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Book ; Thesis: Transport of lysosome-related organelles

Jordens, Ingrid

2005

Author's details	door Ingrid Jordens
Language	English
Size	157 S. : Ill., graph. Darst.
Publishing country	Germany
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Leiden, Univ., Diss., 2005
Note	Zsfassung in niederländ. Sprache
HBZ-ID	HT015143464
Database	Catalogue ZB MED Medicine, Health

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Article ; Online: RSPO3 Furin domain-conjugated liposomes for selective drug delivery to LGR5-high cells.

van Kerkhof, Peter / Kralj, Tomica / Spanevello, Francesca / van Bloois, Louis / Jordens, Ingrid / van der Vaart, Jelte / Jamieson, Cara / Merenda, Alessandra / Mastrobattista, Enrico / Maurice, Madelon M

Journal of controlled release : official journal of the Controlled Release Society

2023 Volume 356, Page(s) 72–83

Abstract: The transmembrane receptor LGR5 potentiates Wnt/β-catenin signaling by binding both secreted R-spondin (RSPOs) and the Wnt tumor suppressors RNF43/ZNRF3, directing clearance of RNF43/ZNRF3 from the cell surface. Besides being widely used as a stem cell ... ...

Abstract	The transmembrane receptor LGR5 potentiates Wnt/β-catenin signaling by binding both secreted R-spondin (RSPOs) and the Wnt tumor suppressors RNF43/ZNRF3, directing clearance of RNF43/ZNRF3 from the cell surface. Besides being widely used as a stem cell marker in various tissues, LGR5 is overexpressed in many types of malignancies, including colorectal cancer. Its expression characterizes a subpopulation of cancer cells that play a crucial role in tumor initiation, progression and cancer relapse, known as cancer stem cells (CSCs). For this reason, ongoing efforts are aimed at eradicating LGR5-positive CSCs. Here, we engineered liposomes decorated with different RSPO proteins to specifically detect and target LGR5-positive cells. Using fluorescence-loaded liposomes, we show that conjugation of full-length RSPO1 to the liposomal surface mediates aspecific, LGR5-independent cellular uptake, largely mediated by heparan sulfate proteoglycan binding. By contrast, liposomes decorated only with the Furin (FuFu) domains of RSPO3 are taken up by cells in a highly specific, LGR5-dependent manner. Moreover, encapsulating doxorubicin in FuFuRSPO3 liposomes allowed us to selectively inhibit the growth of LGR5-high cells. Thus, FuFuRSPO3-coated liposomes allow for the selective detection and ablation of LGR5-high cells, providing a potential drug delivery system for LGR5-targeted anti-cancer strategies.
MeSH term(s)	Liposomes ; Receptors, G-Protein-Coupled/metabolism ; Furin/metabolism ; Wnt Signaling Pathway ; Drug Delivery Systems ; Neoplastic Stem Cells/metabolism
Chemical Substances	Liposomes ; Receptors, G-Protein-Coupled ; Furin (EC 3.4.21.75)
Language	English
Publishing date	2023-03-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632533-6
ISSN	1873-4995 ; 0168-3659
ISSN (online)	1873-4995
ISSN	0168-3659
DOI	10.1016/j.jconrel.2023.02.025
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: RSPO3 Furin domain-conjugated liposomes for selective drug delivery to LGR5-high cells

