scholarly journals Evaluation of 3-l- and 3-d-[18F]Fluorophenylalanines as PET Tracers for Tumor Imaging

Cancers ◽  
2021 ◽  
Vol 13 (23) ◽  
pp. 6030
Author(s):  
Felicia Krämer ◽  
Benedikt Gröner ◽  
Chris Hoffmann ◽  
Austin Craig ◽  
Melanie Brugger ◽  
...  
Keyword(s):  
Amino Acid ◽  
Tumor Imaging ◽  
Human Tumor ◽  
Transport Systems ◽  
Acid Decarboxylase ◽  
Tumor Xenografts ◽  
Tumor Delineation ◽  
Mcf 7

Purpose: The preclinical evaluation of 3-l- and 3-d-[18F]FPhe in comparison to [18F]FET, an established tracer for tumor imaging. Methods: In vitro studies were conducted with MCF-7, PC-3, and U87 MG human tumor cell lines. In vivo µPET studies were conducted in healthy rats with/without the inhibition of peripheral aromatic l-amino acid decarboxylase by benserazide pretreatment (n = 3 each), in mice bearing subcutaneous MCF-7 or PC-3 tumor xenografts (n = 10), and in rats bearing orthotopic U87 MG tumor xenografts (n = 14). Tracer accumulation was quantified by SUVmax, SUVmean and tumor-to-brain ratios (TBrR). Results: The uptake of 3-l-[18F]FPhe in MCF-7 and PC-3 cells was significantly higher relative to [18F]FET. The uptake of all three tracers was significantly reduced by the suppression of amino acid transport systems L or ASC. 3-l-[18F]FPhe but not 3-d-[18F]FPhe exhibited protein incorporation. In benserazide-treated healthy rats, brain uptake after 42–120 min was significantly higher for 3-d-[18F]FPhe vs. 3-l-[18F]FPhe. [18F]FET showed significantly higher uptake into subcutaneous MCF-7 tumors (52–60 min p.i.), while early uptake into orthotopic U87 MG tumors was significantly higher for 3-l-[18F]FPhe (SUVmax: 3-l-[18F]FPhe, 107.6 ± 11.3; 3-d-[18F]FPhe, 86.0 ± 4.3; [18F]FET, 90.2 ± 7.7). Increased tumoral expression of LAT1 and ASCT2 was confirmed immunohistologically. Conclusion: Both novel tracers enable accurate tumor delineation with an imaging quality comparable to [18F]FET.

In vitro and in vivo anticancer activity of mitozolomide and sparsomycin in human tumor xenografts, murine tumors and human bone marrow

1990 ◽  
Vol 116 (6) ◽  
pp. 550-556 ◽  
Author(s):  
Heinz H. Fiebig ◽  
Dietmar P. Berger ◽  
Karin Köpping ◽  
Harry C. J. Ottenheijm ◽  
Zbigniew Zylicz
Keyword(s):  
Bone Marrow ◽  
Anticancer Activity ◽  
Human Tumor ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Human Tumor Xenografts ◽  
Tumor Xenografts ◽  
Murine Tumors

In vitro and in vivo evaluation of US-NCI compounds in human tumor xenografts

1990 ◽  
Vol 17 (2-3) ◽  
pp. 109-117 ◽  
Author(s):  
Heinz-Herbert Fiebig ◽  
Dietmar P. Berger ◽  
Bernd R. Winterhalter ◽  
Jacqueline Plowman
Keyword(s):  
Human Tumor ◽  
In Vivo Evaluation ◽  
Human Tumor Xenografts ◽  
Tumor Xenografts

The Localization and Functional Contribution of Striatal Aromatic L-Amino Acid Decarboxylase to L-3,4-Dihydroxyphenylalanine Decarboxylation in Rodent Parkinsonian Models

2000 ◽  
Vol 9 (5) ◽  
pp. 567-576 ◽  
Author(s):  
Ken Nakamura ◽  
Maqbool Ahmed ◽  
Eliav Barr ◽  
Jeffrey M. Leiden ◽  
Un Jung Kang
Keyword(s):  
Amino Acid ◽  
Dopaminergic Neurons ◽  
Primary Source ◽  
Therapeutic Strategies ◽  
Acid Decarboxylase ◽  
Striatal Neurons ◽  
Amino Acid Decarboxylase ◽  
Cellular Transplantation

