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  1. Article: Ca

    Enrich, Carlos / Lu, Albert / Tebar, Francesc / Rentero, Carles / Grewal, Thomas

    Advances in experimental medicine and biology

    2023  Volume 1422, Page(s) 393–438

    Abstract: Maintaining lipid composition diversity in membranes from different organelles is critical for numerous cellular processes. However, many lipids are synthesized in the endoplasmic reticulum (ER) and require delivery to other organelles. In this scenario, ...

    Abstract Maintaining lipid composition diversity in membranes from different organelles is critical for numerous cellular processes. However, many lipids are synthesized in the endoplasmic reticulum (ER) and require delivery to other organelles. In this scenario, formation of membrane contact sites (MCS) between neighbouring organelles has emerged as a novel non-vesicular lipid transport mechanism. Dissecting the molecular composition of MCS identified phosphoinositides (PIs), cholesterol, scaffolding/tethering proteins as well as Ca
    MeSH term(s) Phosphatidylinositols/metabolism ; Annexins/metabolism ; Cell Membrane/metabolism ; Endoplasmic Reticulum/metabolism ; Carrier Proteins/metabolism ; Cholesterol/metabolism
    Chemical Substances Phosphatidylinositols ; Annexins ; Carrier Proteins ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2023-03-29
    Publishing country United States
    Document type Journal Article
    ISSN 2214-8019 ; 0065-2598
    ISSN (online) 2214-8019
    ISSN 0065-2598
    DOI 10.1007/978-3-031-21547-6_15
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Annexins Bridging the Gap: Novel Roles in Membrane Contact Site Formation.

    Enrich, Carlos / Lu, Albert / Tebar, Francesc / Rentero, Carles / Grewal, Thomas

    Frontiers in cell and developmental biology

    2022  Volume 9, Page(s) 797949

    Abstract: Membrane contact sites (MCS) are specialized small areas of close apposition between two different organelles that have led researchers to reconsider the dogma of intercellular ... ...

    Abstract Membrane contact sites (MCS) are specialized small areas of close apposition between two different organelles that have led researchers to reconsider the dogma of intercellular communication
    Language English
    Publishing date 2022-01-06
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2021.797949
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Annexins in Adipose Tissue: Novel Players in Obesity.

    Grewal, Thomas / Enrich, Carlos / Rentero, Carles / Buechler, Christa

    International journal of molecular sciences

    2019  Volume 20, Issue 14

    Abstract: Obesity and the associated comorbidities are a growing health threat worldwide. Adipose tissue dysfunction, impaired adipokine activity, and inflammation are central to metabolic diseases related to obesity. In particular, the excess storage of lipids in ...

    Abstract Obesity and the associated comorbidities are a growing health threat worldwide. Adipose tissue dysfunction, impaired adipokine activity, and inflammation are central to metabolic diseases related to obesity. In particular, the excess storage of lipids in adipose tissues disturbs cellular homeostasis. Amongst others, organelle function and cell signaling, often related to the altered composition of specialized membrane microdomains (lipid rafts), are affected. Within this context, the conserved family of annexins are well known to associate with membranes in a calcium (Ca
    MeSH term(s) Adipocytes/metabolism ; Adipose Tissue/metabolism ; Animals ; Annexins/genetics ; Annexins/metabolism ; Biomarkers ; Disease Susceptibility ; Gene Expression Regulation ; Glucose/metabolism ; Humans ; Insulin/metabolism ; Lipid Metabolism ; Obesity/etiology ; Obesity/metabolism
    Chemical Substances Annexins ; Biomarkers ; Insulin ; Glucose (IY9XDZ35W2)
    Language English
    Publishing date 2019-07-13
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms20143449
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  4. Article ; Online: Annexin Animal Models-From Fundamental Principles to Translational Research.

