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Article ; Online: Oxygenation of Anandamide by Lipoxygenases.

van Zadelhoff, Guus / van der Stelt, Mario

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2576, Page(s) 307–316

Abstract: The endocannabinoids anandamide and 2-arachidonoylglycerol are not only metabolized by serine hydrolases, such as fatty acid amide hydrolase, monoacylglycerol lipase, and α,β-hydrolases 6 and 12, but they also serve as substrates for cyclooxygenases, ... ...

Abstract	The endocannabinoids anandamide and 2-arachidonoylglycerol are not only metabolized by serine hydrolases, such as fatty acid amide hydrolase, monoacylglycerol lipase, and α,β-hydrolases 6 and 12, but they also serve as substrates for cyclooxygenases, cytochrome P450s, and lipoxygenases. These enzymes oxygenate the 1Z,4Z-pentadiene system of the arachidonic acid backbone of endocannabinoids, thereby giving rise to an entirely new array of bioactive lipids. Hereby, a protocol is provided for the enzymatic synthesis, purification, and characterization of various oxygenated metabolites of anandamide generated by lipoxygenases, which enables the biological study and detection of these metabolites.
MeSH term(s)	Alkadienes ; Arachidonic Acid ; Arachidonic Acids ; Cytochromes ; Endocannabinoids/metabolism ; Lipoxygenases ; Monoacylglycerol Lipases ; Polyunsaturated Alkamides ; Prostaglandin-Endoperoxide Synthases/metabolism ; Serine
Chemical Substances	Alkadienes ; Arachidonic Acids ; Cytochromes ; Endocannabinoids ; Polyunsaturated Alkamides ; Arachidonic Acid (27YG812J1I) ; Serine (452VLY9402) ; Lipoxygenases (EC 1.13.11.-) ; Prostaglandin-Endoperoxide Synthases (EC 1.14.99.1) ; Monoacylglycerol Lipases (EC 3.1.1.23) ; anandamide (UR5G69TJKH)
Language	English
Publishing date	2022-09-24
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2728-0_26
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Article ; Online: Oxygenation of Anandamide by Lipoxygenases.

van Zadelhoff, Guus / van der Stelt, Mario

Methods in molecular biology (Clifton, N.J.)

2016 Volume 1412, Page(s) 217–225

Abstract	The endocannabinoids anandamide and 2-arachidonoylglycerol are not only metabolized by serine hydrolases, such as fatty acid amide hydrolase, monoacylglycerol lipase, and α,β-hydrolases 6 and 12, but they also serve as substrates for cyclooxygenases and lipoxygenases. These enzymes oxygenate the 1Z,4Z-pentadiene system of the arachidonic acid backbone of endocannabinoids, thereby giving rise to an entirely new array of bioactive lipids. Hereby, a protocol is provided for the enzymatic synthesis, purification, and characterization of various oxygenated metabolites of anandamide generated by lipoxygenases, which enables the biological study and detection of these metabolites.
MeSH term(s)	Arachidonic Acids/metabolism ; Endocannabinoids/metabolism ; Gas Chromatography-Mass Spectrometry ; Glycerides/metabolism ; Lipoxygenases/metabolism ; Oxidation-Reduction ; Polyunsaturated Alkamides/metabolism ; Proton Magnetic Resonance Spectroscopy ; Glycine max/enzymology
Chemical Substances	Arachidonic Acids ; Endocannabinoids ; Glycerides ; Polyunsaturated Alkamides ; glyceryl 2-arachidonate (8D239QDW64) ; Lipoxygenases (EC 1.13.11.-) ; anandamide (UR5G69TJKH)
Language	English
Publishing date	2016-05-31
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-3539-0_22
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Article ; Online: Analysis of Disulfide Bond Formation.

Braakman, Ineke / Lamriben, Lydia / van Zadelhoff, Guus / Hebert, Daniel N

Current protocols in protein science

2017 Volume 90, Page(s) 14.1.1–14.1.21

Abstract: In this unit, protocols are provided for detection of disulfide bond formation in cultures of intact cells and in an in vitro translation system containing isolated microsomes or semi-permeabilized cells. First, the newly synthesized protein of interest ... ...