L-3,4-Dihydroxyphenylalanine (L-dopa) is the mainstay of therapy for patients with Parkinson's disease (PD), and mediates its primary effects through conversion into dopamine by aromatic L-amino acid decarboxylase (AADC). Given the loss of AADC-containing nigrostriatal dopaminergic neurons in PD, however, the location of residual AADC that converts L-dopa into dopamine remains controversial. The first objective of this study was to establish the presence of AADC expression in striatal neurons and glia using reverse transcriptase and PCR. Transcripts for the neuronal but not nonneuronal forms of AADC were detected in striatal tissue, cultured striatal neurons, and glia. We then examined whether this striatal AADC expression represents a physiologically significant source of dopamine production. No dopamine release was detected following incubation of striatal cultures with L-dopa or transduction with adenovirus expressing tyrosine hydroxylase. Our data establish the presence of AADC expression in the striatum both in vivo and in vitro, but suggest that striatal components do not represent a primary source of L-dopa decarboxylation following nigrostriatal denervation in rats. Understanding the source and localization of AADC is important in understanding the complications of L-dopa therapy and in designing rational therapeutic strategies for PD, including cellular transplantation and gene therapy.

scholarly journals Chloroform Fraction ofCentratherum anthelminticum(L.) Seed Inhibits Tumor Necrosis Factor Alpha and Exhibits Pleotropic Bioactivities: Inhibitory Role in Human Tumor Cells

2012 ◽  
Vol 2012 ◽  
pp. 1-11 ◽  
Author(s):  
Aditya Arya ◽  
Mouna Achoui ◽  
Shiau-Chuen Cheah ◽  
Siddig Ibrahim Abdelwahab ◽  
Putri Narrima ◽  
...  
Keyword(s):  
Inflammatory Responses ◽  
Human Tumor ◽  
Toxicity Testing ◽  
Antioxidant Property ◽  
Chloroform Fraction ◽  
Necrosis Factor Alpha ◽  
Tnf Α ◽  
Mcf 7

We investigated the antioxidant potential, cytotoxic effect, and TNF-α inhibition activity with NF-κB activation response in a chloroform fraction ofCentratherum anthelminticumseeds (CACF). The antioxidant property of CACF was evaluated with DPPH, ORAC, and FRAP assays, which demonstrated significant antioxidant activity. The cytotoxicity of CACF was tested using the MTT assay; CACF effective inhibitory concentrations (IC50) for A549, PC-3, MCF-7, and WRL-68 cells were31.42±5.4,22.61±1.7,8.1±0.9, and54.93±8.3 μg/mL, respectively. CACF effectively and dose-dependently inhibited TNF-α release,in vitroandin vivo. CACF inhibited TNF-α secretion in stimulated RAW264.7 macrophage supernatants with an IC50of 0.012 μg/mL, without affecting their viability; the highest dose tested reduced serum TNF-α by 61%. Acute toxicity testing in rats revealed that CACF was non-toxic at all doses tested. Matching the cytotoxic activity towards a mechanistic approach, CACF dose-dependently exhibitedin vitroinhibitory effects against the activation of NF-κB translocation in MCF-7 cells. Preliminary phytochemical screening with GC/MS analysis detected 22 compounds in CACF, of which morpholinoethyl isothiocyanate was the most abundant (29.04%). The study reveals the potential of CACF in the treatment of breast cancer and in oxidative stress conditions with associated inflammatory responses.

Monoclonal Antibodies to Six-Transmembrane Epithelial Antigen of the Prostate-1 Inhibit Intercellular Communication In vitro and Growth of Human Tumor Xenografts In vivo

2007 ◽  
Vol 67 (12) ◽  
pp. 5798-5805 ◽  
Author(s):  
Pia M. Challita-Eid ◽  
Kendall Morrison ◽  
Soudabeh Etessami ◽  
Zili An ◽  
Karen J. Morrison ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Intercellular Communication ◽  
Human Tumor ◽  
Human Tumor Xenografts ◽  
Tumor Xenografts
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