    Grewal, Thomas / Rentero, Carles / Enrich, Carlos / Wahba, Mohamed / Raabe, Carsten A / Rescher, Ursula

    International journal of molecular sciences

    2021  Volume 22, Issue 7

    Abstract: Routine manipulation of the mouse genome has become a landmark in biomedical research. Traits that are only associated with advanced developmental stages can now be investigated within a living organism, and the in vivo analysis of corresponding ... ...

    Abstract Routine manipulation of the mouse genome has become a landmark in biomedical research. Traits that are only associated with advanced developmental stages can now be investigated within a living organism, and the in vivo analysis of corresponding phenotypes and functions advances the translation into the clinical setting. The annexins, a family of closely related calcium (Ca
    MeSH term(s) Animals ; Annexin A1/metabolism ; Annexin A2/metabolism ; Annexin A5/metabolism ; Anti-Inflammatory Agents/metabolism ; Anti-Inflammatory Agents/pharmacology ; Calcium/chemistry ; Cell Membrane/metabolism ; Diabetes Mellitus/metabolism ; Disease Progression ; Homeostasis ; Lipids/chemistry ; Mice ; Mice, Knockout ; Nanotechnology ; Neoplasms/metabolism ; Neovascularization, Pathologic ; Peptides/chemistry ; Phenotype ; Protein Binding ; Protein Transport ; Translational Medical Research
    Chemical Substances Annexin A1 ; Annexin A2 ; Annexin A5 ; Anti-Inflammatory Agents ; Anxa2 protein, mouse ; Anxa5 protein, mouse ; Lipids ; Peptides ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2021-03-26
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22073439
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  5. Article: GTPases Rac1 and Ras Signaling from Endosomes.

    Tebar, Francesc / Enrich, Carlos / Rentero, Carles / Grewal, Thomas

    Progress in molecular and subcellular biology

    2018  Volume 57, Page(s) 65–105

    Abstract: The endocytic compartment is not only the functional continuity of the plasma membrane but consists of a diverse collection of intracellular heterogeneous complex structures that transport, amplify, sustain, and/or sort signaling molecules. Over the ... ...

    Abstract The endocytic compartment is not only the functional continuity of the plasma membrane but consists of a diverse collection of intracellular heterogeneous complex structures that transport, amplify, sustain, and/or sort signaling molecules. Over the years, it has become evident that early, late, and recycling endosomes represent an interconnected vesicular-tubular network able to form signaling platforms that dynamically and efficiently translate extracellular signals into biological outcome. Cell activation, differentiation, migration, death, and survival are some of the endpoints of endosomal signaling. Hence, to understand the role of the endosomal system in signal transduction in space and time, it is therefore necessary to dissect and identify the plethora of decoders that are operational in the different steps along the endocytic pathway. In this chapter, we focus on the regulation of spatiotemporal signaling in cells, considering endosomes as central platforms, in which several small GTPases proteins of the Ras superfamily, in particular Ras and Rac1, actively participate to control cellular processes like proliferation and cell mobility.
    MeSH term(s) Cell Movement/genetics ; Cell Proliferation/genetics ; Endocytosis/genetics ; Endosomes/genetics ; Humans ; Protein Transport ; Signal Transduction/genetics ; rac1 GTP-Binding Protein/genetics ; ras Proteins/genetics
    Chemical Substances rac1 GTP-Binding Protein (EC 3.6.5.2) ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2018-08-10
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 0079-6484
    ISSN 0079-6484
    DOI 10.1007/978-3-319-96704-2_3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Linking Late Endosomal Cholesterol with Cancer Progression and Anticancer Drug Resistance.

    Nguyen, Mai K L / Jose, Jaimy / Wahba, Mohamed / Bernaus-Esqué, Marc / Hoy, Andrew J / Enrich, Carlos / Rentero, Carles / Grewal, Thomas

    International journal of molecular sciences

    2022  Volume 23, Issue 13

    Abstract: Cancer cells undergo drastic metabolic adaptions to cover increased bioenergetic needs, contributing to resistance to therapies. This includes a higher demand for cholesterol, which often coincides with elevated cholesterol uptake from low-density ... ...

