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  • 1
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    Intravenous infusion of phage-displayed antibody library in human cancer patients: enrichment and cancer-specificity of tumor-homing phage-antibodies
    Springer Science and Business Media LLC ; 2013
    In:  Cancer Immunology, Immunotherapy Vol. 62, No. 8 ( 2013-8), p. 1397-1410
    Details
    In: Cancer Immunology, Immunotherapy, Springer Science and Business Media LLC, Vol. 62, No. 8 ( 2013-8), p. 1397-1410
    Type of Medium: Online Resource
    ISSN: 0340-7004 , 1432-0851
    URL: Article
    DOI: 10.1007/s00262-013-1443-5
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2013
    detail.hit.zdb_id: 1458489-X
    detail.hit.zdb_id: 195342-4
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  • 2
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    10-yr follow-up results of NSABP B-32, a randomized phase III clinical trial to compare sentinel node resection (SNR) to conventional axillary dissection (AD) in clinically node-negative breast cancer patients.
    American Society of Clinical Oncology (ASCO) ; 2013
    In:  Journal of Clinical Oncology Vol. 31, No. 15_suppl ( 2013-05-20), p. 1000-1000
    Details
    In: Journal of Clinical Oncology, American Society of Clinical Oncology (ASCO), Vol. 31, No. 15_suppl ( 2013-05-20), p. 1000-1000
    Abstract: 1000 Background: NSABP B-32, the largest surgical prospective randomized phase III trial was designed to compare overall survival (OS), disease-free survival (DFS), and morbidity between SNR alone vs SNR + AD in SN negative (-) pts. We present 10 yr outcome data for primary endpoints as well as updated data on the effect of occult metastases, found later in the SN by central, detailed pathologic analysis. Methods: 5,611 women with operable, clinically N0, invasive breast cancer were randomized to SNR + AD (Group [Grp] 1) or to SNR alone with AD only if SNs were positive (Grp2). 3,989 (71.1%) of 5,611 pts were SN-. 3,986 (99.9%) of these SN- pts had follow-up information: Grp 1: 1,975, Grp 2:2,011. Median time on study was 9.4 yrs. Cox proportional hazard models adjusting for study stratification variables were used to compare OS and DFS between the two groups. Two-sided p values were used. HR values 〉 1 indicate a more favorable outcome in Grp 1 Results: At 10 yrs, there continues to be no significant difference in OS between the two groups (HR: 1.11, p = 0.27). 10 yr Kaplan-Meier (K-M) estimates for OS are 87.8% for SNR alone and 88.9% for SNR + AD. There continues to be no significant difference in DFS between the two groups (HR: 1.01, p=0.92). 10-yr K-M estimates for DFS were 76.9% for both groups. Occult nodal disease was originally detected in 3,884 pts (15.8%) with SN- on initial H and E analysis. Comparisons between the groups with and without occult disease yielded an adjusted HR for OS: 1.25 (p = 0.08) with an absolute difference at 10 yrs of 2.8% and a HR for DFS: 1.24 (p = 0.018) with an absolute difference of 4.1%. The cumulative incidences of local-regional events were low (10-yr values: SNR 4.0%, SNR+AD, 4.3%) and not significant (HR: 0.95, p = 0.77). Conclusions: At 10 yrs there continues to be no significant differences in OS and DFS between SNR and SNR + AD in pts with negative SN. The relative increase in risk of DFS and OS for pts with occult SN metastases remains stable. Support: PHS grants: NSABP: U10CA-12027, U10CA-37377, U10CA-69651, U10CA-69974; VT Ca Cntr: P30 CA22435; DNK: 5RO1CA074137 NCI Dpt HHS. Clinical trial information: NCT00003830.
