Differential tumor-targeting abilities of three single-domain antibody formats

Bell, Andrea M.; Wang, Zheng J.; Arbabi‐Ghahroudi, Mehdi; Chang, T. Arthur; Durocher, Yves; Trojahn, Ulrike; Baardsnes, Jason; Jaramillo, María; Li, Sheng‐Hua; Baral, Toya Nath; O’Connor-McCourt, Maureen D.; MacKenzie, Ross; Zhang, Jianbing

doi:10.1016/j.canlet.2009.08.003

Cited by 102 publications

(71 citation statements)

References 38 publications

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“…Yves Durocher of the NRC, Canada kindly provided the cell line (CHODG44-EG2-hFc/clone 1A7). 31 The cells were cultured in 250 mL baffled shaker flasks (VWR International, Radnor, PA) at 120 rpm in an incubator at 37 C with 10% CO 2 overlay. The cells were grown in BioGro-CHO serum-free medium (BioGro Technologies, Winnipeg, MB) supplemented with 0.5 g/L yeast extract (BD, Sparks, MD), 1 mM glutamine (Sigma, St. Louis, MO), and 4 mM GlutaMax I (Invitrogen, Grand Island, NY).…”

Section: Cell Preparationmentioning

confidence: 99%

Monitoring the dielectric response of single cells following mitochondrial adenosine triphosphate synthase inhibition by oligomycin using a dielectrophoretic cytometer

et al. 2014

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One of the main uses of adenosine triphosphate (ATP) within mammalian cells is powering the Na þ /K þ ATPase pumps used to maintain ion concentrations within the cell. Since ion concentrations determine the cytoplasm conductivity, ATP concentration is expected to play a key role in controlling the cytoplasm conductivity. The two major ATP production pathways within cells are via glycolysis within the cytoplasm and via the electron transport chain within the mitochondria. In this work, a differential detector combined with dielectrophoretic (DEP) translation in a microfluidic channel was employed to observe single cell changes in the cytoplasm conductivity. The DEP response was made sensitive to changes in cytoplasm conductivity by measuring DEP response versus media conductivity and using double shell models to choose appropriate frequencies and media conductivity. Dielectric response of Chinese hamster ovary (CHO) cells was monitored following inhibition of the mitochondria ATP production by treatment with oligomycin. We show that in CHO cells following exposure to oligomycin (8 lg/ml) the cytoplasm conductivity drops, with the majority of the change occurring within 50 min. This work demonstrates that dielectric effects due to changes in ATP production can be observed at the single cell level. V C 2014 AIP Publishing LLC.

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Section: Cell Preparationmentioning

confidence: 99%

Monitoring the dielectric response of single cells following mitochondrial adenosine triphosphate synthase inhibition by oligomycin using a dielectrophoretic cytometer

et al. 2014

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“…Another pentabody V2C-EG2 (108 kDa) was constructed and then was labeled with 64 Cu using 1,4,7,10-tetraazacyclododecane-N,N′,N″,N‴-tetraacetic acid (DOTA) as a chelating agent for microPET/CT imaging in mouse tumor models; the results showed that 64 Cu-DOTA-V2C-EG2 failed to target EGFR in xenografted mice, which suggest that EG2-V2C is not an efficient probe. 24 Among the abovementioned multimers, we have reason to believe that EG2-COMP is the most promising antibody in tumor imaging and possible tumor therapy.…”

Section: Biodistribution Studiesmentioning

confidence: 99%

^99mTc‐labeled tetramer and pentamer of single‐domain antibody for targeting epidermal growth factor receptor in xenografted tumors

Feng

Xia

et al. 2016

Labelled Comp Radiopharmac

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The single-domain antibody EG2 can be fused with right-handed coiled-coil (RHCC) and human cartilage oligomeric matrix protein (COMP), to form the multivalent antibodies EG2-RHCC and EG2-COMP. We labeled these two antibodies with (99m) Tc and assessed their targeting efficiency for epidermal growth factor receptor (EGFR). Cell binding, uptake, efflux, and blocking studies were performed with EGFR high- and/or low-expressing cells with (99m) Tc-labeled EG2-RHCC or EG2-COMP. Single photon-emission computed tomography (SPECT) imaging and biodistribution studies were further carried out. Both (99m) Tc-EG2-RHCC and (99m) Tc-EG2-COMP can specially bind to EGFR in vitro. SPECT imaging showed that A431, which expresses high levels of EGFR, was clearly visible 6 h after (99m) Tc-EG2-COMP injection; however, it was not detectable after administration of (99m) Tc-EG2-RHCC. Uptake of both antibodies by the non-EGFR-secreting OCM-1 tumors was low. EG2-COMP shows promise in identifying EGFR over-expression in tumors; however, EG2-RHCC may not be suitable for targeting EGFR in vivo.

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“…Mutagenesis and recombination of CDR regions to improve the affinity and specificity of sdAb fragments have also been discussed Fanning and Horn 2011). Current studies are focused on the development of new cloning and expression strategies to produce humanised fragments, multivalent constructs and fusions of antibody fragments to other proteins (Saerens et al 2005;Vincke et al 2009;Bell et al 2010;Pollithy et al 2011). Selected articles are presented in Table 4.…”

Section: Production Of Sdab Fragments Using Recombinant Technologymentioning

confidence: 99%

Single-domain antibody fragments derived from heavy-chain antibodies: a review

Eyer¹,

Hruška²

2012

Vet. Med.

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Single-domain antibody (sdAb) fragments derived from heavy-chain antibodies of camelids and cartilaginous fish represent a new generation of therapeutic agents and immunoreagents. Due to their unique characteristics, such as low molecular weight, high physical-chemical stability, good water solubility, and the ability to bind antigens inaccessible to conventional antibodies, they could potentially act as a substitute for conventional therapeutic drugs in the treatment of serious human diseases, and, moreover, could be broadly used in analyses and diagnostics. In this review article, an analysis of 826 publications oriented to heavy-chain antibodies and their sdAb fragments indexed in the Web of Science ® database since 1993 has been carried out. Attention has predominantly been paid to papers published from 2010 to June 2012. Key publications are presented in tables and are characterised by descriptive words, abstracts and references. The presented publications have been sorted according to seven basic criteria: review articles and monographs, heavy-chain antibodies of camelids and sharks, production of sdAb fragments using recombinant technology, characteristic properties of sdAb fragments, application of sdAb fragments in therapy, application of sdAb fragments in diagnostic and immunoanalytical methods and other prospective uses of sdAb fragments. This review article should highlight the typical properties of heavy-chain antibodies and sdAb fragments which differentiate them from conventional antibodies and other available recombinant fragments, and also emphasize their extremely broad application potential, mainly in human disease therapy. At the same time it allows an easy and rapid orientation in numerous publications written on this subject, and facilitates the search for the required data.

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Differential tumor-targeting abilities of three single-domain antibody formats

Cited by 102 publications

References 38 publications

Monitoring the dielectric response of single cells following mitochondrial adenosine triphosphate synthase inhibition by oligomycin using a dielectrophoretic cytometer

Monitoring the dielectric response of single cells following mitochondrial adenosine triphosphate synthase inhibition by oligomycin using a dielectrophoretic cytometer

^99mTc‐labeled tetramer and pentamer of single‐domain antibody for targeting epidermal growth factor receptor in xenografted tumors

Single-domain antibody fragments derived from heavy-chain antibodies: a review

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