    Abstract Cancer cells undergo drastic metabolic adaptions to cover increased bioenergetic needs, contributing to resistance to therapies. This includes a higher demand for cholesterol, which often coincides with elevated cholesterol uptake from low-density lipoproteins (LDL) and overexpression of the LDL receptor in many cancers. This implies the need for cancer cells to accommodate an increased delivery of LDL along the endocytic pathway to late endosomes/lysosomes (LE/Lys), providing a rapid and effective distribution of LDL-derived cholesterol from LE/Lys to other organelles for cholesterol to foster cancer growth and spread. LDL-cholesterol exported from LE/Lys is facilitated by Niemann-Pick Type C1/2 (NPC1/2) proteins, members of the steroidogenic acute regulatory-related lipid transfer domain (StARD) and oxysterol-binding protein (OSBP) families. In addition, lysosomal membrane proteins, small Rab GTPases as well as scaffolding proteins, including annexin A6 (AnxA6), contribute to regulating cholesterol egress from LE/Lys. Here, we summarize current knowledge that links upregulated activity and expression of cholesterol transporters and related proteins in LE/Lys with cancer growth, progression and treatment outcomes. Several mechanisms on how cellular distribution of LDL-derived cholesterol from LE/Lys influences cancer cell behavior are reviewed, some of those providing opportunities for treatment strategies to reduce cancer progression and anticancer drug resistance.
    MeSH term(s) Antineoplastic Agents/analysis ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Cholesterol/metabolism ; Cholesterol, LDL/metabolism ; Endosomes/metabolism ; Humans ; Lysosomes/metabolism ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Niemann-Pick C1 Protein/metabolism ; rab GTP-Binding Proteins/metabolism
    Chemical Substances Antineoplastic Agents ; Cholesterol, LDL ; Niemann-Pick C1 Protein ; Cholesterol (97C5T2UQ7J) ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2022-06-29
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms23137206
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  7. Article ; Online: Pleiotropic Roles of Calmodulin in the Regulation of KRas and Rac1 GTPases: Functional Diversity in Health and Disease.

    Tebar, Francesc / Chavero, Albert / Agell, Neus / Lu, Albert / Rentero, Carles / Enrich, Carlos / Grewal, Thomas

    International journal of molecular sciences

    2020  Volume 21, Issue 10

    Abstract: Calmodulin is a ubiquitous signalling protein that controls many biological processes due to its capacity to interact and/or regulate a large number of cellular proteins and pathways, mostly in a ... ...

    Abstract Calmodulin is a ubiquitous signalling protein that controls many biological processes due to its capacity to interact and/or regulate a large number of cellular proteins and pathways, mostly in a Ca
    MeSH term(s) Animals ; Calmodulin/genetics ; Calmodulin/metabolism ; Carcinogenesis/genetics ; Carcinogenesis/metabolism ; Genetic Pleiotropy ; Humans ; Proto-Oncogene Proteins p21(ras)/genetics ; Proto-Oncogene Proteins p21(ras)/metabolism ; Signal Transduction ; rac1 GTP-Binding Protein/genetics ; rac1 GTP-Binding Protein/metabolism
    Chemical Substances Calmodulin ; KRAS protein, human ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2) ; rac1 GTP-Binding Protein (EC 3.6.5.2)
    Language English
    Publishing date 2020-05-23
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21103680
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  8. Article: Annexin A6 in the liver: From the endocytic compartment to cellular physiology.

    Enrich, Carlos / Rentero, Carles / Grewal, Thomas

    Biochimica et biophysica acta. Molecular cell research

    2016  Volume 1864, Issue 6, Page(s) 933–946

    Abstract: Annexin A6 (AnxA6) belongs to the conserved annexin family - a group of ... ...

