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Corrigendum
Su, Q.; Schroder, S.P.; Lelieveld, L.T.; Guimaraes Da Lomba Ferraz, M.J.; Verhoek, M.; Boot, R.G.; ... ; Kuo, C.L. 2023
Corrigendum: xylose-configured cyclophellitols as selective inhibitors for glucocerebrosidase
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Corrigendum: Xylose-configured cyclophellitols as selective inhibitors for glucocerebrosidase
Su, Q.; Schroder, S.P.; Lelieveld, L.T.; Guimaraes Da Lomba Ferraz, M.J.; Verhoek, M.; Boot, R.G.; ... ; Kuo, C.-L. 2023
Corrigendum: Xylose-configured cyclophellitols as selective inhibitors for glucocerebrosidase
Article / Letter to editor
open access
2023-08-02T00:00:00Z

Corrigendum: Xylose-configured cyclophellitols as selective inhibitors for glucocerebrosidase
Su, Q.; Schröder, S.P.; Lelieveld, L.T.; Guimaraes Da Lomba Ferraz M.J.; Verhoek, M.; Boot, R.G.; ... ; Kuo, C.L. 2022
Corrigendum: Xylose-configured cyclophellitols as selective inhibitors for glucocerebrosidase
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Xylose-configured cyclophellitols as selective inhibitors for glucocerebrosidase
Su, Q.; Schröder, S.P.; Lelieveld, L.T.; Ferraz, M.J.; Verhoek, M.; Boot, R.G.; ... ; Kuo, C.L. 2021
Xylose-configured cyclophellitols as selective inhibitors for glucocerebrosidase
Article / Letter to editor
open access
Glucocerebrosidase (GBA), a lysosomal retaining beta-d-glucosidase, has recently been shown to hydrolyze beta-d-xylosides and to transxylosylate cholesterol. Genetic defects in GBA cause the... Show moreGlucocerebrosidase (GBA), a lysosomal retaining beta-d-glucosidase, has recently been shown to hydrolyze beta-d-xylosides and to transxylosylate cholesterol. Genetic defects in GBA cause the lysosomal storage disorder Gaucher disease (GD), and also constitute a risk factor for developing Parkinson's disease. GBA and other retaining glycosidases can be selectively visualized by activity-based protein profiling (ABPP) using fluorescent probes composed of a cyclophellitol scaffold having a configuration tailored to the targeted glycosidase family. GBA processes beta-d-xylosides in addition to beta-d-glucosides, this in contrast to the other two mammalian cellular retaining beta-d-glucosidases, GBA2 and GBA3. Here we show that the xylopyranose preference also holds up for covalent inhibitors: xylose-configured cyclophellitol and cyclophellitol aziridines selectively react with GBA over GBA2 and GBA3 in vitro and in vivo, and that the xylose-configured cyclophellitol is more potent and more selective for GBA than the classical GBA inhibitor, conduritol B-epoxide (CBE). Both xylose-configured cyclophellitol and cyclophellitol aziridine cause accumulation of glucosylsphingosine in zebrafish embryo, a characteristic hallmark of GD, and we conclude that these compounds are well suited for creating such chemically induced GD models. Show less
The Iminosugar AMP-DNM Improves Satiety and Activates Brown Adipose Tissue Through GLP1
Chao, D.H.M.; Wang, Y.N.; Foppen, E.; Ottenhoff, R.; Roomen, C. van; Parlevliet, E.T.; ... ; Yi, C.X. 2019
The Iminosugar AMP-DNM Improves Satiety and Activates Brown Adipose Tissue Through GLP1
Article / Letter to editor
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Obesity is taking on worldwide epidemic proportions, yet effective pharmacological agents with long-term efficacy remain unavailable. Previously, we designed the iminosugar N-adamantine... Show moreObesity is taking on worldwide epidemic proportions, yet effective pharmacological agents with long-term efficacy remain unavailable. Previously, we designed the iminosugar N-adamantine-methyloxypentyl-deoxynojirimycin (AMP-DNM), which potently improves glucose homeostasis by lowering excessive glycosphingolipids. Here we show that AMP-DNM promotes satiety and activates brown adipose tissue (BAT) in obese rodents. Moreover, we demonstrate that the mechanism mediating these favorable actions depends on oral, but not central, administration of AMP-DNM, which ultimately stimulates systemic glucagon-like peptide 1 (GLP1) secretion. We evidence an essential role of brain GLP1 receptors (GLP1r), as AMP-DNM fails to promote satiety and activate BAT in mice lacking the brain GLP1r as well as in mice treated intracerebroventricularly with GLP1r antagonist exendin-9. In conclusion, AMP-DNM markedly ameliorates metabolic abnormalities in obese rodents by restoring satiety and activating BAT through central GLP1r, while improving glucose homeostasis by mechanisms independent of central GLP1r. Show less