Journal of Controlled Release. 2023 Apr., v. 356 p.72-83

2023

Abstract	The transmembrane receptor LGR5 potentiates Wnt/β-catenin signaling by binding both secreted R-spondin (RSPOs) and the Wnt tumor suppressors RNF43/ZNRF3, directing clearance of RNF43/ZNRF3 from the cell surface. Besides being widely used as a stem cell marker in various tissues, LGR5 is overexpressed in many types of malignancies, including colorectal cancer. Its expression characterizes a subpopulation of cancer cells that play a crucial role in tumor initiation, progression and cancer relapse, known as cancer stem cells (CSCs). For this reason, ongoing efforts are aimed at eradicating LGR5-positive CSCs. Here, we engineered liposomes decorated with different RSPO proteins to specifically detect and target LGR5-positive cells. Using fluorescence-loaded liposomes, we show that conjugation of full-length RSPO1 to the liposomal surface mediates aspecific, LGR5-independent cellular uptake, largely mediated by heparan sulfate proteoglycan binding. By contrast, liposomes decorated only with the Furin (FuFu) domains of RSPO3 are taken up by cells in a highly specific, LGR5-dependent manner. Moreover, encapsulating doxorubicin in FuFuRSPO3 liposomes allowed us to selectively inhibit the growth of LGR5-high cells. Thus, FuFuRSPO3-coated liposomes allow for the selective detection and ablation of LGR5-high cells, providing a potential drug delivery system for LGR5-targeted anti-cancer strategies.
Keywords	colorectal neoplasms ; doxorubicin ; drug delivery systems ; heparan sulfate ; proteoglycans ; relapse ; stem cells ; R-spondin-3 ; LGR5 ; Liposomes ; Drug delivery ; Cancer stem cells ; RSPO ; CSC ; LGR ; Fu
Language	English
Dates of publication	2023-04
Size	p. 72-83.
Publishing place	Elsevier B.V.
Document type	Article ; Online
ZDB-ID	632533-6
ISSN	1873-4995 ; 0168-3659
ISSN (online)	1873-4995
ISSN	0168-3659
DOI	10.1016/j.jconrel.2023.02.025
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Intestinal Paneth cell differentiation relies on asymmetric regulation of Wnt signaling by Daam1/2.

Colozza, Gabriele / Lee, Heetak / Merenda, Alessandra / Wu, Szu-Hsien Sam / Català-Bordes, Andrea / Radaszkiewicz, Tomasz W / Jordens, Ingrid / Lee, Ji-Hyun / Bamford, Aileen-Diane / Farnhammer, Fiona / Low, Teck Yew / Maurice, Madelon M / Bryja, Vítězslav / Kim, Jihoon / Koo, Bon-Kyoung

Science advances

2023 Volume 9, Issue 47, Page(s) eadh9673

Abstract: The mammalian intestine is one of the most rapidly self-renewing tissues, driven by stem cells residing at the crypt bottom. Paneth cells form a major element of the niche microenvironment providing various growth factors to orchestrate intestinal stem ... ...

Abstract	The mammalian intestine is one of the most rapidly self-renewing tissues, driven by stem cells residing at the crypt bottom. Paneth cells form a major element of the niche microenvironment providing various growth factors to orchestrate intestinal stem cell homeostasis, such as Wnt3. Different Wnt ligands can selectively activate β-catenin-dependent (canonical) or -independent (noncanonical) signaling. Here, we report that the Dishevelled-associated activator of morphogenesis 1 (Daam1) and its paralogue Daam2 asymmetrically regulate canonical and noncanonical Wnt (Wnt/PCP) signaling. Daam1/2 interacts with the Wnt inhibitor RNF43, and Daam1/2 double knockout stimulates canonical Wnt signaling by preventing RNF43-dependent degradation of the Wnt receptor, Frizzled (Fzd). Single-cell RNA sequencing analysis revealed that Paneth cell differentiation is impaired by Daam1/2 depletion because of defective Wnt/PCP signaling. Together, we identified Daam1/2 as an unexpected hub molecule coordinating both canonical and noncanonical Wnt, which is fundamental for specifying an adequate number of Paneth cells.
MeSH term(s)	Animals ; Wnt Signaling Pathway ; Paneth Cells ; Intestines ; Cell Differentiation ; Stem Cells/metabolism ; Mammals
Language	English
Publishing date	2023-11-24
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.adh9673
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Article ; Online: Wnt Signaling Directs Neuronal Polarity and Axonal Growth.

