Integrin‐mediated calcium signaling and regulation of cell adhesion by intracellular calcium

Sjaastad, Michael D.; Nelson, W. James

doi:10.1002/bies.950190109

Cited by 144 publications

(104 citation statements)

References 82 publications

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“…To determine whether intracellular tension is needed to maintain myofibril alignment, we incubated patterned hPSC-CMs in EDTA to chelate calcium and reduce integrin-mediated cell-substrate adhesion (33,34) and disrupt myofibril tension (35) and the intracellular balance of forces. Beating stopped upon EDTA addition, whereas buckling, disruption, and loosening of myofibrils and loss of sarcomere periodic organization increased with incubation (SI Appendix, Fig.…”

Section: Resultsmentioning

confidence: 99%

Contractility of single cardiomyocytes differentiated from pluripotent stem cells depends on physiological shape and substrate stiffness

Ribeiro

Ang

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

415

456

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Single cardiomyocytes contain myofibrils that harbor the sarcomerebased contractile machinery of the myocardium. Cardiomyocytes differentiated from human pluripotent stem cells (hPSC-CMs) have potential as an in vitro model of heart activity. However, their fetallike misalignment of myofibrils limits their usefulness for modeling contractile activity. We analyzed the effects of cell shape and substrate stiffness on the shortening and movement of labeled sarcomeres and the translation of sarcomere activity to mechanical output (contractility) in live engineered hPSC-CMs. Single hPSC-CMs were cultured on polyacrylamide substrates of physiological stiffness (10 kPa), and Matrigel micropatterns were used to generate physiological shapes (2,000-μm 2 rectangles with length:width aspect ratios of 5:1-7:1) and a mature alignment of myofibrils. Translation of sarcomere shortening to mechanical output was highest in 7:1 hPSC-CMs. Increased substrate stiffness and applied overstretch induced myofibril defects in 7:1 hPSC-CMs and decreased mechanical output. Inhibitors of nonmuscle myosin activity repressed the assembly of myofibrils, showing that subcellular tension drives the improved contractile activity in these engineered hPSC-CMs. Other factors associated with improved contractility were axially directed calcium flow, systematic mitochondrial distribution, more mature electrophysiology, and evidence of transverse-tubule formation. These findings support the potential of these engineered hPSC-CMs as powerful models for studying myocardial contractility at the cellular level.contractility | sarcomeres | cardiomyocyte | stem cell | single cell

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Section: Resultsmentioning

confidence: 99%

Contractility of single cardiomyocytes differentiated from pluripotent stem cells depends on physiological shape and substrate stiffness

Ribeiro

Ang

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

415

456

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“…The association of cytosolic-free Ca 2ϩ with cell shape and dynamics of the actin cytoskeleton, as well as the formation and disassembly of cell-to-substrate adhesions, is well known. 19) Ca 2ϩ also serves as a second messenger in many biochemical signal-transduction events. 19) These observations strongly suggest that the cause of decreased ROS formation in Hep G2/SMP30 cells may be intracellular Ca 2ϩ modulation by SMP30/GNL over-expression.…”

Section: Discussionmentioning

confidence: 99%

“…19) Ca 2ϩ also serves as a second messenger in many biochemical signal-transduction events. 19) These observations strongly suggest that the cause of decreased ROS formation in Hep G2/SMP30 cells may be intracellular Ca 2ϩ modulation by SMP30/GNL over-expression.…”

Section: Discussionmentioning

confidence: 99%

Over-expression of Senescence Marker Protein-30 Decreases Reactive Oxygen Species in Human Hepatic Carcinoma Hep G2 Cells