Abstract	In this unit, protocols are provided for detection of disulfide bond formation in cultures of intact cells and in an in vitro translation system containing isolated microsomes or semi-permeabilized cells. First, the newly synthesized protein of interest is biosynthetically labeled with radioactive amino acids in a short pulse. The labeled protein then is chased with unlabeled amino acids. At different times during the chase, a sample is collected, membranes are lysed with detergent, and the protein is isolated by immunoprecipitation, as described. A support protocol is provided for analysis of disulfide bonds in the immunoprecipitates by SDS-PAGE with and without prior reduction. The difference in mobility observed between the gels with nonreduced and reduced samples is due to disulfide bonds in the nonreduced protein. An additional support protocol is included that uses PEG-maleimide to modify free thiols and follow disulfide-bond formation by SDS-PAGE. © 2017 by John Wiley & Sons, Inc.
MeSH term(s)	Animals ; Cysteine/metabolism ; Disulfides/analysis ; Disulfides/metabolism ; Electrophoresis, Polyacrylamide Gel ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Ethylmaleimide/chemistry ; HEK293 Cells ; Humans ; Immunoprecipitation ; Methionine/metabolism ; Oxidation-Reduction ; Protein Biosynthesis ; Protein Folding ; Staining and Labeling ; Sulfur Radioisotopes
Chemical Substances	Disulfides ; Sulfur Radioisotopes ; Methionine (AE28F7PNPL) ; Cysteine (K848JZ4886) ; Ethylmaleimide (O3C74ACM9V)
Language	English
Publishing date	2017-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2179077-2
ISSN	1934-3663 ; 1934-3655
ISSN (online)	1934-3663
ISSN	1934-3655
DOI	10.1002/cpps.43
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Article: Analysis of protein folding, transport, and degradation in living cells by radioactive pulse chase

McCaul, Nicholas / Yeoh, Hui Ying / van Zadelhoff, Guus / Lodder, Naomi / Kleizen, Bertrand / Braakman, Ineke

Journal of visualized experiments. 2019 Feb. 12, , no. 144

2019

Abstract: Radioactive pulse-chase labeling is a powerful tool for studying the conformational maturation, the transport to their functional cellular location, and the degradation of target proteins in live cells. By using short (pulse) radiolabeling times (<30 min) ...

Abstract	Radioactive pulse-chase labeling is a powerful tool for studying the conformational maturation, the transport to their functional cellular location, and the degradation of target proteins in live cells. By using short (pulse) radiolabeling times (<30 min) and tightly controlled chase times, it is possible to label only a small fraction of the total protein pool and follow its folding. When combined with nonreducing/reducing SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoprecipitation with (conformation-specific) antibodies, folding processes can be examined in great detail. This system has been used to analyze the folding of proteins with a huge variation in properties such as soluble proteins, single and multi-pass transmembrane proteins, heavily N- and O-glycosylated proteins, and proteins with and without extensive disulfide bonding. Pulse-chase methods are the basis of kinetic studies into a range of additional features, including co- and posttranslational modifications, oligomerization, and polymerization, essentially allowing the analysis of a protein from birth to death. Pulse-chase studies on protein folding are complementary with other biochemical and biophysical methods for studying proteins in vitro by providing increased temporal resolution and physiological information. The methods as described within this paper are adapted easily to study the folding of almost any protein that can be expressed in mammalian or insect-cell systems.
Keywords	antibodies ; death ; mammals ; oligomerization ; polyacrylamide gel electrophoresis ; polymerization ; post-translational modification ; precipitin tests ; protein content ; protein folding ; radiolabeling ; transmembrane proteins
Language	English
Dates of publication	2019-0212
Size	p. e58952.
Publishing place	Journal of Visualized Experiments
Document type	Article
ISSN	1940-087X
DOI	10.3791/58952
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Article ; Online: Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase.

McCaul, Nicholas / Yeoh, Hui Ying / van Zadelhoff, Guus / Lodder, Naomi / Kleizen, Bertrand / Braakman, Ineke