Stanganello, Eliana / Zahavi, Eitan Erez / Burute, Mithila / Smits, Jasper / Jordens, Ingrid / Maurice, Madelon M / Kapitein, Lukas C / Hoogenraad, Casper C

iScience

2019 Volume 13, Page(s) 318–327

Abstract: The establishment of neuronal polarity is driven by cytoskeletal remodeling that stabilizes and promotes the growth of a single axon from one of the multiple neurites. The importance of the local microtubule stabilization in this process has been ... ...

Abstract	The establishment of neuronal polarity is driven by cytoskeletal remodeling that stabilizes and promotes the growth of a single axon from one of the multiple neurites. The importance of the local microtubule stabilization in this process has been revealed however, the external signals initiating the cytoskeletal rearrangements are not completely understood. In this study, we show that local activation of the canonical Wnt pathway regulates neuronal polarity and axonal outgrowth. We found that in the early stages of neuronal polarization, Wnt3a accumulates in one of the neurites of unpolarized cells and thereby could determine axon positioning. Subsequently, Wnt3a localizes to the growing axon, where it activates the canonical Wnt pathway and controls axon positioning and axonal length. We propose a model in which Wnt3a regulates the formation and growth of the axon by activating local intracellular signaling events leading to microtubule remodeling.
Language	English
Publishing date	2019-03-02
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2019.02.029
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Book ; Online: Topkeurmerken voor duurzame voeding

Aaldijk, Ingrid / Snoek, Jonna / Jordens, Wicher

resultaten ordening keurmerken en logo's 2016

2016

Abstract: Doel van de ordening is: verwarring door de groei van keurmerken/logo’s terugdringen zodat keurmerken/logo’s hun oorspronkelijke functie terugkrijgen: 1. Een betrouwbaar hulpmiddel voor consumenten om een duurzame keuze te maken; 2. Laten zien dat de ... ...

Abstract	Doel van de ordening is: verwarring door de groei van keurmerken/logo’s terugdringen zodat keurmerken/logo’s hun oorspronkelijke functie terugkrijgen: 1. Een betrouwbaar hulpmiddel voor consumenten om een duurzame keuze te maken; 2. Laten zien dat de desbetreffende organisatie of het bedrijf inspanningen verricht op het gebied van duurzaamheid.
Keywords	"Organics" in general
Publisher	Milieu Centraal
Publishing country	dk
Document type	Book ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Wnt Signaling Directs Neuronal Polarity and Axonal Growth

Eliana Stanganello / Eitan Erez Zahavi / Mithila Burute / Jasper Smits / Ingrid Jordens / Madelon M. Maurice / Lukas C. Kapitein / Casper C. Hoogenraad

iScience, Vol 13, Iss , Pp 318-

2019 Volume 327

Abstract: Summary: The establishment of neuronal polarity is driven by cytoskeletal remodeling that stabilizes and promotes the growth of a single axon from one of the multiple neurites. The importance of the local microtubule stabilization in this process has ... ...

Abstract	Summary: The establishment of neuronal polarity is driven by cytoskeletal remodeling that stabilizes and promotes the growth of a single axon from one of the multiple neurites. The importance of the local microtubule stabilization in this process has been revealed however, the external signals initiating the cytoskeletal rearrangements are not completely understood. In this study, we show that local activation of the canonical Wnt pathway regulates neuronal polarity and axonal outgrowth. We found that in the early stages of neuronal polarization, Wnt3a accumulates in one of the neurites of unpolarized cells and thereby could determine axon positioning. Subsequently, Wnt3a localizes to the growing axon, where it activates the canonical Wnt pathway and controls axon positioning and axonal length. We propose a model in which Wnt3a regulates the formation and growth of the axon by activating local intracellular signaling events leading to microtubule remodeling. : Neuroscience; Molecular Neuroscience; Cellular Neuroscience Subject Areas: Neuroscience, Molecular Neuroscience, Cellular Neuroscience
Keywords	Science ; Q
Language	English
Publishing date	2019-03-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: R-spondins engage heparan sulfate proteoglycans to potentiate WNT signaling.

