Cell surface proteins are especially important, because they have potential utility as diagnostic markers and therapeutic targets. Identification of ligands for these proteins will allow use of these ligands as diagnostic and therapeutic tools and permit the investigation of receptor function. We performed a search for peptide ligands to prostate cancer cell-specific receptors. METHODS: Peptide phage display library was used to isolate specific ligands to LNCaP prostate carcinoma cells receptors. Selected phage and cognate peptides were investigated for their cancer-related functions, such as the ability to interfere with cell adhesion, spreading, motility, and invasion. RESULTS: Phage designated pg35, blocked spreading of LNCaP cells and their derivatives C4-2 and C4-2b. Cognate peptide did not inhibit spreading, but incubation of C4-2 and C4-2b cells with cognate peptide increased their affinity for endothelial cells and invasiveness. In addition, the peptide activates matrix metalloproteinase (MMP)-2 and 9 in C4-2 and C4-2b cells. CONCLUSIONS: These results indicate that identified ligands may play a role in tumorigenicity and metastatic transformation of prostate cancer. To our knowledge, this is the first identification of a functional cancer-specific peptide ligand using the phage display approach.
    Mesh Terms Amino Acid Sequence; Animals; Bacteriophages/metabolism; Carcinoma/drug therapy; Carcinoma/metabolism; Carcinoma/pathology; Cell Adhesion/drug effects; Cell Adhesion/physiology; Cell Movement/drug effects; Cell Movement/physiology; Chemotaxis/physiology; Electrophoresis; Endothelium/physiology; Enzyme Activation; Humans; Ligands; Male; Matrix Metalloproteinase 2/metabolism; Matrix Metalloproteinase 9/metabolism; Mice; Mice, Nude; Molecular Sequence Data; Neoplasm Proteins/metabolism; Neoplasm Proteins/pharmacology; Neoplasm Proteins/physiology; Peptide Library; Prostatic Neoplasms/drug therapy; Prostatic Neoplasms/metabolism; Prostatic Neoplasms/pathology; Sequence Homology, Amino Acid; Substrate Specificity; Tumor Cells, Cultured
    References
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