The significance of integrin ligand nanopatterning on lipid raft clustering in hematopoietic stem cells

Altrock, Eva; Muth, Christine Anna; Klein, Gerd; Spatz, Joachim P.; Lee-Thedieck, Cornelia

doi:10.1016/j.biomaterials.2012.01.002

Cited by 70 publications

(65 citation statements)

References 41 publications

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“…Differentiation between the possible role of PI3K in the mechanosensing machinery, the signal integration or cell response was not possible on the basis of the inhibition experiments performed here. Nevertheless, we and others have found that adhesion of KG-1a cells and HSPCs to fibronectin is mediated by integrins (Altrock et al, 2012;Franke et al, 2007;Liesveld et al, 1993). Because adhesion is a prerequisite for cell migration over a surface, the mechanosensitive migration behavior of the HSPCs on the applied fibronectin-functionalized substrates with different stiffnesses is also dependent on the integrin-mediated adhesion to fibronectin.…”

Section: Discussionmentioning

confidence: 57%

Impact of substrate elasticity on human hematopoietic stem and progenitor cell adhesion and motility

Lee-Thedieck

Rauch

Fiammengo

et al. 2012

Journal of Cell Science

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SummaryIn the bone marrow, hematopoietic stem cells (HSCs) reside in endosteal and vascular niches. The interactions with the niches are essential for the maintenance of HSC number and properties. Although the molecular nature of these interactions is well understood, little is known about the role of physical parameters such as matrix elasticity. Osteoblasts, the major cellular component of the endosteal HSC niche, flatten during HSC mobilization. We show that this process is accompanied by osteoblast stiffening, demonstrating that not only biochemical signals but also mechanical properties of the niche are modulated. HSCs react to stiffer substrates with increased cell adhesion and migration, which could facilitate the exit of HSCs from the niche. These results indicate that matrix elasticity is an important factor in regulating the retention of HSCs in the endosteal niche and should be considered in attempts to propagate HSCs in vitro for clinical applications.

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Section: Discussionmentioning

confidence: 57%

Impact of substrate elasticity on human hematopoietic stem and progenitor cell adhesion and motility

Lee-Thedieck

Rauch

Fiammengo

et al. 2012

Journal of Cell Science

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“…However, following activation of these cells (via fibronectin or ligation using anti-CD34 antibodies), CD34 redistributes to lipid rafts and in some cases is even polarized toward the uropod, suggesting a role in enhanced homotypic adhesion. [78][79][80][81] In fact, studies comparing full-length CD34, a truncated form of CD34 (where most of the cytoplasmic domain is removed), and a chimeric molecule where the cytoplasmic domain of CD34 is fused with the extracellular domain of a cytokine receptor that is not believed to have a role in adhesion, implicate the cytoplasmic domain in the mediation of signaling events causing increased adhesion. 4,79 This role of CD34 in homotypic cell adhesion is significantly abrogated through the tyrosine kinase inhibitor and integrin mAb blockers for LFA-1 and ICAM-1, suggesting a concomitant activation of the LFA-1/ICAM-1 pathway.…”

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confidence: 99%

Not just a marker: CD34 on human hematopoietic stem/progenitor cells dominates vascular selectin binding along with CD44

AbuSamra¹,

Aleisa²,

Al-Amoodi³

et al. 2017

Blood Advances

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“…Reports have described, using DRMs, raft clustering upon activation of the Fcγ receptor IIA (FcγRIIA) in U937 monocytes [53]. Altrock et al, by using conventional confocal microscopy, reported raft clustering upon interaction of integrins to a fibronectin layer in human acute myelogenous leukemia KG-1 myeloblasts [54]. In isolated DRM from B cells, raft coalescence has been described [55].…”

Section: Discussionmentioning

confidence: 99%

Oxidative stress effect on progesterone-induced blocking factor (PIBF) binding to PIBF-receptor in lymphocytes

Haba

Palacio

Palkovics

et al. 2014

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Receptor-ligand binding is an essential interaction for biological function. Oxidative stress can modify receptors and/or membrane lipid dynamics, thus altering cell physiological functions. The aim of this study is to analyze how oxidative stress may alter receptor-ligand binding and lipid domain distribution in the case of progesterone-induced blocking factor/progesterone-induced blocking factor-receptor. For membrane fluidity regionalization analysis of MEC-1 lymphocytes, two-photon microscopy was used in individual living cells. Lymphocytes were also double stained with AlexaFluor647/progesterone-induced blocking factor and Laurdan to evaluate -induced blocking factor/progesterone-induced blocking factor-receptor distribution in the different membrane domains, under oxidative stress. A new procedure has been developed which quantitatively analyzes the regionalization of a membrane receptor among the lipid domains of different fluidity in the plasma membrane. We have been able to establish a new tool which detects and evaluates lipid raft clustering from two-photon microscopy images of individual living cells. We show that binding of progesterone-induced blocking factor to progesterone-induced blocking factor-receptor causes a rigidification of plasma membrane which is related to an increase of lipid raft clustering. However, this clustering is inhibited under oxidative stress conditions. In conclusion, oxidative stress decreases membrane fluidity, impairs receptor-ligand binding and reduces lipid raft clustering.

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The significance of integrin ligand nanopatterning on lipid raft clustering in hematopoietic stem cells

Cited by 70 publications

References 41 publications

Impact of substrate elasticity on human hematopoietic stem and progenitor cell adhesion and motility

Impact of substrate elasticity on human hematopoietic stem and progenitor cell adhesion and motility

Not just a marker: CD34 on human hematopoietic stem/progenitor cells dominates vascular selectin binding along with CD44

Oxidative stress effect on progesterone-induced blocking factor (PIBF) binding to PIBF-receptor in lymphocytes

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