Dubey, Ramin / van Kerkhof, Peter / Jordens, Ingrid / Malinauskas, Tomas / Pusapati, Ganesh V / McKenna, Joseph K / Li, Dan / Carette, Jan E / Ho, Mitchell / Siebold, Christian / Maurice, Madelon / Lebensohn, Andres M / Rohatgi, Rajat

eLife

2020 Volume 9

Abstract: R-spondins (RSPOs) amplify WNT signaling during development and regenerative responses. We previously demonstrated that RSPOs 2 and 3 potentiate WNT/β-catenin signaling in cells lacking leucine-rich repeat-containing G-protein coupled receptors (LGRs) 4, ...

Abstract	R-spondins (RSPOs) amplify WNT signaling during development and regenerative responses. We previously demonstrated that RSPOs 2 and 3 potentiate WNT/β-catenin signaling in cells lacking leucine-rich repeat-containing G-protein coupled receptors (LGRs) 4, 5 and 6 (Lebensohn and Rohatgi, 2018). We now show that heparan sulfate proteoglycans (HSPGs) act as alternative co-receptors for RSPO3 using a combination of ligand mutagenesis and ligand engineering. Mutations in RSPO3 residues predicted to contact HSPGs impair its signaling capacity. Conversely, the HSPG-binding domains of RSPO3 can be entirely replaced with an antibody that recognizes heparan sulfate (HS) chains attached to multiple HSPGs without diminishing WNT-potentiating activity in cultured cells and intestinal organoids. A genome-wide screen for mediators of RSPO3 signaling in cells lacking LGRs 4, 5 and 6 failed to reveal other receptors. We conclude that HSPGs are RSPO co-receptors that potentiate WNT signaling in the presence and absence of LGRs.
MeSH term(s)	Cells, Cultured ; Developmental Biology ; Heparan Sulfate Proteoglycans/genetics ; Heparan Sulfate Proteoglycans/metabolism ; Humans ; Intercellular Signaling Peptides and Proteins/genetics ; Intercellular Signaling Peptides and Proteins/metabolism ; Ligands ; Organoids ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism ; Thrombospondins ; Wnt Signaling Pathway
Chemical Substances	Heparan Sulfate Proteoglycans ; Intercellular Signaling Peptides and Proteins ; Ligands ; RSPO3 protein, human ; Receptors, G-Protein-Coupled ; Rspo2 protein, human ; Thrombospondins
Language	English
Publishing date	2020-05-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.54469
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: R-spondins engage heparan sulfate proteoglycans to potentiate WNT signaling

Ramin Dubey / Peter van Kerkhof / Ingrid Jordens / Tomas Malinauskas / Ganesh V Pusapati / Joseph K McKenna / Dan Li / Jan E Carette / Mitchell Ho / Christian Siebold / Madelon Maurice / Andres M Lebensohn / Rajat Rohatgi

eLife, Vol

2020 Volume 9

Abstract	R-spondins (RSPOs) amplify WNT signaling during development and regenerative responses. We previously demonstrated that RSPOs 2 and 3 potentiate WNT/β-catenin signaling in cells lacking leucine-rich repeat-containing G-protein coupled receptors (LGRs) 4, 5 and 6 (Lebensohn and Rohatgi, 2018). We now show that heparan sulfate proteoglycans (HSPGs) act as alternative co-receptors for RSPO3 using a combination of ligand mutagenesis and ligand engineering. Mutations in RSPO3 residues predicted to contact HSPGs impair its signaling capacity. Conversely, the HSPG-binding domains of RSPO3 can be entirely replaced with an antibody that recognizes heparan sulfate (HS) chains attached to multiple HSPGs without diminishing WNT-potentiating activity in cultured cells and intestinal organoids. A genome-wide screen for mediators of RSPO3 signaling in cells lacking LGRs 4, 5 and 6 failed to reveal other receptors. We conclude that HSPGs are RSPO co-receptors that potentiate WNT signaling in the presence and absence of LGRs.
Keywords	R-spondin ; heparan sulfate proteoglycans ; WNT ; LGR ; development ; single chain antibody ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2020-05-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Anti-LRP5/6 VHHs promote differentiation of Wnt-hypersensitive intestinal stem cells.

