Catherine F. Foulon
Duke University
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Featured researches published by Catherine F. Foulon.
Nuclear Medicine and Biology | 1999
Craig J. Reist; Catherine F. Foulon; Kevin L. Alston; Darell D. Bigner; Michael R. Zalutsky
Monoclonal antibodies (MAbs) such as the anti-epidermal growth factor variant III (EGFRvIII) MAb L8A4 are rapidly internalized, which can lead to rapid loss of radioactivity from the tumor cell. The aim of this study was to evaluate the potential utility of N-succinimidyl 5-[211At]astato-3-pyridinecarboxylate ([211At]SAPC) for labeling murine L8A4 with 211At. SAPC was synthesized by astatodestannylation of N-succinimidyl 5-tri-n-butylstannyl 3-pyridinecarboxylate and then coupled to L8A4 in approximately 50% yield. The affinity and immunoreactive fraction for 211At-labeled L8A4 were comparable to those obtained when the MAb was labeled with 131I via N-succinimidyl 5-[131I]iodo-3-pyridinecarboxylate (SIPC). Paired-label comparisons of the 211At- and 131I-labeled MAbs demonstrated similar internalization and catabolism by EGFRvIII-positive cells in vitro, and with the exception of the stomach, similar tissue distribution in athymic mice with EGFRvIII-expressing U87MGdeltaEGFR xenografts. These results suggest that SAPC may be a useful reagent for labeling L8A4, and possibly other internalizing proteins, with 211At.
Nuclear Medicine and Biology | 1999
Michael R. Zalutsky; Fengji Xu; Yinhua Yu; Catherine F. Foulon; Xiao-Guang Zhao; Susan Slade; Donna J. Affleck; Robert C. Bast
Monoclonal antibody (MAb) internalization can have a major effect on tumor retention of radiolabel. Two anti-HER-2/neu MAbs (TA1 and 520C9) were radioiodinated using the iodogen, N-succinimidyl 5-iodo-3-pyridinecarboxylate (SIPC), and tyramine-cellobiose (TCB) methods. Paired-label studies compared internalization and cellular processing of the labeled MAbs by SKOv3 9002-18 ovarian cancer cells in vitro. Intracellular radioiodine activity for 520C9 was up to 2.6 and 3.0 times higher for SIPC and TCB labeling, respectively, compared with iodogen. Likewise, intracellular activity for TA1 was up to 2.3 and 2.9 times higher with the SIPC and TCB methods compared with iodogen labeling. Unfortunately, similar advantages in tumor accumulation were not achieved in athymic mice bearing SKOv3 9008-18 ovarian cancer xenografts.
Nuclear Medicine and Biology | 1998
Catherine F. Foulon; Kevin L. Alston; Michael R. Zalutsky
We report herein the preparation and biological evaluation of two radioastatinated biotin conjugates, (3-[211At]astatobenzoyl)norbiotinamide and ((5-[211At]astato-3-pyridinyl)carbonyl)norbiotinamide. Both conjugates were stable in the presence of human serum and cerebrospinal fluid as well as murine serum, indicating a resistance to degradation to biotinidase. The normal tissue clearance of (3-[211At]astatobenzoyl)norbiotinamide and ((5-[211At]astato-3-pyridinyl)carbonyl)norbiotinamide was rapid, as observed previously with their iodo analogues. Also reported are the first syntheses of N-succinimidyl 5-[211At]astato-3-pyridinecarboxylate and 3-[211At]astatoaniline, two reagents of potential utility for labeling proteins and peptides with 211At.
Nuclear Medicine and Biology | 2001
Catherine F. Foulon; Philip Welsh; Darell D. Bigner; Michael R. Zalutsky
Receptor-mediated internalization of monoclonal antibodies (mAbs), such as those specific for the epidermal growth factor receptor variant III (EGFRvIII), can lead to rapid loss of radioactivity from the target cell. In the current study, the anti-EGFRvIII mAb L8A4 was radioiodinated using two methods -N-succinimidyl 5-iodo-3-pyridinecarboxylate (SIPC) and via a D-amino acid peptide LysArgTyrArgArg (D-KRYRR). Paired-label internalization assays performed on EGFRvIII-expressing U87DeltaEGFR cells in vitro demonstrated that labeling L8A4 using D-KRYRR resulted in significantly higher retention of radioiodine in the intracellular compartment. In athymic mice with D256 human glioma xenografts, tumor uptake was similar for both labeling methods through 24 hr. However, an up to fourfold higher tumor retention was observed for mAb labeled with the D-amino acid peptide at later time points. Radiation absorbed dose calculations based on these biodistribution data indicated that L8A4 labeled using D-KRYRR exhibited better tumor-to-normal-organ radiation dose ratios, suggesting that this labeling method may be of particular value for labeling internalizing mAbs.
Nuclear Medicine and Biology | 1997
Catherine F. Foulon; Bent W. Schoultz; Michael R. Zalutsky
Abstract Biotinyl-3-[ 211 At]astatoanilide ([ 211 At]AtBA) was prepared in more than 80% yield by destannylation. In vitro , [ 211 At]AtBA exhibited a high affinity for streptavidin, and was stable after incubation in human serum, cerebrospinal fluid and distilled water, whereas it was rapidly degraded in mouse serum. HPLC analysis showed that the main degradation pathway in mouse serum was the cleavage of [ 211 At]astatoaniline. In mice, [ 211 At]AtBA and its 125 I-labeled analogue cleared rapidly from most tissues; however, there was some evidence for dehalogenation of both tracers.
Bioconjugate Chemistry | 2004
D. Scott Wilbur; Ming Kuan Chyan; Donald K. Hamlin; Brian B. Kegley; Reudi Risler; Pradip M. Pathare; Janna E. Quinn; Robert L. Vessella; Catherine F. Foulon; Michael R. Zalutsky; Timothy J. Wedge; M. Frederick Hawthorne
Cancer Research | 2000
Catherine F. Foulon; Craig J. Reist; Darell D. Bigner; Michael R. Zalutsky
Clinical Cancer Research | 1999
Chien-Tsun Kuan; Craig J. Reist; Catherine F. Foulon; Ian A. J. Lorimer; Gary E. Archer; Charles N. Pegram; Ira Pastan; Michael R. Zalutsky; Darell D. Bigner
Bioconjugate Chemistry | 1997
Catherine F. Foulon; Kevin L. Alston; Michael R. Zalutsky
Bioconjugate Chemistry | 1999
Catherine F. Foulon; Darell D. Bigner; Michael R. Zalutsky