The iminosugar AMP-DNM improves satiety and activates brown adipose tissue through GLP1
Moro Chao, D.H.; Wang, Y.; Foppen, E.; Ottenhoff, R.; Roomen, C. van; Parlevliet, E.T.; ... ; Yi, C.X. 2019
The iminosugar AMP-DNM improves satiety and activates brown adipose tissue through GLP1
Article / Letter to editor
open access
Obesity is taking worldwide epidemic proportions, yet effective pharmacological agents with long-term efficacy remain unavailable. Previously, we designed the iminosugar AMP-DNM which potently... Show moreObesity is taking worldwide epidemic proportions, yet effective pharmacological agents with long-term efficacy remain unavailable. Previously, we designed the iminosugar AMP-DNM which potently improves glucose homeostasis by lowering excessive glycosphingolipids. Here we show that AMP-DNM promotes satiety and activates brown adipose tissue (BAT) in obese rodents. Moreover, we demonstrate that the mechanism mediating these favorable actions depends on oral, but not central, administration of AMP-DNM, which ultimately stimulates systemic glucagon-like peptide-1 (GLP1) secretion. We evidence an essential role of brain GLP1 receptors (GLP1r) as AMP-DNM fails to promote satiety and activate BAT in mice lacking the brain GLP1r as well as in mice treated intracerebroventricularly with GLP1r antagonist exendin-9. In conclusion, AMP-DNM markedly ameliorates metabolic abnormalities in obese rodents by restoring satiety and activating BAT through central GLP1r, while improving glucose homeostasis by mechanisms independent of central GLP1r. Show less
A specific activity-based probe to monitor family GH59 galactosylceramidase - the enzyme deficient in Krabbe disease
Marques, A.R.; Willems, L.I.; Herrera Moro, D.; Florea, B.I.; Scheij, S.; Ottenhof, R.; ... ; Aerts, J.M.F.G. 2017
A specific activity-based probe to monitor family GH59 galactosylceramidase - the enzyme deficient in Krabbe disease
Article / Letter to editor
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Elevation of glycoprotein nonmetastatic melanoma protein B in type 1 Gaucher disease patients and mouse models
Kramer, G.; Wegdam, W.; Donker-Koopman, W.; Ottenhoff, R.; Gaspar, P.; Verhoek, M.; ... ; Eijk, M.C. van 2016
Elevation of glycoprotein nonmetastatic melanoma protein B in type 1 Gaucher disease patients and mouse models
Article / Letter to editor
open access
Gaucher disease is caused by inherited deficiency of lysosomal glucocerebrosidase. Proteome analysis of laser-dissected splenic Gaucher cells revealed increased amounts of glycoprotein... Show moreGaucher disease is caused by inherited deficiency of lysosomal glucocerebrosidase. Proteome analysis of laser-dissected splenic Gaucher cells revealed increased amounts of glycoprotein nonmetastatic melanoma protein B (gpNMB). Plasma gpNMB was also elevated, correlating with chitotriosidase and CCL18, which are established markers for human Gaucher cells. In Gaucher mice, gpNMB is also produced by Gaucher cells. Correction of glucocerebrosidase deficiency in mice by gene transfer or pharmacological substrate reduction reverses gpNMB abnormalities. In conclusion, gpNMB acts as a marker for glucosylceramide-laden macrophages in man and mouse and gpNMB should be considered as candidate biomarker for Gaucher disease in treatment monitoring. Show less
Endo-β-Glucosidase Tag Allows Dual Detection of Fusion Proteins by Fluorescent Mechanism-Based Probes and Activity Measurement
Kallemeijn, W.W.; Scheij, S.; Voorn-Brouwer, T.M.; Witte, M.D.; Verhoek, M.; Overkleeft, H.S.; ... ; Aerts, J.M. 2016
Endo-β-Glucosidase Tag Allows Dual Detection of Fusion Proteins by Fluorescent Mechanism-Based Probes and Activity Measurement
Article / Letter to editor