Fenderico, Nicola / van Scherpenzeel, Revina C / Goldflam, Michael / Proverbio, Davide / Jordens, Ingrid / Kralj, Tomica / Stryeck, Sarah / Bass, Tarek Z / Hermans, Guy / Ullman, Christopher / Aastrup, Teodor / Gros, Piet / Maurice, Madelon M

Nature communications

2019 Volume 10, Issue 1, Page(s) 365

Abstract: Wnt-induced β-catenin-mediated transcription is a driving force for stem cell self-renewal during adult tissue homeostasis. Enhanced Wnt receptor expression due to mutational inactivation of the ubiquitin ligases RNF43/ZNRF3 recently emerged as a leading ...

Abstract	Wnt-induced β-catenin-mediated transcription is a driving force for stem cell self-renewal during adult tissue homeostasis. Enhanced Wnt receptor expression due to mutational inactivation of the ubiquitin ligases RNF43/ZNRF3 recently emerged as a leading cause for cancer development. Consequently, targeting canonical Wnt receptors such as LRP5/6 holds great promise for treatment of such cancer subsets. Here, we employ CIS display technology to identify single-domain antibody fragments (VHH) that bind the LRP6 P3E3P4E4 region with nanomolar affinity and strongly inhibit Wnt3/3a-induced β-catenin-mediated transcription in cells, while leaving Wnt1 responses unaffected. Structural analysis reveal that individual VHHs variably employ divergent antigen-binding regions to bind a similar surface in the third β-propeller of LRP5/6, sterically interfering with Wnt3/3a binding. Importantly, anti-LRP5/6 VHHs block the growth of Wnt-hypersensitive Rnf43/Znrf3-mutant intestinal organoids through stem cell exhaustion and collective terminal differentiation. Thus, VHH-mediated targeting of LRP5/6 provides a promising differentiation-inducing strategy for treatment of Wnt-hypersensitive tumors.
MeSH term(s)	Animals ; Binding Sites ; Cell Differentiation ; Cell Line, Tumor ; Cell Proliferation ; Crystallography, X-Ray ; Fibroblasts/cytology ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Gene Expression Regulation ; HEK293 Cells ; Humans ; Intestine, Small/cytology ; Intestine, Small/drug effects ; Intestine, Small/metabolism ; Low Density Lipoprotein Receptor-Related Protein-5/antagonists & inhibitors ; Low Density Lipoprotein Receptor-Related Protein-5/chemistry ; Low Density Lipoprotein Receptor-Related Protein-5/genetics ; Low Density Lipoprotein Receptor-Related Protein-5/metabolism ; Low Density Lipoprotein Receptor-Related Protein-6/antagonists & inhibitors ; Low Density Lipoprotein Receptor-Related Protein-6/chemistry ; Low Density Lipoprotein Receptor-Related Protein-6/genetics ; Low Density Lipoprotein Receptor-Related Protein-6/metabolism ; Mice ; Models, Molecular ; Organoids/cytology ; Organoids/drug effects ; Organoids/metabolism ; Protein Binding ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Single-Domain Antibodies/chemistry ; Single-Domain Antibodies/genetics ; Single-Domain Antibodies/metabolism ; Stem Cells/cytology ; Stem Cells/drug effects ; Stem Cells/metabolism ; Transcription, Genetic ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Wnt3A Protein/genetics ; Wnt3A Protein/metabolism ; beta Catenin/genetics ; beta Catenin/metabolism
Chemical Substances	CTNNB1 protein, mouse ; Low Density Lipoprotein Receptor-Related Protein-5 ; Low Density Lipoprotein Receptor-Related Protein-6 ; Lrp5 protein, mouse ; Lrp6 protein, mouse ; Single-Domain Antibodies ; Wnt3A Protein ; Wnt3a protein, mouse ; beta Catenin ; RNF43 protein, mouse (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2019-01-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-018-08172-z
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