Journal of visualized experiments : JoVE

2019 , Issue 144

Abstract	Radioactive pulse-chase labeling is a powerful tool for studying the conformational maturation, the transport to their functional cellular location, and the degradation of target proteins in live cells. By using short (pulse) radiolabeling times (<30 min) and tightly controlled chase times, it is possible to label only a small fraction of the total protein pool and follow its folding. When combined with nonreducing/reducing SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoprecipitation with (conformation-specific) antibodies, folding processes can be examined in great detail. This system has been used to analyze the folding of proteins with a huge variation in properties such as soluble proteins, single and multi-pass transmembrane proteins, heavily N- and O-glycosylated proteins, and proteins with and without extensive disulfide bonding. Pulse-chase methods are the basis of kinetic studies into a range of additional features, including co- and posttranslational modifications, oligomerization, and polymerization, essentially allowing the analysis of a protein from birth to death. Pulse-chase studies on protein folding are complementary with other biochemical and biophysical methods for studying proteins in vitro by providing increased temporal resolution and physiological information. The methods as described within this paper are adapted easily to study the folding of almost any protein that can be expressed in mammalian or insect-cell systems.
MeSH term(s)	Cell Movement ; Protein Folding ; Radioactive Pollutants/adverse effects ; Transfection
Chemical Substances	Radioactive Pollutants
Language	English
Publishing date	2019-02-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/58952
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Article ; Online: Intramolecular quality control: HIV-1 envelope gp160 signal-peptide cleavage as a functional folding checkpoint.

McCaul, Nicholas / Quandte, Matthias / Bontjer, Ilja / van Zadelhoff, Guus / Land, Aafke / Crooks, Ema T / Binley, James M / Sanders, Rogier W / Braakman, Ineke

Cell reports

2021 Volume 36, Issue 9, Page(s) 109646

Abstract: Removal of the membrane-tethering signal peptides that target secretory proteins to the endoplasmic reticulum is a prerequisite for proper folding. While generally thought to be removed co-translationally, we report two additional post-targeting ... ...

Abstract	Removal of the membrane-tethering signal peptides that target secretory proteins to the endoplasmic reticulum is a prerequisite for proper folding. While generally thought to be removed co-translationally, we report two additional post-targeting functions for the HIV-1 gp120 signal peptide, which remains attached until gp120 folding triggers its removal. First, the signal peptide improves folding fidelity by enhancing conformational plasticity of gp120 by driving disulfide isomerization through a redox-active cysteine. Simultaneously, the signal peptide delays folding by tethering the N terminus to the membrane, until assembly with the C terminus. Second, its carefully timed cleavage represents intramolecular quality control and ensures release of (only) natively folded gp120. Postponed cleavage and the redox-active cysteine are both highly conserved and important for viral fitness. Considering the ∼15% proteins with signal peptides and the frequency of N-to-C contacts in protein structures, these regulatory roles of signal peptides are bound to be more common in secretory-protein biogenesis.
MeSH term(s)	Cysteine ; HEK293 Cells ; HIV Envelope Protein gp120/genetics ; HIV Envelope Protein gp120/metabolism ; HIV Envelope Protein gp160/genetics ; HIV Envelope Protein gp160/metabolism ; HIV-1/genetics ; HIV-1/growth & development ; HIV-1/metabolism ; HeLa Cells ; Humans ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Processing, Post-Translational ; Protein Sorting Signals ; Protein Stability ; Structure-Activity Relationship ; Viral Load ; Virus Replication
Chemical Substances	HIV Envelope Protein gp120 ; HIV Envelope Protein gp160 ; Protein Sorting Signals ; gp120 protein, Human immunodeficiency virus 1 ; gp160 protein, Human immunodeficiency virus 1 ; Cysteine (K848JZ4886)
Language	English
Publishing date	2021-08-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.109646
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Article ; Online: Calcium as a crucial cofactor for low density lipoprotein receptor folding in the endoplasmic reticulum.

Pena, Florentina / Jansens, Annemieke / van Zadelhoff, Guus / Braakman, Ineke

The Journal of biological chemistry

2010 Volume 285, Issue 12, Page(s) 8656–8664

Abstract: The family of low density lipoprotein (LDL) receptors mediate uptake of a plethora of ligands from the circulation and couple this to signaling, thereby performing a crucial role in physiological processes including embryonic development, cancer ... ...

