scholarly journals Syndecan-4 Modulates Cell Polarity and Migration by Influencing Centrosome Positioning and Intracellular Calcium Distribution

2020 ◽  
Vol 8 ◽  
Author(s):  
Daniel Becsky ◽  
Kitti Szabo ◽  
Szuzina Gyulai-Nagy ◽  
Tamas Gajdos ◽  
Zsuzsa Bartos ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
Cell Polarity ◽  
Calcium Distribution ◽  
And Migration

scholarly journals WDR5 modulates cell motility and morphology and controls nuclear changes induced by a 3D environment

2018 ◽  
Vol 115 (34) ◽  
pp. 8581-8586 ◽  
Author(s):  
Pengbo Wang ◽  
Marcel Dreger ◽  
Elena Madrazo ◽  
Craig J. Williams ◽  
Rafael Samaniego ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Polarity ◽  
Underlying Mechanism ◽  
H3k4 Methylation ◽  
Nuclear Mechanics ◽  
3D Environment ◽  
3D Environments ◽  
And Migration

Cell migration through extracellular matrices requires nuclear deformation, which depends on nuclear stiffness. In turn, chromatin structure contributes to nuclear stiffness, but the mechanosensing pathways regulating chromatin during cell migration remain unclear. Here, we demonstrate that WD repeat domain 5 (WDR5), an essential component of H3K4 methyltransferase complexes, regulates cell polarity, nuclear deformability, and migration of lymphocytes in vitro and in vivo, independent of transcriptional activity, suggesting nongenomic functions for WDR5. Similarly, depletion of RbBP5 (another H3K4 methyltransferase subunit) promotes similar defects. We reveal that a 3D environment increases the H3K4 methylation dependent on WDR5 and results in a globally less compacted chromatin conformation. Further, using atomic force microscopy, nuclear particle tracking, and nuclear swelling experiments, we detect changes in nuclear mechanics that accompany the epigenetic changes induced in 3D conditions. Indeed, nuclei from cells in 3D environments were softer, and thereby more deformable, compared with cells in suspension or cultured in 2D conditions, again dependent on WDR5. Dissecting the underlying mechanism, we determined that actomyosin contractility, through the phosphorylation of myosin by MLCK (myosin light chain kinase), controls the interaction of WDR5 with other components of the methyltransferase complex, which in turn up-regulates H3K4 methylation activation in 3D conditions. Taken together, our findings reveal a nongenomic function for WDR5 in regulating H3K4 methylation induced by 3D environments, physical properties of the nucleus, cell polarity, and cell migratory capacity.

Intracellular calcium distribution in apoptosis of HL-60 cells induced by harringtonine: intranuclear accumulation and regionalization

1998 ◽  
Vol 127 (1-2) ◽  
pp. 113-121 ◽  
Author(s):  
Min Fang ◽  
Hongqing Zhang ◽  
Shaobai Xue ◽  
Nan Li ◽  
Liming Wang
Keyword(s):  
Intracellular Calcium ◽  
Calcium Distribution

scholarly journals Fine Tuning Cell Migration by a Disintegrin and Metalloproteinases

2017 ◽  
Vol 2017 ◽  
pp. 1-22 ◽  
Author(s):  
D. Dreymueller ◽  
K. Theodorou ◽  
M. Donners ◽  
A. Ludwig
Keyword(s):  
Cell Migration ◽  
Cell Polarity ◽  
Immune Cell ◽  
Tissue Homeostasis ◽  
Fine Tuning ◽  
Tissue Cell ◽  
Cancer Cell Migration ◽  
Physiological Processes ◽  
Cell Tissue ◽  
And Migration

Cell migration is an instrumental process involved in organ development, tissue homeostasis, and various physiological processes and also in numerous pathologies. Both basic cell migration and migration towards chemotactic stimulus consist of changes in cell polarity and cytoskeletal rearrangement, cell detachment from, invasion through, and reattachment to their neighboring cells, and numerous interactions with the extracellular matrix. The different steps of immune cell, tissue cell, or cancer cell migration are tightly coordinated in time and place by growth factors, cytokines/chemokines, adhesion molecules, and receptors for these ligands. This review describes how a disintegrin and metalloproteinases interfere with several steps of cell migration, either by proteolytic cleavage of such molecules or by functions independent of proteolytic activity.

Effect of halomethanes on intracellular calcium distribution in hepatocytes

Life Sciences ◽  
1984 ◽  
Vol 35 (11) ◽  
pp. 1231-1240 ◽  
Author(s):  
William J. Brattin ◽  
Robert L. Waller
Keyword(s):  
Intracellular Calcium ◽  
Calcium Distribution

scholarly journals Planar Cell Polarity Acts Through Septins to Control Collective Cell Movement and Ciliogenesis

Science ◽  
2010 ◽  
Vol 329 (5997) ◽  
pp. 1337-1340 ◽  
Author(s):  
Su Kyoung Kim ◽  
Asako Shindo ◽  
Tae Joo Park ◽  
Edwin C. Oh ◽  
Srimoyee Ghosh ◽  
...  
Keyword(s):  
Cell Polarity ◽  
Planar Cell Polarity ◽  
Control Point ◽  
Cell Movement ◽  
Cytoskeletal Proteins ◽  
Pcp Signaling ◽  
Cellular Machinery ◽  
And Migration ◽  
Controlling Behaviors ◽  
Shed Light

The planar cell polarity (PCP) signaling pathway governs collective cell movements during vertebrate embryogenesis, and certain PCP proteins are also implicated in the assembly of cilia. The septins are cytoskeletal proteins controlling behaviors such as cell division and migration. Here, we identified control of septin localization by the PCP protein Fritz as a crucial control point for both collective cell movement and ciliogenesis in Xenopus embryos. We also linked mutations in human Fritz to Bardet-Biedl and Meckel-Gruber syndromes, a notable link given that other genes mutated in these syndromes also influence collective cell movement and ciliogenesis. These findings shed light on the mechanisms by which fundamental cellular machinery, such as the cytoskeleton, is regulated during embryonic development and human disease.

