Reactions of a glucosinolate breakdown product (benzyl isothiocyanate) with myoglobin

Rawel, Harshadrai M.; Kroll, J.; Haebel, Sophie; Peter, Martin G.

doi:10.1016/s0031-9422(98)00101-0

Cited by 24 publications

(26 citation statements)

References 8 publications

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“…The study with BSA provides strong evidence that PEITC covalently modifies proteins to a greater extent than SFN and the modifications seem to occur exclusively at the cysteine residues. Other possible important sites of ITC binding include amino group of lysine and hydroxyl group of serine (39,40). Modification of thiols in proteins may have important consequences, as previous studies showed that the binding to cysteines in Keap1 by SFN constitutes a critical step in its induction of phase II enzymes mediated by Nrf2 translocation from cytoplasm to nucleus (15)(16)(17).…”

Section: Discussionmentioning

confidence: 99%

The Role of Protein Binding in Induction of Apoptosis by Phenethyl Isothiocyanate and Sulforaphane in Human Non–Small Lung Cancer Cells

et al. 2007

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Induction of apoptosis underlies a mechanism for inhibiting tumorigenesis by phenethyl isothiocyanate (PEITC) and sulforaphane (SFN). However, the upstream events by which isothiocyanates (ITC) induce apoptosis have not been fully investigated. As electrophiles, ITCs could trigger apoptosis by binding to DNA or proteins or by inducing oxidative stress. To better understand the molecular mechanisms of apoptosis by ITCs, we examined, as a first step, the role of these events in human non-small lung cancer A549 cells. PEITC was a more potent inducer than SFN; it induced apoptosis at 20 Mmol/L, whereas SFN induced at 40 Mmol/L but not at 20 Mmol/L. To study binding with cellular proteins and DNA, cells were treated with 14 C-ITCs; the initial protein binding by PEITC was almost 3-fold than that of SFN. The binding by PEITC increased with time, whereas binding by SFN remained low. Therefore, 4 h after incubation proteins became the predominant targets for PEITC with a 6-fold binding than that of SFN. To characterize the chemical nature of binding by the ITCs, we used bovine serum albumin (BSA) as a surrogate protein. PEITC also modified BSA covalently to a greater extent than SFN occurring exclusively at cysteine residues. Surprisingly, neither PEITC nor SFN bound to DNA or RNA at detectable levels or caused significant DNA strand breakage. The levels of oxidative damage in cells, measured as reactive oxygen species, 8-oxo-deoxyguanosine, and protein carbonyls formation, were greater in cells treated with SFN than PEITC. Because PEITC is a stronger inducer of apoptosis than SFN, these results indicate that direct covalent binding to cellular proteins is an important early event in the induction of apoptosis by the ITCs. [Cancer Res 2007;67(13):6409-16]

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Section: Discussionmentioning

confidence: 99%

The Role of Protein Binding in Induction of Apoptosis by Phenethyl Isothiocyanate and Sulforaphane in Human Non–Small Lung Cancer Cells

et al. 2007

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“…They readily bind to amino acids and proteins forming thiourea derivatives and dithiocarbamate esters. When egg white protein was treated with benzyl-ITC, lysine content and availability was significantly decreased to 60% as well as the bioaccessibility of the ITC [162,163]. According to Björkmann, addition of radiolabelled ITCs at a level normally present to rapeseed meal resulted in a 36% binding of the ITC to meal components.…”

Section: Gastric and Small Intestinal Digestionmentioning

confidence: 99%

Glucosinolates inBrassicavegetables: The influence of the food supply chain on intake, bioavailability and human health

Verkerk¹,

Schreiner

Krumbein

et al. 2009

Molecular Nutrition Food Res

526

424

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Glucosinolates (GLSs) are found in Brassica vegetables. Examples of these sources include cabbage, Brussels sprouts, broccoli, cauliflower and various root vegetables (e.g. radish and turnip). A number of epidemiological studies have identified an inverse association between consumption of these vegetables and the risk of colon and rectal cancer. Animal studies have shown changes in enzyme activities and DNA damage resulting from consumption of Brassica vegetables or isothiocyanates, the breakdown products (BDP) of GLSs in the body. Mechanistic studies have begun to identify the ways in which the compounds may exert their protective action but the relevance of these studies to protective effects in the human alimentary tract is as yet unproven. In vitro studies with a number of specific isothiocyanates have suggested mechanisms that might be the basis of their chemoprotective effects. The concentration and composition of the GLSs in different plants, but also within a plant (e.g. in the seeds, roots or leaves), can vary greatly and also changes during plant development. Furthermore, the effects of various factors in the supply chain of Brassica vegetables including breeding, cultivation, storage and processing on intake and bioavailability of GLSs are extensively discussed in this paper.

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“…Two ll of this solution were brought on to the target and covered with 1 ll sinapic acid as matrix. After crystallization of the sample by air-drying, measurements were carried out on Reflex TM II Bruker MALDI-TOF-MS instrumentation as described in Rawel et al [29].…”

Section: Physicochemical Characterizationmentioning

confidence: 99%

Model studies on reactions of plant phenols with whey proteins

Rawel

Kröll

Höhl

2001

Nahrung

145

115

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Whey proteins were modified by reaction with selected phenolic compounds (ferulic-, chlorogenic-, caffeic- and gallic acid) and related substances (quinic acid and p-quinone) as well as with extracts from coffee, tea, potato and pear at pH 9. The derivatives formed were characterized in terms of their physicochemical and digestion properties. The derivatization was accompanied by a reaction at the lysine and tryptophan side chains, whereby their content was decreased in comparison to that in the control whey proteins. Moreover, the solubility of the derivatives decreased over a broad pH range and the derivatization influenced the hydrophobe-hydrophile character of the whey proteins. The isoelectric points were shifted to lower pH values in the order of reactivity as follows: gallic acid > p-quinone > caffeic acid > chlorogenic acid. The other derivatives showed no or few changes compared to the control whey proteins. The formation of high molecular fractions was documented with SDS-PAGE. Especially the derivatives of chlorogenic-, caffeic-, gallic acid and p-quinone showed an increase in molecular weight of beta-lactoglobulin fraction from 18,300 to 20,000 Da. A dimer formation in molecular range 40,000 was also registered. MALDI-TOF-MS was applied to characterize the binding of the individual phenolic compounds or their oxidation products to the whey protein fractions, alpha-lactalbumin and beta-lactoglobulin. In vitro experiments showed that the digestion of the derivatized whey proteins with the enzymes of the gastrointestinal tract (trypsin, chymotrypsin, pepsin and pancreatin) was adversely effected. Similar results with regard to physicochemical characterization and digestion properties of the whey proteins treated with the applied extracts from plant beverages, fruit and vegetable were also documented. Coffee and tee were comparatively the most reactive extracts.

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Reactions of a glucosinolate breakdown product (benzyl isothiocyanate) with myoglobin

Cited by 24 publications

References 8 publications

The Role of Protein Binding in Induction of Apoptosis by Phenethyl Isothiocyanate and Sulforaphane in Human Non–Small Lung Cancer Cells

The Role of Protein Binding in Induction of Apoptosis by Phenethyl Isothiocyanate and Sulforaphane in Human Non–Small Lung Cancer Cells

Glucosinolates inBrassicavegetables: The influence of the food supply chain on intake, bioavailability and human health

Model studies on reactions of plant phenols with whey proteins

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