Abstract	The family of low density lipoprotein (LDL) receptors mediate uptake of a plethora of ligands from the circulation and couple this to signaling, thereby performing a crucial role in physiological processes including embryonic development, cancer development, homeostasis of lipoproteins, viral infection, and neuronal plasticity. Structural integrity of individual ectodomain modules in these receptors depends on calcium, and we showed before that the LDL receptor folds its modules late after synthesis via intermediates with abundant non-native disulfide bonds and structure. Using a radioactive pulse-chase approach, we here show that for proper LDL receptor folding, calcium had to be present from the very early start of folding, which suggests at least some native, essential coordination of calcium ions at the still largely non-native folding phase. As long as the protein was in the endoplasmic reticulum (ER), its folding was reversible, which changed only upon both proper incorporation of calcium and exit from the ER. Coevolution of protein folding with the high calcium concentration in the ER may be the basis for the need for this cation throughout the folding process even though calcium is only stably integrated in native repeats at a later stage.
MeSH term(s)	Calcium/metabolism ; Cations ; DNA/chemistry ; Disulfides/chemistry ; Dithiothreitol/chemistry ; Endoplasmic Reticulum/metabolism ; Epitopes/chemistry ; Glycosylation ; Golgi Apparatus/metabolism ; HeLa Cells ; Humans ; Immunoprecipitation ; Protein Folding ; Receptors, LDL/chemistry ; Time Factors
Chemical Substances	Cations ; Disulfides ; Epitopes ; Receptors, LDL ; DNA (9007-49-2) ; Calcium (SY7Q814VUP) ; Dithiothreitol (T8ID5YZU6Y)
Language	English
Publishing date	2010-01-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M110.105718
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Article: Calcium as a Crucial Cofactor for Low Density Lipoprotein Receptor Folding in the Endoplasmic Reticulum

Pena, Florentina / Jansens, Annemieke / van Zadelhoff, Guus / Braakman, Ineke

Journal of biological chemistry. 2010 Mar. 19, v. 285, no. 12

2010

Abstract	The family of low density lipoprotein (LDL) receptors mediate uptake of a plethora of ligands from the circulation and couple this to signaling, thereby performing a crucial role in physiological processes including embryonic development, cancer development, homeostasis of lipoproteins, viral infection, and neuronal plasticity. Structural integrity of individual ectodomain modules in these receptors depends on calcium, and we showed before that the LDL receptor folds its modules late after synthesis via intermediates with abundant non-native disulfide bonds and structure. Using a radioactive pulse-chase approach, we here show that for proper LDL receptor folding, calcium had to be present from the very early start of folding, which suggests at least some native, essential coordination of calcium ions at the still largely non-native folding phase. As long as the protein was in the endoplasmic reticulum (ER), its folding was reversible, which changed only upon both proper incorporation of calcium and exit from the ER. Coevolution of protein folding with the high calcium concentration in the ER may be the basis for the need for this cation throughout the folding process even though calcium is only stably integrated in native repeats at a later stage.
Language	English
Dates of publication	2010-0319
Size	p. 8656-8664.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article ; Online: TORC2 mediates the heat stress response in Drosophila by promoting the formation of stress granules.

Jevtov, Irena / Zacharogianni, Margarita / van Oorschot, Marinke M / van Zadelhoff, Guus / Aguilera-Gomez, Angelica / Vuillez, Igor / Braakman, Ineke / Hafen, Ernst / Stocker, Hugo / Rabouille, Catherine

Journal of cell science

2015 Volume 128, Issue 14, Page(s) 2497–2508

Abstract: The kinase TOR is found in two complexes, TORC1, which is involved in growth control, and TORC2, whose roles are less well defined. Here, we asked whether TORC2 has a role in sustaining cellular stress. We show that TORC2 inhibition in Drosophila ... ...

Abstract	The kinase TOR is found in two complexes, TORC1, which is involved in growth control, and TORC2, whose roles are less well defined. Here, we asked whether TORC2 has a role in sustaining cellular stress. We show that TORC2 inhibition in Drosophila melanogaster leads to a reduced tolerance to heat stress, whereas sensitivity to other stresses is not affected. Accordingly, we show that upon heat stress, both in the animal and Drosophila cultured S2 cells, TORC2 is activated and is required for maintaining the level of its known target, Akt1 (also known as PKB). We show that the phosphorylation of the stress-activated protein kinases is not modulated by TORC2 nor is the heat-induced upregulation of heat-shock proteins. Instead, we show, both in vivo and in cultured cells, that TORC2 is required for the assembly of heat-induced cytoprotective ribonucleoprotein particles, the pro-survival stress granules. These granules are formed in response to protein translation inhibition imposed by heat stress that appears to be less efficient in the absence of TORC2 function. We propose that TORC2 mediates heat resistance in Drosophila by promoting the cell autonomous formation of stress granules.
MeSH term(s)	Animals ; Cell Line ; Cytoplasmic Granules/genetics ; Cytoplasmic Granules/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Heat-Shock Response/physiology ; Mechanistic Target of Rapamycin Complex 2 ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Proto-Oncogene Proteins c-akt/genetics ; Proto-Oncogene Proteins c-akt/metabolism ; TOR Serine-Threonine Kinases/genetics ; TOR Serine-Threonine Kinases/metabolism
Chemical Substances	Drosophila Proteins ; Multiprotein Complexes ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Akt1 protein, Drosophila (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2015-07-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.168724
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Article ; Online: Methylation and acetylation of 15-hydroxyanandamide modulate its interaction with the endocannabinoid system.

