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4 results on '"L-[ring-13C6]-Tyrosine"'

1. Mass spectrometry imaging of L-[ring-13C6]-labeled phenylalanine and tyrosine kinetics in non-small cell lung carcinoma

Author

Jianhua Cao, Benjamin Balluff, Martijn Arts, Ludwig J. Dubois, Luc J. C. van Loon, Tilman M. Hackeng, Hans M. H. van Eijk, Gert Eijkel, Lara R. Heij, Zita Soons, Steven W. M. Olde Damink, and Ron M. A. Heeren

Subjects
L-[ring-13C6]-Phenylalanine, L-[ring-13C6]-Tyrosine, Amino acids, Isotope labeling, Tumor, Mass spectrometry imaging, Neoplasms. Tumors. Oncology. Including cancer and carcinogens, RC254-282
Abstract

Abstract Background Metabolic reprogramming is a common phenomenon in tumorigenesis and tumor progression. Amino acids are important mediators in cancer metabolism, and their kinetics in tumor tissue are far from being understood completely. Mass spectrometry imaging is capable to spatiotemporally trace important endogenous metabolites in biological tissue specimens. In this research, we studied L-[ring-13C6]-labeled phenylalanine and tyrosine kinetics in a human non-small cell lung carcinoma (NSCLC) xenografted mouse model using matrix-assisted laser desorption/ionization Fourier-transform ion cyclotron resonance mass spectrometry imaging (MALDI-FTICR-MSI). Methods We investigated the L-[ring-13C6]-Phenylalanine (13C6-Phe) and L-[ring-13C6]-Tyrosine (13C6-Tyr) kinetics at 10 min (n = 4), 30 min (n = 3), and 60 min (n = 4) after tracer injection and sham-treated group (n = 3) at 10 min in mouse-xenograft lung tumor tissues by MALDI-FTICR-MSI. Results The dynamic changes in the spatial distributions of 19 out of 20 standard amino acids are observed in the tumor tissue. The highest abundance of 13C6-Phe was detected in tumor tissue at 10 min after tracer injection and decreased progressively over time. The overall enrichment of 13C6-Tyr showed a delayed temporal trend compared to 13C6-Phe in tumor caused by the Phe-to-Tyr conversion process. Specifically, 13C6-Phe and 13C6-Tyr showed higher abundances in viable tumor regions compared to non-viable regions. Conclusions We demonstrated the spatiotemporal intra-tumoral distribution of the essential aromatic amino acid 13C6-Phe and its de-novo synthesized metabolite 13C6-Tyr by MALDI-FTICR-MSI. Our results explore for the first time local phenylalanine metabolism in the context of cancer tissue morphology. This opens a new way to understand amino acid metabolism within the tumor and its microenvironment.

Published
2021
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3. Mass spectrometry imaging of L-[ring-13C6]-labeled phenylalanine and tyrosine kinetics in non-small cell lung carcinoma

Author

Lara R. Heij, Benjamin Balluff, Steven W.M. Olde Damink, Hans M.H. van Eijk, Martijn Arts, Gert B. Eijkel, Luc J. C. van Loon, Ludwig Dubois, Zita Soons, Tilman M. Hackeng, Ron M. A. Heeren, Jianhua Cao, Physiotherapy, Human Physiology and Anatomy, Human Physiology and Sports Physiotherapy Research Group, RS: Carim - B01 Blood proteins & engineering, Imaging Mass Spectrometry (IMS), RS: M4I - Imaging Mass Spectrometry (IMS), Surgery, RS: NUTRIM - R2 - Liver and digestive health, Precision Medicine, RS: GROW - R2 - Basic and Translational Cancer Biology, Humane Biologie, RS: NUTRIM - R3 - Respiratory & Age-related Health, Biochemie, and MUMC+: MA Heelkunde (9)

Subjects
L-[ring-C-13(6)]-Phenylalanine, Metabolite, TUMOR HETEROGENEITY, L-[ring-C-13(6)]-Tyrosine, PROTEIN, Phenylalanine, METABOLISM, Mass spectrometry imaging, chemistry.chemical_compound, Metabolomics, Aromatic amino acids, Tyrosine, RC254-282, chemistry.chemical_classification, Tumor, Neoplasms. Tumors. Oncology. Including cancer and carcinogens, MUSCLE, CANCER, Amino acid, Psychiatry and Mental health, chemistry, Biochemistry, Tumor progression, L-[ring-13C6]-Phenylalanine, L-[ring-13C6]-Tyrosine, Amino acids, Isotope labeling
Abstract

Cancer & metabolism 9, 26 (2021). doi:10.1186/s40170-021-00262-9, Published by Biomed Central, London

Published
2021

4. Mass spectrometry imaging of L-[ring

Author

Jianhua, Cao, Benjamin, Balluff, Martijn, Arts, Ludwig J, Dubois, Luc J C, van Loon, Tilman M, Hackeng, Hans M H, van Eijk, Gert, Eijkel, Lara R, Heij, Zita, Soons, Steven W M, Olde Damink, and Ron M A, Heeren

Subjects
Mass spectrometry imaging, Tumor, L-[ring-13C6]-Phenylalanine, L-[ring-13C6]-Tyrosine, Amino acids, Rapid Communication, Isotope labeling
Abstract

Background Metabolic reprogramming is a common phenomenon in tumorigenesis and tumor progression. Amino acids are important mediators in cancer metabolism, and their kinetics in tumor tissue are far from being understood completely. Mass spectrometry imaging is capable to spatiotemporally trace important endogenous metabolites in biological tissue specimens. In this research, we studied L-[ring-13C6]-labeled phenylalanine and tyrosine kinetics in a human non-small cell lung carcinoma (NSCLC) xenografted mouse model using matrix-assisted laser desorption/ionization Fourier-transform ion cyclotron resonance mass spectrometry imaging (MALDI-FTICR-MSI). Methods We investigated the L-[ring-13C6]-Phenylalanine (13C6-Phe) and L-[ring-13C6]-Tyrosine (13C6-Tyr) kinetics at 10 min (n = 4), 30 min (n = 3), and 60 min (n = 4) after tracer injection and sham-treated group (n = 3) at 10 min in mouse-xenograft lung tumor tissues by MALDI-FTICR-MSI. Results The dynamic changes in the spatial distributions of 19 out of 20 standard amino acids are observed in the tumor tissue. The highest abundance of 13C6-Phe was detected in tumor tissue at 10 min after tracer injection and decreased progressively over time. The overall enrichment of 13C6-Tyr showed a delayed temporal trend compared to 13C6-Phe in tumor caused by the Phe-to-Tyr conversion process. Specifically, 13C6-Phe and 13C6-Tyr showed higher abundances in viable tumor regions compared to non-viable regions. Conclusions We demonstrated the spatiotemporal intra-tumoral distribution of the essential aromatic amino acid 13C6-Phe and its de-novo synthesized metabolite 13C6-Tyr by MALDI-FTICR-MSI. Our results explore for the first time local phenylalanine metabolism in the context of cancer tissue morphology. This opens a new way to understand amino acid metabolism within the tumor and its microenvironment. Supplementary Information The online version contains supplementary material available at 10.1186/s40170-021-00262-9.

Published
2020

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