Analysis of endogenous ATP analogs and mevalonate pathway metabolites in cancer cell cultures using liquid chromatography–electrospray ionization mass spectrometry

Jauhiainen, Marjo; Mönkkönen, Hannu; Räikkönen, Johanna; Mönkkönen, Jukka; Auriola, Seppo

doi:10.1016/j.jchromb.2009.07.010

Cited by 39 publications

(37 citation statements)

References 46 publications

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“…Until now, this has been attributed to their action on MVP downstream from FPPS by rescuing protein prenylation, but here we show that they could simultaneously act also upstream from [14,39], and both isomers for conjugation reaction to AMP to form ATP analogs, ApppI and ApppD [17,22]. The reversible reaction involved in the transformation of the relatively unreactive IPP into the relatively reactive isomer DMAPP is catalyzed by IPP isomerase enzyme [41,42].…”

Section: Discussionmentioning

confidence: 68%

“…In our previous studies, only the mixture of the isomeric molecules has been analyzed, but recently we have described a method which is capable of quantifying the relative amount of both isomers, IPP and DMAPP, in cell extracts [22]. Using this procedure, we discovered that there were no differences in the isomerization capacity of the enzyme between the treatments (Fig.…”

Section: Page 14 Of 35mentioning

confidence: 95%

“…6 However, in addition to the loss of prenylated proteins, inhibition of FPPS by NBPs in the MVP causes intracellular accumulation of isopentenyl pyrophosphate (IPP) and consequently induces the biosynthesis of a novel pro-apoptotic ATP analog ApppI (triphosphoric acid 1-adenosin-5'-yl ester 3-(3-methylbut-3-enyl) ester), in vitro [17][18][19][20] and in vivo [19,21]. Recently we observed that in addition to IPP/ApppI formation, NBPs induce isomeric dimethylallyl pyrophosphate (DMAPP) accumulation and consequent ApppD (triphosphoric acid 1-adenosin-5'-yl ester 3-(3-methylbut-2-enyl) ester) production [22]. However, for the sake of clarity, IPP/ApppI is used to describe both IPP/DMAPP and ApppI/ApppD formation throughout this text.…”

Section: Introductionmentioning

confidence: 99%

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Mevalonate pathway intermediates downregulate zoledronic acid-induced isopentenyl pyrophosphate and ATP analog formation in human breast cancer cells

Räikkönen

Mönkkönen

Auriola

et al. 2010

Biochemical Pharmacology

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To cite this version:Johanna Räikkönen, Hannu Mönkkönen, Seppo Auriola, Jukka Mönkkönen. Mevalonate pathway intermediates downregulate zoledronic acid-induced isopentenyl pyrophosphate and ATP analog formation in human breast cancer cells. Biochemical Pharmacology, Elsevier, 2009, 79 (5) This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Page 1 of 35A c c e p t e d M a n u s c r i p t A c c e p t e d M a n u s c r i p t 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 This study represents a novel insight into the mechanism of action of MVP intermediates on the regulation of MVP after FPPS inhibition. The data implies that in addition to the previously reported effects on rescuing protein prenylation, MVP intermediates can preserve cell activity by inhibiting the accumulation of IPP/ApppI via

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Section: Discussionmentioning

confidence: 68%

Section: Page 14 Of 35mentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

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Mevalonate pathway intermediates downregulate zoledronic acid-induced isopentenyl pyrophosphate and ATP analog formation in human breast cancer cells

Räikkönen

Mönkkönen

Auriola

et al. 2010

Biochemical Pharmacology

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“…38 As shown in Fig. 5, LS180 cell line stimulated with Zol 5 mM for 24 h (panel Aa) produced about 3-fold or 7-fold IPP than DLD1 (panel Ba) or SW620 (panel Ca) cells, respectively.…”

Section: Differential Ipp Production By Crc Cell Lines Upon Zol Treatmentioning

confidence: 77%

“…IPP production by the CRC cell lines SW620, LS180, DLD1, HCT15 and Colo320, either untreated or exposed to Zol, either as continuous treatment with 5 mM for 24 h, or as pulse treatment of 50 mM and 100 mM for 4 h, as described in Supplementary Materials and Methods, was performed according to Jauhiainen et al 38 with modifications, as detailed in supporting information (Supplementary Materials and Methods).…”

Section: Hplc Negative Ion Electrospray Ionization Tof-msmentioning

confidence: 99%

Zoledronate can induce colorectal cancer microenvironment expressing BTN3A1 to stimulate effector γδ T cells with antitumor activity

et al. 2017

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Amino-bis-phosphonates (N-BPs) such as zoledronate (Zol) have been used in anticancer clinical trials due to their ability to upregulate pyrophosphate accumulation promoting antitumor Vg9Vd2 T cells. The butyrophilin 3A (BTN3A, CD277) family, mainly the BTN3A1 isoform, has emerged as an important structure contributing to Vg9Vd2 T cells stimulation. It has been demonstrated that the B30.2 domain of BTN3A1 can bind phosphoantigens (PAg) and drive the activation of Vg9Vd2 T cells through conformational changes of the extracellular domains. Moreover, BTN3A1 binding to the cytoskeleton, and its consequent membrane stabilization, is crucial to stimulate the PAg-induced tumor cell reactivity by human Vg9Vd2 T cells. Aim of this study was to investigate the relevance of BTN3A1 in N-BPs-induced antitumor response in colorectal cancer (CRC) and the cell types involved in the tumor microenvironment.In this paper, we show that (i) CRC, exposed to Zol, stimulates the expansion of Vd2 T lymphocytes with effector memory phenotype and antitumor cytotoxic activity, besides sensitizing cancer cells to gd T cellmediated cytotoxicity; (ii) this effect is partially related to BTN3A1 expression and in particular with its cellular re-distribution in the membrane and cytoskeleton-associated fraction; (iii) BTN3A1 is detected in CRC at the tumor site, both on epithelial cells and on tumor-associated fibroblasts (TAF), close to areas infiltrated by Vd2 T lymphocytes; (iv) Zol is effective in stimulating antitumor effector Vd2 T cells from exvivo CRC cell suspensions; and (v) both CRC cells and TAF can be primed by Zol to trigger Vd2 T cells.

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LC‐MS Bioanalysis of Intracellular Drugs

Zhang

Bartels

2013

Handbook of LC‐MS Bioanalysis

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Analysis of endogenous ATP analogs and mevalonate pathway metabolites in cancer cell cultures using liquid chromatography–electrospray ionization mass spectrometry

Cited by 39 publications

References 46 publications

Mevalonate pathway intermediates downregulate zoledronic acid-induced isopentenyl pyrophosphate and ATP analog formation in human breast cancer cells

Mevalonate pathway intermediates downregulate zoledronic acid-induced isopentenyl pyrophosphate and ATP analog formation in human breast cancer cells

Zoledronate can induce colorectal cancer microenvironment expressing BTN3A1 to stimulate effector γδ T cells with antitumor activity

LC‐MS Bioanalysis of Intracellular Drugs

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