Amadio, Daniele / Fezza, Filomena / Catanzaro, Giuseppina / Incani, Ottaviano / van Zadelhoff, Guus / Finazzi Agrò, Alessandro / Maccarrone, Mauro

Biochimie

2010 Volume 92, Issue 4, Page(s) 378–387

Abstract: The biological activity of endocannabinoids like anandamide (AEA) and 2-arachidonoylglycerol (2-AG) is subjected in vivo to a "metabolic control", exerted mainly by catabolic enzymes. AEA is inactivated by fatty acid amide hydrolase (FAAH), that is ... ...

Abstract	The biological activity of endocannabinoids like anandamide (AEA) and 2-arachidonoylglycerol (2-AG) is subjected in vivo to a "metabolic control", exerted mainly by catabolic enzymes. AEA is inactivated by fatty acid amide hydrolase (FAAH), that is inhibited competitively by hydroxyanandamides (HAEAs) generated from AEA by lipoxygenase activity. Among these derivatives, 15-HAEA has been shown to be an effective (K(i) approximately 0.6 muM) FAAH inhibitor, that blocks also type-1 cannabinoid receptor (CB1R) but not other components of the "endocannabinoid system (ECS)", like the AEA transporter (AMT) or CB2R. Here, we extended the study of the effect of 15-HAEA on the AEA synthetase (NAPE-PLD) and the AEA-binding vanilloid receptor (TRPV1), showing that 15-HAEA activates the former (up to approximately 140% of controls) and inhibits the latter protein (down to approximately 70%). We also show that 15-HAEA halves the synthesis of 2-AG and almost doubles the transport of this compound across the membrane. In addition, we synthesized methyl and acetyl derivatives of 15-HAEA (15-MeOAEA and 15-AcOAEA, respectively), in order to check their ability to modulate FAAH and the other ECS elements. In fact, methylation and acetylation are common biochemical reactions in the cellular environment. We show that 15-MeOAEA, unlike 15-AcOAEA, is still a powerful competitive inhibitor of FAAH (K(i) approximately 0.7 muM), and that both derivatives have negligible interactions with the other proteins of ECS. Therefore, 15-MeOAEA is a FAAH inhibitor more selective than 15-HAEA. Further molecular dynamics analysis gave clues to the molecular requirements for the interaction of 15-HAEA and 15-MeOAEA with FAAH.
MeSH term(s)	Acetylation ; Amidohydrolases/metabolism ; Animals ; Arachidonic Acids/metabolism ; Arachidonic Acids/pharmacology ; Cannabinoid Receptor Modulators/metabolism ; Endocannabinoids ; Kinetics ; Methylation ; Mice ; Phospholipase D/drug effects ; Phospholipase D/metabolism ; Polyunsaturated Alkamides/metabolism ; Polyunsaturated Alkamides/pharmacology ; Receptor, Cannabinoid, CB1/drug effects ; TRPV Cation Channels/metabolism
Chemical Substances	15-hydroxyanandamide ; Arachidonic Acids ; Cannabinoid Receptor Modulators ; Endocannabinoids ; Polyunsaturated Alkamides ; Receptor, Cannabinoid, CB1 ; TRPV Cation Channels ; TRPV1 protein, mouse ; N-acylphosphatidylethanolamine phospholipase D, mouse (EC 3.1.4.4) ; Phospholipase D (EC 3.1.4.4) ; Amidohydrolases (EC 3.5.-) ; fatty-acid amide hydrolase (EC 3.5.1.-)
Language	English
Publishing date	2010-04
Publishing country	France
Document type	Journal Article
ZDB-ID	120345-9
ISSN	1638-6183 ; 0300-9084
ISSN (online)	1638-6183
ISSN	0300-9084
DOI	10.1016/j.biochi.2010.01.001
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