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β-Glucoside-configured cyclophellitols are activity-based probes (ABPs) that allow sensitive detection of β-glucosidases. Their applicability to detect proteins fused with β-glucosidase was... Show moreβ-Glucoside-configured cyclophellitols are activity-based probes (ABPs) that allow sensitive detection of β-glucosidases. Their applicability to detect proteins fused with β-glucosidase was investigated in the cellular context. The tag was Rhodococcus sp. M-777 endoglycoceramidase II (EGCaseII), based on its lack of glycans and ability to hydrolyze fluorogenic 4-methylumbelliferyl β-d-lactoside (an activity absent in mammalian cells). Specific dual detection of fusion proteins was possible in vitro and in situ by using fluorescent ABPs and a fluorogenic substrate. Pre-blocking with conduritol β-epoxide (a poor inhibitor of EGCaseII) eliminated ABP labeling of endogenous β-glucosidases. ABPs equipped with biotin allowed convenient purification of the fusion proteins. Diversification of ABPs (distinct fluorophores, fluorogenic high-resolution detection moieties) should assist further research in living cells and organisms. Show less
Lysosomal glycosphingolipid catabolism by acid ceramidase: formation of glycosphingoid bases during deficiency of glycosidases
Guimaraes Da Lomba Ferraz, M.J.; Marques, A.R.; Appelman, M.D.; Verhoek, M.; Strijland, A.; Mirzaian, M.; ... ; Aerts, J.M.F.G. 2016
Lysosomal glycosphingolipid catabolism by acid ceramidase: formation of glycosphingoid bases during deficiency of glycosidases
Article / Letter to editor
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Glycosphingoid bases are elevated in inherited lysosomal storage disorders with deficient activity of glycosphingolipid catabolizing glycosidases. We investigated the molecular basis of the... Show moreGlycosphingoid bases are elevated in inherited lysosomal storage disorders with deficient activity of glycosphingolipid catabolizing glycosidases. We investigated the molecular basis of the formation of glucosylsphingosine and globotriaosylsphingosine during deficiency of glucocerebrosidase (Gaucher disease) and α-galactosidase A (Fabry disease). Independent genetic and pharmacological evidence is presented pointing to an active role of acid ceramidase in both processes through deacylation of lysosomal glycosphingolipids. The potential pathophysiological relevance of elevated glycosphingoid bases generated through this alternative metabolism in patients suffering from lysosomal glycosidase defects is discussed. Show less
Biochemical response to substrate reduction therapy versus enzyme replacement therapy in Gaucher disease type 1 patients
Smid, B.E.; Ferraz, M.J.; Verhoek, M.; Mirzaian, M.; Wisse, P.; Overkleeft, H.S.; ... ; Aerts, J.M. 2016
Biochemical response to substrate reduction therapy versus enzyme replacement therapy in Gaucher disease type 1 patients
Article / Letter to editor
open access
BACKGROUND We retrospectively compared biochemical responses in type 1 Gaucher disease patients to treatment with glycosphingolipid synthesis inhibitors miglustat and eliglustat and ERT. METHODS... Show moreBACKGROUND We retrospectively compared biochemical responses in type 1 Gaucher disease patients to treatment with glycosphingolipid synthesis inhibitors miglustat and eliglustat and ERT. METHODS Seventeen GD1 patients were included (n = 6 eliglustat, (two switched from ERT), n = 9 miglustat (seven switchers), n = 4 ERT (median dose 60U/kg/m). Plasma protein markers reflecting disease burden (chitotriosidase, CCL18) and lipids reflecting substrate accumulation (glucosylsphingosine, glucosylceramide) were determined. Also, liver and spleen volumes, hemoglobin, platelets, and fat fraction were measured. RESULTS In patients naïve to treatment, chitotriosidase, CCL18 and glucosylsphingosine decreased comparably upon eliglustat and ERT treatment, while the response to miglustat was less. After 2 years, median decrease of chitotriosidase was 89% (range 77-98), 88% (78-92) and 37% (29-46) for eliglustat, ERT and miglustat naïve patients respectively; decrease of CCL18 was 73% (63-78), 54% (43-86), and 10% (3-18); decrease of glucosylsphingosine was 86% (78-93), 78% (65-91), 48% (46-50). Plasma glucosylceramide in eliglustat treated patients (n = 4) reached values below the normal range (n = 20 healthy controls). Biochemical markers decreased or stabilized in switchers from ERT to eliglustat (n = 2), but less in miglustat switchers (n = 7). Clinical parameters responded comparably upon eliglustat and ERT treatment. CONCLUSIONS Our explorative study provides evidence that biochemical markers respond comparably in patients receiving eliglustat treatment and ERT, while the corresponding response to miglustat treatment is less. Show less
