Tissue factor is the receptor for plasminogen type 1 on 1-LN human prostate cancer cells

Gonzalez-Gronow, Mario; Gawdi, Govind; Pizzo, Salvatore V.

doi:10.1182/blood.v99.12.4562

Cited by 23 publications

(22 citation statements)

References 33 publications

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“…Several proteins with carboxy-terminal lysines (␣-enolase, annexin II) have been identified as Pg receptors on the cell surface, 17,18 while other Pg-binding molecules (amphoterin, integrin glycoprotein IIbIIIa [GPIIbIIIa], cytokeratin-8, dipeptidyl peptidase, tissue factor) appear to utilize internal lysines. 11,[19][20][21][22] The interactions of surface-bound Pg with several proteins involves, in addition to LBSs, some other binding regions, 23,24 suggesting that the alteration of Pg conformation may control recognition.…”

Section: Introductionmentioning

confidence: 99%

Characterization of plasminogen as an adhesive ligand for integrins αMβ2 (Mac-1) and α5β1 (VLA-5)

Lishko

Novokhatny

Yakubenko

et al. 2004

Blood

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Section: Introductionmentioning

confidence: 99%

Characterization of plasminogen as an adhesive ligand for integrins αMβ2 (Mac-1) and α5β1 (VLA-5)

Lishko

Novokhatny

Yakubenko

et al. 2004

Blood

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“…TF, also called thromboplastin, factor III, or CD142, is aberrantly expressed in many types of cancers, including non-small cell lung cancer (5), colorectal cancer (6), genito-urethal (7,8), and gynecologic cancers (9)(10)(11), pancreatic cancer (12), head and neck cancer (13), glioma (14), and metastatic breast cancer (15). Under physiologic conditions, TF is expressed by fibroblasts, pericytes, and smooth muscle cells in the subendothelial vessel wall.…”

Section: Introductionmentioning

confidence: 99%

High Turnover of Tissue Factor Enables Efficient Intracellular Delivery of Antibody–Drug Conjugates

Goeij

Satijn

Freitag

et al. 2015

Molecular Cancer Therapeutics

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Antibody-drug conjugates (ADC) are emerging as powerful cancer treatments that combine antibody-mediated tumor targeting with the potent cytotoxic activity of toxins. We recently reported the development of a novel ADC that delivers the cytotoxic payload monomethyl auristatin E (MMAE) to tumor cells expressing tissue factor (TF). By carefully selecting a TFspecific antibody that interferes with TF:FVIIa-dependent intracellular signaling, but not with the procoagulant activity of TF, an ADC was developed (TF-011-MMAE/HuMax-TF-ADC) that efficiently kills tumor cells, with an acceptable toxicology profile. To gain more insight in the efficacy of TF-directed ADC treatment, we compared the internalization characteristics and intracellular routing of TF with the EGFR and HER2. Both in absence and presence of antibody, TF demonstrated more efficient internalization, lysosomal targeting, and degradation than EGFR and HER2. By conjugating TF, EGFR, and HER2-specific antibodies with duostatin-3, a toxin that induces potent cytotoxicity upon antibody-mediated internalization but lacks the ability to induce bystander killing, we were able to compare cytotoxicity of ADCs with different tumor specificities. TF-ADC demonstrated effective killing against tumor cell lines with variable levels of target expression. In xenograft models, TF-ADC was relatively potent in reducing tumor growth compared with EGFR-and HER2-ADCs. We hypothesize that the constant turnover of TF on tumor cells makes this protein specifically suitable for an ADC approach.

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“…The membranes were thoroughly rinsed with PBS and then incubated with 3% BSA in PBS for 1 h at room temperature to block the non-conjugated areas. For the detection of Pg forms, the membranes were incubated with a goat anti-human Pg IgG (Santa Cruz Biotechnology) followed by incubation with a rabbit anti-goat IgG conjugated to horseradish peroxidase and detected with a peroxidase substrate as described previously (33).…”

Section: Measurement Of Vdac Mrna Levels By Reversementioning

confidence: 99%

The Voltage-dependent Anion Channel (VDAC) Binds Tissue-type Plasminogen Activator and Promotes Activation of Plasminogen on the Cell Surface

Gonzalez-Gronow

Ray

Wang

et al. 2013

Journal of Biological Chemistry

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Background:The VDAC receptor, a major mitochondrial protein, is also present in the plasma membrane of normal brain cells. Results: VDAC binds t-PA and stimulates plasminogen activation in normal and injured brain cells. Conclusion: Formation of the ternary VDAC⅐t-PA⅐plasminogen complex enhances both t-PA activity and plasminogen activation.Significance: This ternary complex may play a significant role in normal and injured brain physiology.

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Tissue factor is the receptor for plasminogen type 1 on 1-LN human prostate cancer cells

Cited by 23 publications

References 33 publications

Characterization of plasminogen as an adhesive ligand for integrins αMβ2 (Mac-1) and α5β1 (VLA-5)

Characterization of plasminogen as an adhesive ligand for integrins αMβ2 (Mac-1) and α5β1 (VLA-5)

High Turnover of Tissue Factor Enables Efficient Intracellular Delivery of Antibody–Drug Conjugates

The Voltage-dependent Anion Channel (VDAC) Binds Tissue-type Plasminogen Activator and Promotes Activation of Plasminogen on the Cell Surface

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