    Abstract Annexin A6 (AnxA6) belongs to the conserved annexin family - a group of Ca
    MeSH term(s) Animals ; Annexin A6/metabolism ; Cell Compartmentation ; Cell Line ; Cell Line, Tumor ; Endocytosis ; Humans ; Liver/metabolism
    Chemical Substances Annexin A6
    Language English
    Publishing date 2016-10-27
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2016.10.017
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
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  9. Article ; Online: Cholesterol Overload: Contact Sites to the Rescue!

    Enrich, Carlos / Rentero, Carles / Grewal, Thomas / Futter, Clare E / Eden, Emily R

    Contact (Thousand Oaks (Ventura County, Calif.))

    2019  Volume 2, Page(s) 2515256419893507

    Abstract: Delivery of low-density lipoprotein-derived cholesterol to the endoplasmic reticulum (ER) is essential for cholesterol homeostasis, yet the mechanism of this transport has largely remained elusive. Two recent reports shed some light on this process, ... ...

    Abstract Delivery of low-density lipoprotein-derived cholesterol to the endoplasmic reticulum (ER) is essential for cholesterol homeostasis, yet the mechanism of this transport has largely remained elusive. Two recent reports shed some light on this process, uncovering a role for Niemann Pick type-C1 protein (NPC1) in the formation of membrane contact sites (MCS) between late endosomes (LE)/lysosomes (Lys) and the ER. Both studies identified a loss of MCS in cells lacking functional NPC1, where cholesterol accumulates in late endocytic organelles. Remarkably, and taking different approaches, both studies have made a striking observation that expansion of LE/Lys-ER MCS can rescue the cholesterol accumulation phenotype in NPC1 mutant or deficient cells. In both cases, the cholesterol was shown to be transported to the ER, demonstrating the importance of ER-LE/Lys contact sites in the direct transport of low-density lipoprotein-derived cholesterol to the ER.
    Language English
    Publishing date 2019-12-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2964312-0
    ISSN 2515-2564 ; 2515-2564
    ISSN (online) 2515-2564
    ISSN 2515-2564
    DOI 10.1177/2515256419893507
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  10. Article ; Online: Role of cholesterol in SNARE-mediated trafficking on intracellular membranes.

    Enrich, Carlos / Rentero, Carles / Hierro, Aitor / Grewal, Thomas

    Journal of cell science

    2015  Volume 128, Issue 6, Page(s) 1071–1081

    Abstract: The cell surface delivery of extracellular matrix (ECM) and integrins is fundamental for cell migration in wound healing and during cancer cell metastasis. This process is not only driven by several soluble NSF attachment protein (SNAP) receptor (SNARE) ... ...

    Abstract The cell surface delivery of extracellular matrix (ECM) and integrins is fundamental for cell migration in wound healing and during cancer cell metastasis. This process is not only driven by several soluble NSF attachment protein (SNAP) receptor (SNARE) proteins, which are key players in vesicle transport at the cell surface and intracellular compartments, but is also tightly modulated by cholesterol. Cholesterol-sensitive SNAREs at the cell surface are relatively well characterized, but it is less well understood how altered cholesterol levels in intracellular compartments impact on SNARE localization and function. Recent insights from structural biology, protein chemistry and cell microscopy have suggested that a subset of the SNAREs engaged in exocytic and retrograde pathways dynamically 'sense' cholesterol levels in the Golgi and endosomal membranes. Hence, the transport routes that modulate cellular cholesterol distribution appear to trigger not only a change in the location and functioning of SNAREs at the cell surface but also in endomembranes. In this Commentary, we will discuss how disrupted cholesterol transport through the Golgi and endosomal compartments ultimately controls SNARE-mediated delivery of ECM and integrins to the cell surface and, consequently, cell migration.
    MeSH term(s) Animals ; Cholesterol/metabolism ; Humans ; Intracellular Membranes/metabolism ; Protein Transport ; SNARE Proteins/metabolism
    Chemical Substances SNARE Proteins ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2015-03-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.164459
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