Increased YKL-40 and Chitotriosidase in Asthma and Chronic Obstructive Pulmonary Disease
James, A.J.; Reinius, L.E.; Verhoek, M.; Gomes, A.; Kupczyk, M.; Hammar, U.; ... ; Dahlen, S.-E. 2016
Increased YKL-40 and Chitotriosidase in Asthma and Chronic Obstructive Pulmonary Disease
Article / Letter to editor
open access
Glucosylated cholesterol in mammalian cells and tissues: formation and degradation by multiple cellular β-glucosidases
Marques, A.R.; Mirzaian, M.; Akiyama, H.; Wisse, P.; Ferraz, M.J.; Gaspar, P.; ... ; Aerts, J.M. 2016
Glucosylated cholesterol in mammalian cells and tissues: formation and degradation by multiple cellular β-glucosidases
Article / Letter to editor
open access
The membrane lipid glucosylceramide (GlcCer) is continuously formed and degraded. Cells express two GlcCer-degrading β-glucosidases, GBA and GBA2, located in and outside the lysosome, respectively... Show moreThe membrane lipid glucosylceramide (GlcCer) is continuously formed and degraded. Cells express two GlcCer-degrading β-glucosidases, GBA and GBA2, located in and outside the lysosome, respectively. Here we demonstrate that through transglucosylation both GBA and GBA2 are able to catalyze in vitro the transfer of glucosyl-moieties from GlcCer to cholesterol, and vice versa. Furthermore, the natural occurrence of 1-O-cholesteryl-β-D-glucopyranoside (GlcChol) in mouse tissues and human plasma is demonstrated using LC-MS/MS and 13C6-labelled GlcChol as internal standard. In cells the inhibition of GBA increases GlcChol, whereas inhibition of GBA2 decreases glucosylated sterol. Similarly, in GBA2-deficient mice GlcChol is reduced. Depletion of GlcCer by inhibition of GlcCer synthase decreases GlcChol in cells and likewise in plasma of inhibitor-treated Gaucher disease patients. In tissues of mice with Niemann-Pick type C, a condition characterized by intralysosomal accumulation of cholesterol, marked elevations in GlcChol occur as well. When lysosomal accumulation of cholesterol is induced in cultured cells, GlcChol is formed via lysosomal GBA. This illustrates that reversible transglucosylation reactions are highly dependent on local availability of suitable acceptors. In conclusion, mammalian tissues contain GlcChol formed by transglucosylation through β-glucosidases using GlcCer as donor. Our findings reveal a novel metabolic function for GlcCer. Show less
In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 alpha-L-fucosidases
Jiang, J.; Kallemeijn, W.W.; Wright, D.W.; Nieuwendijk, A.M.C.H. van den; Coco Rohde, V.; Folch, E.C.; ... ; Overkleeft, H.S. 2015
In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 alpha-L-fucosidases
Article / Letter to editor
open access
Mass spectrometric quantification of glucosylsphingosine in plasma and urine of type 1 Gaucher patients using an isotope standard
Mirzaian, M.; Wisse, P.; Ferraz, M.J.; Gold, H.; Donker-Koopman, W.E.; Verhoek, M.; ... ; Aerts, J.M.F.G. 2015
Mass spectrometric quantification of glucosylsphingosine in plasma and urine of type 1 Gaucher patients using an isotope standard
Article / Letter to editor
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Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2
Boot, R.G.; Verhoek, M.; Donker-Koopman, W.; Strijland, A.; Marle, J. van; Overkleeft, H.S.; ... ; Aerts, J.M.F.G. 2007
Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2
Article / Letter to editor
open access
Marked differences in tissue-specific expression of chitinases in mouse and man
Boot, R.G.; Bussink, A.P.; Verhoek, M.; Boer, P.A.J. de; Moorman, A.F.M.; Aerts, J.M.F.G. 2005
Marked differences in tissue-specific expression of chitinases in mouse and man
Article / Letter to editor
open access
The human chitotriosidase gene - Nature of inherited enzyme deficiency
Boot, R.G.; Renkema, G.H.; Verhoek, M.; Strijland, A.; Bliek, J.; Meulemeester, T.M.A.M.O. de; ... ; Aerts, J.M.F.G. 1998
The human chitotriosidase gene - Nature of inherited enzyme deficiency
Article / Letter to editor
open access
The human chitotriosidase gene - Nature of inherited enzyme deficiency
Boot, R.G.; Renkema, G.H.; Verhoek, M.; Strijland, A.; Bliek, J.; Meulemeester, T.M.A.M.O. de; ... ; Aerts, J.M.F.G. 1998
The human chitotriosidase gene - Nature of inherited enzyme deficiency
Article / Letter to editor
open access