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| 024 | 7 | _ | |a 10.1016/j.jim.2015.04.024 |2 doi |
| 024 | 7 | _ | |a pmid:25967950 |2 pmid |
| 024 | 7 | _ | |a 0022-1759 |2 ISSN |
| 024 | 7 | _ | |a 1872-7905 |2 ISSN |
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| 037 | _ | _ | |a DKFZ-2017-02704 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 610 |
| 100 | 1 | _ | |a Hazin, John |0 P:(DE-HGF)0 |b 0 |e First author |
| 245 | _ | _ | |a A novel method for measuring cellular antibody uptake using imaging flow cytometry reveals distinct uptake rates for two different monoclonal antibodies targeting L1. |
| 260 | _ | _ | |a Amsterdam [u.a.] |c 2015 |b Elsevier Science |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1508416161_6998 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Monoclonal antibodies (mAbs) have emerged as a promising tool for cancer therapy. Differing approaches utilize mAbs to either deliver a drug to the tumor cells or to modulate the host's immune system to mediate tumor kill. The rate by which a therapeutic antibody is being internalized by tumor cells is a decisive feature for choosing the appropriate treatment strategy. We herein present a novel method to effectively quantitate antibody uptake of tumor cells by using image-based flow cytometry, which combines image analysis with high throughput of sample numbers and sample size. The use of this method is established by determining uptake rate of an anti-EpCAM antibody (HEA125), from single cell measurements of plasma membrane versus internalized antibody, in conjunction with inhibitors of endocytosis. The method is then applied to two mAbs (L1-9.3, L1-OV52.24) targeting the neural cell adhesion molecule L1 (L1CAM) at two different epitopes. Based on median cell population responses, we find that mAb L1-OV52.24 is rapidly internalized by the ovarian carcinoma cell line SKOV3ip while L1 mAb 9.3 is mainly retained at the cell surface. These findings suggest the L1 mAb OV52.24 as a candidate to be further developed for drug-delivery to cancer cells, while L1-9.3 may be optimized to tag the tumor cells and stimulate immunogenic cancer cell killing. Furthermore, when analyzing cell-to-cell variability, we observed L1 mAb OV52.24 rapidly transition into a subpopulation with high-internalization capacity. In summary, this novel high-content method for measuring antibody internalization rate provides a high level of accuracy and sensitivity for cell population measurements and reveals further biologically relevant information when taking into account cellular heterogeneity. |
| 536 | _ | _ | |a 312 - Functional and structural genomics (POF3-312) |0 G:(DE-HGF)POF3-312 |c POF3-312 |f POF III |x 0 |
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| 650 | _ | 7 | |a Antibodies, Monoclonal |2 NLM Chemicals |
| 650 | _ | 7 | |a Antigens, Neoplasm |2 NLM Chemicals |
| 650 | _ | 7 | |a CADM1 protein, human |2 NLM Chemicals |
| 650 | _ | 7 | |a Cell Adhesion Molecules |2 NLM Chemicals |
| 650 | _ | 7 | |a EPCAM protein, human |2 NLM Chemicals |
| 650 | _ | 7 | |a Epithelial Cell Adhesion Molecule |2 NLM Chemicals |
| 650 | _ | 7 | |a Immunoglobulins |2 NLM Chemicals |
| 700 | 1 | _ | |a Moldenhauer, Gerhard |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Altevogt, Peter |0 P:(DE-He78)e6057131c71c90a6fcf61035f12b46c3 |b 2 |u dkfz |
| 700 | 1 | _ | |a Brady, Nathan R |0 P:(DE-He78)5bf984e94f0a31773a103cd293e01f92 |b 3 |e Last author |u dkfz |
| 773 | _ | _ | |a 10.1016/j.jim.2015.04.024 |g Vol. 423, p. 70 - 77 |0 PERI:(DE-600)1500495-8 |p 70 - 77 |t Journal of immunological methods |v 423 |y 2015 |x 0022-1759 |
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