    Type of Medium: Online Resource
    ISSN: 0732-183X , 1527-7755
    URL: Article
    DOI: 10.1200/jco.2013.31.15_suppl.1000
    RVK:
    XA 52760
    RVK:
    XA 10000
    Language: English
    Publisher: American Society of Clinical Oncology (ASCO)
    Publication Date: 2013
    detail.hit.zdb_id: 2005181-5
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  • 3
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    Relationship Between Arm Morbidity and Patient-Reported Outcomes Following Surgery in Women with Node-Negative Breast Cancer: NSABP Protocol B-32
    Elsevier BV ; 2012
    In:  The Journal of Supportive Oncology ( 2012-8)
    Details
    In: The Journal of Supportive Oncology, Elsevier BV, ( 2012-8)
    Type of Medium: Online Resource
    ISSN: 1544-6794
    URL: Article
    DOI: 10.1016/j.suponc.2012.05.003
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2012
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  • 4
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    Sentinel-lymph-node resection compared with conventional axillary-lymph-node dissection in clinically node-negative patients with breast cancer: overall survival findings from the NSABP B-32 randomised phase 3 trial
    Elsevier BV ; 2010
    In:  The Lancet Oncology Vol. 11, No. 10 ( 2010-10), p. 927-933
    Details
    In: The Lancet Oncology, Elsevier BV, Vol. 11, No. 10 ( 2010-10), p. 927-933
    Type of Medium: Online Resource
    ISSN: 1470-2045
    URL: Article
    DOI: 10.1016/S1470-2045(10)70207-2
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2010
    detail.hit.zdb_id: 2049730-1
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  • 5
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    Abstract 3365: Identification of target antigens on breast cancer stem cells using phage-developed scFv antibodies: A Proteomic Approach
    American Association for Cancer Research (AACR) ; 2010
    In:  Cancer Research Vol. 70, No. 8_Supplement ( 2010-04-15), p. 3365-3365
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 70, No. 8_Supplement ( 2010-04-15), p. 3365-3365
    Abstract: The term ‘cancer stem cell’ has only recently emerged, and is defined as a cancer cell that has the ability to self-renew and give rise to another malignant stem cell, as well as differentiate to give rise to the phenotypically diverse non-tumorigenic cancer cells. The ‘cancer stem cell’ hypothesis emerged from the fact that tumors contain a heterogeneous mixture of cells and that not all the cells within a tumor contribute to tumor growth. Using phage display technology, our previous studies have identified two single chain variable fragment (scFv) antibodies (clones 207, 208) that were found to specifically bind human SUM159 breast cancer stem cells (BCSC). We have also shown in a murine xenograft tumor model prepared from the implanted SUM159 cells that these scFv antibodies predominantly bind to the cells located at the periphery of the tumors. Taking in light of these discoveries, the next logical question to be investigated was, “What cellular-antigens are these scFvs binding to?” In order to answer this in the present investigation, we used proteomic approaches based on a small scale immunoprecipitation, followed by purification and mass-spectrometry-based identification of the binding target antigens. A pure population of BCSC was acquired by flow cytometry, using ALDEFLUOR®-based sorting of the SUM159 cell line. Cell lysates of the sorted BCSC were prepared and the target antigens were immunoprecipitated with scFv-207 and scFv-208 antibodies using a solid-state immunoprecipitation assay. The immunoprecipitated targets were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The target antigens were purified and mass-spectrometric techniques (LQT-MS/ESI mass-fingerprinting) were employed to compare the proteomic data to protein databases. The details of the recovery of peptide-based target antigens and their identification using the proteomic approach as outlined above, will be presented and discussed. The identification of BCSC-specific targets will be a crucial step in designing and developing better and more specific antibody-based therapies against breast cancer. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 3365.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM10-3365
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2010
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 6
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    Abstract 3638: Vaccine-draining lymph nodes of cancer patients for generating anticancer antibodies
    American Association for Cancer Research (AACR) ; 2014
    In:  Cancer Research Vol. 74, No. 19_Supplement ( 2014-10-01), p. 3638-3638
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 74, No. 19_Supplement ( 2014-10-01), p. 3638-3638
