Prominin-1/CD133: Lipid Raft Association, Detergent Resistance, and Immunodetection

Karbanová, Jana; Lorico, Aurelio; Bornhäuser, Martin; Corbeil, Denis; Fargeas, Christine A.

doi:10.1002/sctm.17-0223

Cited by 18 publications

(16 citation statements)

References 45 publications

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“…They were then rinsed and quenched for 10 minutes in PBS containing 50 mM NH 4 Cl prior to the incubation with the appropriate Alexa Fluor 488/546/555‐conjugated goat anti‐mouse IgG 1 (1:500; Molecular Probes, Life Technologies). For the intracellular labeling, PFA‐fixed cells were permeabilized with 0.1% saponin diluted in PBS containing 0.2% gelatin (blocking buffer IV) for 20 minutes at RT prior to immunolabeling for prominin‐1 (see above) and p34‐Arc/ARPC2 subunit of Arp2/3 complex using rabbit antiserum (5 μg/mL; Merck). Primary antibodies were observed using Alexa Fluor 488‐conjugated goat anti‐mouse IgG 1 and Alexa Fluor 555‐conjugated donkey anti‐rabbit IgG.…”

Section: Methodsmentioning

confidence: 99%

Prominin‐1 (CD133) modulates the architecture and dynamics of microvilli

Thamm

Šimaitė

Karbanová

et al. 2018

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Prominin‐1 is a cell surface biomarker that allows the identification of stem and cancer stem cells from different organs. It is also expressed in several differentiated epithelial and non‐epithelial cells. Irrespective of the cell type, prominin‐1 is associated with plasma membrane protrusions. Here, we investigate its impact on the architecture of membrane protrusions using microvilli of Madin‐Darby canine kidney cells as the main model. Our high‐resolution analysis revealed that upon the overexpression of prominin‐1 the number of microvilli and clusters of them increased. Microvilli with branched and/or knob‐like morphologies were observed and stimulated by mutations in the ganglioside‐binding site of prominin‐1. The altered phenotypes were caused by the interaction of prominin‐1 with phosphoinositide 3‐kinase and Arp2/3 complex. Mutation of tyrosine 828 of prominin‐1 impaired its phosphorylation and thereby inhibited the aforementioned interactions abolishing altered microvilli. This suggests that the interplay of prominin‐1‐ganglioside membrane complexes, phosphoinositide 3‐kinase and cytoskeleton components regulates microvillar architecture. Lastly, the expression of prominin‐1 and its mutants modified the structure of filopodia emerging from fibroblast‐like cells and silencing human prominin‐1 in primary hematopoietic stem cells resulted in the loss of uropod‐associated microvilli. Altogether, these findings strengthen the role of prominin‐1 as an organizer of cellular protrusions.

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Section: Methodsmentioning

confidence: 99%

Prominin‐1 (CD133) modulates the architecture and dynamics of microvilli

Thamm

Šimaitė

Karbanová

et al. 2018

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“…It is now considered as a stem cell and cancer stem cell marker, although this remains a matter of debate . Association of CD133 with specific lipid rafts is also being debated, and a concept has been proposed whereby “stem cell‐specific lipid rafts” would host determinants necessary for maintaining stem cell properties …”

Section: Exosomes and Differentiationmentioning

confidence: 99%

“…84 Association of CD133 with specific lipid rafts is also being debated, and a concept has been proposed whereby "stem cellspecific lipid rafts" would host determinants necessary for maintaining stem cell properties. 85 Hematopoietic stem and progenitor cells have a self-renewal capacity and can differentiate into mature blood cells. In these cells, it was shown that prominin-1 is present on the cell surface but also in an intracellular pool, partially co-localizing with CD63.…”

Section: Exosomal Release Of Prominin-1 During Cell Differentiationmentioning

confidence: 99%

Exosomes: Revisiting their role as “garbage bags”

Vidal

2019

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In recent years, the term “extracellular vesicle” (EV) has been used to define different types of vesicles released by various cells. It includes plasma membrane‐derived vesicles (ectosomes/microvesicles) and endosome‐derived vesicles (exosomes). Although it remains difficult to evaluate the compartment of origin of the two kinds of vesicles once released, it is critical to discriminate these vesicles because their mode of biogenesis is probably directly related to their physiologic function and/or to the physio‐pathologic state of the producing cell. The purpose of this review is to specifically consider exosome secretion and its consequences in terms of a material loss for producing cells, rather than on the effects of exosomes once they are taken up by recipient cells. I especially describe one putative basic function of exosomes, that is, to convey material out of cells for off‐site degradation by recipient cells. As illustrated by some examples, these components could be evacuated from cells for various reasons, for example, to promote “differentiation” or enhance homeostatic responses. This basic function might explain why so many diseases have made use of the exosomal pathway during pathogenesis.

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“…In this respect, immunological synapses formed as interfaces between activated lymphocytes and their cognate antigen presenting cells have been hypothesized to be an example of organized raft domains within the immune system ( 44 – 46 ). Furthermore, lipid rafts are also discussed to play a crucial role in hematopoietic stem cell homing ( 47 – 49 ), mobilization ( 47 , 50 , 51 ), and differentiation ( 52 – 54 ). Moreover, many studies indicate lipid rafts to be involved in various diseases, e.g., HIV-1 infection including a role in virus budding ( 55 , 56 ), cancer ( 57 ), or neurodegenerative disorders such as prion diseases ( 58 ), and Alzheimer's ( 59 , 60 ).…”

Section: The Cell Membrane Is a Highly Complex Lipid Bilayermentioning

confidence: 99%

Impact of Plasma Membrane Domains on IgG Fc Receptor Function

et al. 2020

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Lipid cell membranes not only represent the physical boundaries of cells. They also actively participate in many cellular processes. This contribution is facilitated by highly complex mixtures of different lipids and incorporation of various membrane proteins. One group of membrane-associated receptors are Fc receptors (FcRs). These cell-surface receptors are crucial for the activity of most immune cells as they bind immunoglobulins such as immunoglobulin G (IgG). Based on distinct mechanisms of IgG binding, two classes of Fc receptors are now recognized: the canonical type I FcγRs and select C-type lectin receptors newly referred to as type II FcRs. Upon IgG immune complex induced cross-linking, these receptors are known to induce a multitude of cellular effector responses in a cell-type dependent manner, including internalization, antigen processing, and presentation as well as production of cytokines. The response is also determined by specific intracellular signaling domains, allowing FcRs to either positively or negatively modulate immune cell activity. Expression of cell-type specific combinations and numbers of receptors therefore ultimately sets a threshold for induction of effector responses. Mechanistically, receptor cross-linking and localization to lipid rafts, i.e., organized membrane microdomains enriched in intracellular signaling proteins, were proposed as major determinants of initial FcR activation. Given that immune cell membranes might also vary in their lipid compositions, it is reasonable to speculate, that the cell membrane and especially lipid rafts serve as an additional regulator of FcR activity. In this article, we aim to summarize the current knowledge on the interplay of lipid rafts and IgG binding FcRs with a focus on the plasma membrane composition and receptor localization in immune cells, the proposed mechanisms underlying this localization and consequences for FcR function with respect to their immunoregulatory capacity.

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Prominin-1/CD133: Lipid Raft Association, Detergent Resistance, and Immunodetection

Cited by 18 publications

References 45 publications

Prominin‐1 (CD133) modulates the architecture and dynamics of microvilli

Prominin‐1 (CD133) modulates the architecture and dynamics of microvilli

Exosomes: Revisiting their role as “garbage bags”

Impact of Plasma Membrane Domains on IgG Fc Receptor Function

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