scholarly journals CCL19/CCL21-triggered signal transduction and migration of dendritic cells requires prostaglandin E2

Blood ◽  
2004 ◽  
Vol 103 (5) ◽  
pp. 1595-1601 ◽  
Author(s):  
Elke Scandella ◽  
Ying Men ◽  
Daniel F. Legler ◽  
Silke Gillessen ◽  
Ladislav Prikler ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Intracellular Calcium ◽  
Human Monocyte ◽  
Surface Expression ◽  
Calcium Flux ◽  
Cell Surface Expression ◽  
Phosphatidylinositol 3 Kinase ◽  
Inflammatory Stimuli ◽  
And Migration ◽  
Phosphatidylinositol 3

Abstract The control of dendritic cell (DC) migration is pivotal for the initiation of cellular immune responses. When activated with inflammatory stimuli, the chemokine receptor CCR7 is up-regulated on DCs. Activated DCs home to lymphoid organs, where the CCR7 ligands CCL19 and CCL21 are expressed. We previously found that human monocyte-derived DCs (MoDCs) exclusively migrated to CCL19 and CCL21 when matured in the presence of prostaglandin (PG) E2. Because PGE2 did not alter CCR7 cell surface expression, we examined whether PGE2 may exert its effect by coupling CCR7 to signal transduction modules. Indeed, stimulation with CCR7 ligands led to enhanced phosphatidylinositol-3-kinase–mediated phosphorylation of protein kinase B when MoDCs were matured in the presence of PGE2. Moreover, CCL19/CCL21-induced intracellular calcium mobilization in MoDCs occurred only when PGE2 was present during maturation. MoDC migration to CCL19 and CCL21 was dependent on phospholipase C and intracellular calcium flux but not on phosphatidylinositol-3 kinase. Hence, our data provide insight into CCL19/CCL21-triggered signal transduction pathways and identify a novel function for PGE2 in controlling the migration of mature MoDCs by facilitating CCR7 signal transduction.

Cytochemical analysis of intracellular calcium distribution in the anterior pituitary of the rat

1981 ◽  
Vol 220 (1) ◽  
Author(s):  
M.Patricia Leuschen ◽  
C.Michael Moriarty ◽  
H.Wayne Sampson ◽  
I. Piscopo
Keyword(s):  
Intracellular Calcium ◽  
Anterior Pituitary ◽  
Calcium Distribution ◽  
Cytochemical Analysis

scholarly journals Microtubule Asymmetry during Neutrophil Polarization and Migration

2002 ◽  
Vol 13 (12) ◽  
pp. 4470-4483 ◽  
Author(s):  
Robert J. Eddy ◽  
Lynda M. Pierini ◽  
Frederick R. Maxfield
Keyword(s):  
Cell Polarity ◽  
Myosin Light Chain Kinase ◽  
Large Scale ◽  
Myosin Light Chain ◽  
Kinase Inhibitor ◽  
Myosin Ii ◽  
Cytochalasin D ◽  
Polymorphonuclear Neutrophils ◽  
Specific Marker ◽  
And Migration

The development of cell polarity in response to chemoattractant stimulation in human polymorphonuclear neutrophils (PMNs) is characterized by the rapid conversion from round to polarized morphology with a leading lamellipod at the front and a uropod at the rear. During PMN polarization, the microtubule (MT) array undergoes a dramatic reorientation toward the uropod that is maintained during motility and does not require large-scale MT disassembly or cell adhesion to the substratum. MTs are excluded from the leading lamella during polarization and motility, but treatment with a myosin light chain kinase inhibitor (ML-7) or the actin-disrupting drug cytochalasin D causes an expansion of the MT array and penetration of MTs into the lamellipod. Depolymerization of the MT array before stimulation caused 10% of the cells to lose their polarity by extending two opposing lateral lamellipodia. These multipolar cells showed altered localization of a leading lamella-specific marker, talin, and a uropod-specific marker, CD44. In summary, these results indicate that F-actin– and myosin II-dependent forces lead to the development and maintenance of MT asymmetry that may act to reinforce cell polarity during PMN migration.

Intracellular calcium distribution map and chemical shift of neurons examined by computer controlled electron probe X-ray microanalyser

1978 ◽  
Vol 36 (2) ◽  
pp. 126-127
Author(s):  
Minoru Onozuka ◽  
Eiichi Sugaya ◽  
Aiko Sugaya ◽  
Masayoshi Usami
Keyword(s):  
Chemical Shift ◽  
Intracellular Calcium ◽  
Electron Probe ◽  
Cellular Function ◽  
Distribution Map ◽  
X Ray ◽  
Calcium Distribution ◽  
Computer Controlled ◽  
Bursting Activity

The role of divalent cations, particularly of calcium, has gained increasing interest as a charge carrier and in processes such as regulation of enzymatic activities, in secretions of humoral transmitters and initiation of muscle contraction. The role of calcium has become very important in manifesting the bursting activity of neurons by various electrophysiological techniques, especially by voltage clamping. The distribution of calcium compared with the ultrastructure of nerve cells, however, has not been widely investigated. Analysis by the electron probe X-ray microanalyser(EPXMA) makes this type of research easier. To determine the relationship between calcium localization within the neuron and cellular function, we tried to make an intracellular calcium distribution map of the normal state and that during bursting activity by the computer controlled EPXMA. We also detected the chemical shift between the different states of cellular function caused by the intracellular calcium binding state.

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