    Abstract: Human vaccine studies regularly demonstrate vaccine-induced antibodies in the blood. Characterization of these antibodies shows that they exhibit an extensive range of bioactive mechanisms. Unfortunately, there is not yet a reliable method by which to produce these important antibodies. Human antibodies may not require any molecular modification for therapeutic application and have a much faster pipeline to clinical studies than animal-derived antibodies. Lymph nodes are the primary destination of tumor or vaccine antigens. In the node, B cells undergo clonal expansion and somatic hypermutation, leading to the affinity-matured populations of effector B cells secreting antibodies that bind to the tumor or vaccine. The cancer vaccine-draining node is the ideal source of B cells that produce anticancer antibodies. Despite multiple human cancer vaccine studies, very little research has been done to recover the B cells responsible for vaccine-induced anticancer antibodies. In the present study, we used mononuclear cells from surgically removed vaccine-draining lymph nodes of melanoma patients vaccinated with 6 melanoma peptides derived from cancer-testis antigens and from melanocytic differentiation proteins for generating anti-vaccine peptide antibodies. The lymph node draining the vaccination site was localized by lymphatic mapping with a radiotracer. The development and maturity of B cells were assessed by determining phenotypic characters of lymph node cells using multicolor flow cytometry. The results showed that these vaccine-draining nodes contain high numbers of class-switched (CD19+CD27+IgD-IgM-) B cells and plasmablasts (CD19+CD38+IgM-). B-cell ELISpot assay was used to quantify the proportion of B cells in vaccine-draining lymph nodes that secrete anti-melanoma peptide antibodies. Positive ELISpot responses were observed in patients who also showed serum antibody-reactivity towards the vaccine peptides. The identification of lymph node cell samples exhibiting strong B-cell responses allows efficient generation and screening of hybridomas that secrete antibodies against cancer vaccine antigens. This study establishes a step-wise protocol for generating anti-cancer antibodies from vaccine-draining lymph nodes. We anticipate that the ability to reliably generate in vitro the same antibodies observed in the blood of vaccinated patients will further stimulate research to understand mechanisms of human antibody activity. Citation Format: Girja S. Shukla, Stephanie C. Pero, Yu-jing Sun, Chelsea L. Carman, Walter C. Olson, Craig L. Slingluff, David N. Krag. Vaccine-draining lymph nodes of cancer patients for generating anticancer antibodies. [abstract]. In: Proceedings of the 105th Annual Meeting of the American Association for Cancer Research; 2014 Apr 5-9; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2014;74(19 Suppl):Abstract nr 3638. doi:10.1158/1538-7445.AM2014-3638
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2014-3638
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2014
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 7
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    Abstract 255: GRB7 – a novel target in triple-negative breast cancer
    American Association for Cancer Research (AACR) ; 2011
    In:  Cancer Research Vol. 71, No. 8_Supplement ( 2011-04-15), p. 255-255
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 71, No. 8_Supplement ( 2011-04-15), p. 255-255
    Abstract: Triple-negative breast tumors lack expression of estrogen and progesterone receptors and HER2, rendering them non-responsive to the most effective targeted therapies in breast cancer. These tumors are typically more aggressive than other breast cancer subtypes and, consequently, have a poor prognosis. In a clinical trial of triple-negative breast cancer patients treated with anthracyclines and taxanes, we and others have recently determined that high levels of GRB7 are predictive of tumor recurrence. GRB7 is a cytoplasmic adaptor protein that interacts with receptor tyrosine kinases and integrins, transducing information to their downstream signaling cascades. In this study, we have tested the hypothesis that triple-negative breast cancer cell lines are dependent on GRB7 for migration, invasion and colony formation in 3D culture. Using a highly specific peptide inhibitor (G7-18NATE), we found that the GRB7 inhibition significantly impaired each of these phenotypes in four triple-negative breast cancer cell lines: MDA-MB-468, MDA-MB-231, HCC70 and T4-2. In addition, we have tested whether GRB7 inhibition may sensitize these cell lines to the chemotherapies used in the initial clinical trial. Combination treatment with G7-18NATE and doxorubicin or docetaxel resulted in cooperative cell growth inhibition in each of the four cell lines. Co-treatment lowered the IC40 of both chemotherapeutic agents, and it proved to be synergistic in all cases (Combination Index values & lt;1) These data implicate GRB7 as a key mediator of migration, invasion, colony growth and chemoresistance of triple-negative breast cancer cells and suggest that GRB7 itself, or GRB7-dependent pathways, may prove to be important targets therapeutic. This work was supported in part by Susan G. Komen for the Cure (KG091136). Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 255. doi:10.1158/1538-7445.AM2011-255