Handa

Maruyama

Ishigami

2009

Biological & Pharmaceutical Bulletin

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Senescence Marker Protein-30 (SMP30) was originally identified as a novel protein in the rat liver, the expression of which decreases androgen-independently with aging. 1,2) SMP30 is a 34 kDa protein expressed mainly in hepatocytes and renal tubular epithelia, 1) and its amino acid sequences are highly conserved among vertebrates, i.e., 70 to 90%, strongly suggesting that the age-dependent decreases of SMP30 reported in the liver, kidney and lung may contribute to senescence.1,3-7) SMP30 transcripts have been detected in multiple mouse tissues including the liver, kidney, brain, lung and testis by reverse transcription-polymerase chain reaction (RT-PCR) analysis. 7) In humans, immunohistochemical staining has localized SMP30 mainly in parenchymal cells of the liver, proximal tubular cells of the kidney, acinal and ductal cells of the pancreas and fasciculata cells of the adrenal cortex.2) The human SMP30 gene, which is located in the p11.3-q11.2 segment of the X chromosome, 4) could be a candidate agent of X-linked diseases mapped to that region.To clarify the physiological functions and the relationships between age-associated decreases of SMP30 and disorders of aged organs, we established SMP30 knockout mice. 8) These knockout animals are viable and fertile but lower in body weight and shorter in life span than the wild-type. 9) Throughout our experiments in vitro and in vivo, the livers of SMP30 knockout mice were far more susceptible to tumor necrosis factor (TNF)-a-and Fas-mediated apoptosis than those from the wild-type. 8) Moreover, histological and biochemical analyses of livers from SMP30 knockout mice showed abnormal accumulations of neutral lipids and phospholipids.9) This abnormal lipid metabolism must increase the tissues' susceptibility to apoptosis. Such changes of SMP30 expression might, then, account for the deterioration of cellular functions and lowered resistance to harmful stimuli in aged tissues.We recently identified SMP30 as a gluconolactonase (GNL, EC 3.1.1.17) that is involved in the vitamin C biosynthetic pathway and found that SMP30/GNL knockout mice cannot synthesize vitamin C in vivo.10) Humans, monkeys and guinea pigs are similarly incapable of synthesizing vitamin C in vivo, because the gluconolactone oxidase gene has mutated throughout evolution; however, mice, rats and many other animals do synthesize vitamin C in vivo. With aging, SMP30/GNL content decreases in the liver, kidney and lung, and such decreases affect the normally copious amount of SMP30/GNL in the livers of younger humans.2) To discern what, if any, functions SMP30/GNL has in the human liver, we transfected the Hep G2 human liver carcinoma cell line with the human SMP30/GNL gene. In the present study, we found that the over-expression of SMP30/GNL in these Hep G2 cells contributed to the decrease of reactive oxygen species (ROS) formation, presumably increasing the cells' state of oxidative stress. MATERIALS AND METHODSCell Culture Stable transfectants expressing the human SMP30/GNL were established as described p...

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“…Perhaps, IL-1 binding to its receptor also triggers activation of integrin-associated signaling components within the same focal adhesion complex. Indeed, integrin-fibronectin interactions have been shown to activate MAP kinases and mediate calcium flux (32,33). Localization of IL-1 receptors and integrin-associated signaling molecules at focal adhesions may be required to enhance the sensitivity to IL-1 binding and generation of calcium fluxes; this sensitization could induce signaling levels that are sufficient for the activation of ERK kinases and c-fos expression.…”

Section: Requirement Of Focal Adhesions and Calcium On Serum Responsementioning

confidence: 99%

Requirements of Focal Adhesions and Calcium Fluxes for Interleukin-1-induced ERK Kinase Activation and c-fos Expression in Fibroblasts

Lo¹,

Luo²,

McCulloch³

et al. 1998

Journal of Biological Chemistry

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Integrin‐mediated calcium signaling and regulation of cell adhesion by intracellular calcium

Cited by 144 publications

References 82 publications

Contractility of single cardiomyocytes differentiated from pluripotent stem cells depends on physiological shape and substrate stiffness

Contractility of single cardiomyocytes differentiated from pluripotent stem cells depends on physiological shape and substrate stiffness

Over-expression of Senescence Marker Protein-30 Decreases Reactive Oxygen Species in Human Hepatic Carcinoma Hep G2 Cells

Requirements of Focal Adhesions and Calcium Fluxes for Interleukin-1-induced ERK Kinase Activation and c-fos Expression in Fibroblasts

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