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2011-255
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2011
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 8
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    Abstract 720: Phage display selection of ligands against extracellular domain of ErbB2 receptor using novel β-lactamase-random peptide fusion libraries
    American Association for Cancer Research (AACR) ; 2010
    In:  Cancer Research Vol. 70, No. 8_Supplement ( 2010-04-15), p. 720-720
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 70, No. 8_Supplement ( 2010-04-15), p. 720-720
    Abstract: There are now unprecedented opportunities for increased throughput to develop novel molecules that target cancer. Phage display is one example of a high throughput method of generating massive libraries of molecules that have different structural properties. We constructed novel phage-display random peptide libraries in fusion to β-lactamase (β-lactam hydrolase, E.C. # 3.5.2.6) enzyme as a reporter. The linear dodecapeptide (X12) and cysteine-constrained decapeptide (CX10C) libraries were created at the N-terminal end of the Enterobacter cloacae P99 cephalosporinase molecule (P99 β-lactamase), between the signal peptide and the enzyme protein. Peptide-β-lactamase fusions were displayed at the amino terminus of the minor coat pIII protein of filamentous (M13) phage. The overall representations of different amino acids in the random regions of both libraries were very good. The amino acid diversity at each position in the random regions of both the libraries was also good. The libraries were selected against the extracellular domain of ErbB2 receptor (ErbB2-ECD). The target-selected clones were already conjugated to an enzyme reporter, therefore, did not require subcloning or any other post-panning modifications. β-Lactamase is known for high turnover of its enzyme activity with several commercially available chromogenic and fluorogenic substrates. This helped us to develop a very sensitive and efficient assay for measuring concentrations and target-binding of β-lactamase-peptide fusion proteins in their both phage-displayed and soluble forms. The β-lactamase enzyme assay protocol is a one-step process and unlike a typical phage-ELISA it does not require secondary proteins, several steps of lengthy incubations, or washings and can be finished in a few minutes instead of hours. The clone screening protocol can be adopted for a high throughput platform. The identities of peptide-β-lactase fusion clones that bound to purified ErbB2-ECD and ErbB2-overexpressing MCF-7/ErbB2 and SK-BR-3 cell lines were determined by DNA sequencing of the random inserts. The peptide sequences of the selected binding clones were found to share significant motifs with several rationally designed peptide mimetics and phage-display derived peptides that have been reported to bind ErbB2-ECD. Target-specific β-lactamase-linked affinity reagents selected by this procedure can be produced in bulk and purified. The synthesis and successful use of cephalosporin prodrugs of mechanistically diverse anticancer agents, such as doxorubicin, taxol, platinum complexes, phenylenediamine mustard, and vinblastine have been reported in experimental studies. Using an appropriate β-lactam-substrate, the cancer cell-specific ligands selected from these libraries can be used directly for the targeted enzyme prodrug therapy and/or in vivo imaging of cancers. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 720.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM10-720
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2010
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 9
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    Abstract 1769: Phage display selection of cancer cell-binding and -internalizing ligands using random peptide libraries constructed at N-terminus of P99 cephalosporinase
    American Association for Cancer Research (AACR) ; 2011
    In:  Cancer Research Vol. 71, No. 8_Supplement ( 2011-04-15), p. 1769-1769
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 71, No. 8_Supplement ( 2011-04-15), p. 1769-1769
    Abstract: The cancer researchers today are focused in developing new types of cancer treatments that use drugs or other substances to identify and kill cancer cells while doing very little or no damage to normal healthy cells. It is believed that an ability to home in on cancer cells makes chemotherapy both more effective and less likely to cause side effects. One of the strategies to achieve this goal depends on developing ligands that specifically bind/internalize to cancer cells and exert therapeutic effects of their own or guide a targeted delivery of a therapeutic agent (cytotoxic drug, gene, radionuclide, or enzyme) to the tumor cells. Phage display is one example of high throughput technologies that has been successfully utilized for the generation of massive ligand libraries and their selection against specific targets. We constructed novel phage-displayed random linear dodecapeptide (X12) and cysteine-constrained random decapeptide (CX10C) libraries at N-terminal end of the Enterobacter cloacae P99 cephalosporinase molecule (P99 β-lactamase: β-lactam hydrolase, E.C. # 3.5.2.6). The peptide-β-lactamase fusions were displayed at the amino terminus of the minor coat pIII protein of M13 filamentous phage. Several cancer cell-specific binding β-lactamase-peptide fusion ligands were isolated by selecting these libraries on live BT-474 human breast cancer cells. The identified ligands shared several significant motifs, which showed their selectivity and possible binding to some common cancer cell targets. β-Lactamase is a high turnover enzyme with several available chromogenic and fluorogenic substrates. The peptide fusion to this enzyme made the post-panning steps very fast and simple. The concentrations of β-lactamase-peptide fusions in phage samples, lysates and purified fusion proteins were normalized based on the β-lactamase activity. The clone screening was also based on assaying the residual cell-bound β-lactamase activity. Some of the cancer cell binding β-lactamase-peptide fusion proteins showed cell internalization by both immunofluorescence and β-lactamase activity-based procedures. The staining with FRET-based substrate CCF4 confirmed the functional integrity of the internalized β-lactamase, and demonstrated that at least a part of the internalized enzyme conjugate could escape the endosomal degradation pathway in intact form and reacted with the substrate present in the cytoplasm. The specificity of the selected ligands was assessed by studying their binding and internalization in 11 other cancer and non-cancer cell lines. The β-lactamase fusion to peptides not only accelerates the clone screening process but can also facilitate the tracking of ligand molecules in various biological studies. The cancer-specific affinity reagents selected from these libraries have a potential for their use in targeted therapies. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 1769. doi:10.1158/1538-7445.AM2011-1769
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2011-1769
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2011
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 10
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    Abstract LB-267: GRB7: A novel target in basal breast cancer
    American Association for Cancer Research (AACR) ; 2010
    In:  Cancer Research Vol. 70, No. 8_Supplement ( 2010-04-15), p. LB-267-LB-267
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 70, No. 8_Supplement ( 2010-04-15), p. LB-267-LB-267
    Abstract: Basal breast cancers lack expression of estrogen and progesterone receptors and HER2, rendering them non-responsive to the most commonly used targeted therapies in breast cancer. These tumors are typically more aggressive, more locally invasive and more likely to metastasize to the brain than other breast cancer subtypes and, consequently, have a poor prognosis. GRB7 is a cytoplasmic adaptor protein that interacts with receptor tyrosine kinases, relaying information to their downstream signaling cascades. It also plays a role in integrin signaling and cell migration by binding focal adhesion kinase (FAK) and ephrin receptors. It is a part of the HER2 amplicon and is frequently overexpressed in HER2-amplified breast tumors. Breast tumors in which HER2 and GRB7 are both co-amplified and co-overexpressed have a poor prognosis. We and others have recently determined that high levels of GRB7 are associated with recurrence in women with triple-negative breast cancer treated with anthracyclines (Sparano et al. J Clin Oncol 27(15s) 500). In this study, we have tested the hypothesis that triple-negative breast cancer cell lines are dependent on GRB7 for proliferation, migration and invasion. We have utilized a highly specific cell-penetrating peptide inhibitor of GRB7 (G7-18NATE) and tested its effects on a panel of 5 basal breast cancer cell lines in a series of culture assays: monolayer wound healing assays (motility on 2D substrates), transwell invasion assays (in vitro invasiveness) and 3D Matrigel cultures (morphogenesis in 3D environment). In all cases evaluated, the Grb7 inhibitory peptide impaired the proliferation, migration and invasion of these cell lines, even though these cells express low levels of GRB7 compared to HER2-amplified cell lines. These data implicate GRB7 as a key mediator of several important phenotypes of basal breast cancer cells and suggest that GRB7 itself, or GRB7-dependent pathways, may prove to be important targets for the development of specific therapies for this disease. This work was supported in part by Susan G. Komen for the Cure (KG091136). Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr LB-267.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM10-LB-267
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2010
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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