Stimulatory Effect of Lipoprotein (a) on Proliferation of Human Mesangial Cells: Role of Lipoprotein (a) in Renal Disease

1998 ◽  
Vol 249 (2) ◽  
pp. 313-320 ◽  
Author(s):  
Ryuichi Morishita ◽  
Kei Yamamoto ◽  
Shingo Yamada ◽  
Hidetsugu Matsushita ◽  
Naruya Tomita ◽  
...  
Keyword(s):  
Renal Disease ◽  
Mesangial Cells ◽  
Human Mesangial Cells ◽  
Lipoprotein A

Mesangial cells express PDGF mRNAs and proliferate in response to PDGF

1988 ◽  
Vol 255 (4) ◽  
pp. F674-F684 ◽  
Author(s):  
P. J. Shultz ◽  
P. E. DiCorleto ◽  
B. J. Silver ◽  
H. E. Abboud
Keyword(s):  
Endothelial Cells ◽  
Growth Factor ◽  
Northern Blot Analysis ◽  
Mesangial Cells ◽  
Glomerular Mesangial Cells ◽  
Human Mesangial Cells ◽  
Human Foreskin Fibroblasts ◽  
Human Glomerular Mesangial Cells ◽  
Paracrine Growth Factor

Platelet-derived growth factor (PDGF) is a potent mitogen for cells of mesenchymal origin and is released and/or synthesized by platelets, macrophages, endothelial cells, and rat mesangial cells. In the present investigation, we found that human glomerular mesangial cells in culture release a PDGF-like protein which competes for 125I-PDGF binding to human foreskin fibroblasts and is mitogenic for these fibroblasts. The competing and to a lesser extent the mitogenic activities present in the conditioned medium are partially recognized by an anti-PDGF antibody. Northern blot analysis of poly(A)+ RNA from human mesangial cells demonstrates the expression of both PDGF A- and B-chain mRNAs. PDGF also binds to mesangial cells in a specific manner and stimulates DNA synthesis and cell proliferation. These data suggest that a PDGF-like protein secreted by mesangial cells or released from platelets, monocytes, or endothelial cells during glomerular inflammation may function as an autocrine or a paracrine growth factor for these cells. The biological role of PDGF in mediating proliferative and other inflammatory events in the glomerulus remains to be identified.

Dexamethasone upregulates ANP C-receptor protein in human mesangial cells without affecting mRNA

1996 ◽  
Vol 270 (3) ◽  
pp. F440-F446 ◽  
Author(s):  
N. Ardaillou ◽  
V. Blaise ◽  
S. Placier ◽  
F. Amestoy ◽  
R. Ardaillou
Keyword(s):  
Glucocorticoid Receptor ◽  
Natriuretic Peptide ◽  
Mesangial Cells ◽  
Receptor Protein ◽  
C Protein ◽  
Human Mesangial Cells ◽  
Receptor Inhibition ◽  
Target Sites ◽  
Dissociation Constant Kd

The objective of this study was to examine the role of dexamethasone on the expression of natriuretic peptide B-type and C-type receptors (ANPR-B and ANPR-C) in cultured human mesangial cells, which only possess these two subtypes. Dexamethasone caused concentration- and time-dependent increases in 125I-labeled ANP binding, which were prevented by glucocorticoid receptor inhibition with RU-38486. A lag time of 24 h and a concentration of dexamethasone of at least 1 nmol/l were necessary for this effect to occur. Dexamethasone-induced upregulation of 125I-ANP binding resulted from increased receptor density. No change in dissociation constant (Kd) was observed. Only ANPR-C were affected by dexamethasone. Indeed, dexamethasone did not modify C-type natriuretic peptide (i.e., CNP)-dependent cGMP production by mesangial cells. Moreover, dexamethasone upregulated ANPR-C protein expression as shown by Western blot analysis and by an increase in ANPR-C immunoreactivity at the cell surface. In contrast, dexamethasone did not modify ANPR-C mRNA expression. In conclusion, glucocorticoids increase ANPR-C density on mesangial cells through a mechanism implying, successively, interaction with the glucocorticoid receptor and increase of ANPR-C protein synthesis at a posttranscriptional stage. Thus dexamethasone may influence availability of natriuretic peptides at their glomerular target sites.

Multiple P2X receptors are involved in the modulation of apoptosis in human mesangial cells: evidence for a role of P2X4

2007 ◽  
Vol 292 (5) ◽  
pp. F1537-F1547 ◽  
Author(s):  
Anna Solini ◽  
Eleonora Santini ◽  
Daniele Chimenti ◽  
Paola Chiozzi ◽  
Federico Pratesi ◽  
...  
Keyword(s):  
Mesangial Cells ◽  
Chronic Renal Disease ◽  
Morphological Changes ◽  
Purinergic Signaling ◽  
Annexin V ◽  
Renal Tissue ◽  
P2x Receptor ◽  
Main Role ◽  
Human Mesangial Cells

Apoptosis, a normal event in renal tissue homeostasis, has been considered as a major mechanism for either resolution of glomerular hypercellularity in glomerulonephritis or loss of cellularity and progression to glomerulosclerosis in chronic renal disease. This study was aimed at investigating the role of extracellular ATP (eATP) in mediating apoptosis in human mesangial cells (HMC) and identifying the subtype(s) of purinergic receptors involved. eATP, but not uridin-5′-triphosphate (UTP), caused dose-dependent modifications of cellular morphology, as assessed by contrast-phase microscopy, and late apoptosis, as measured by Annexin V/propidium iodide-based flow cytometry and caspase-3 activation. Both phenomena were prevented by the P2X antagonist oxidized-ATP. 2′, 3′-O-(4-benzoylbenzoyl)adenosine 5′-triphosphate (BzATP) was less effective than ATP, whereas 1[N,O-bis (5-isoquinolinesulfonyl)-N-methyl-l-tyrosyl] -4-phenylpiperazine (KN62), a selective inhibitor of human P2X7, prevented morphological changes but potentiated apoptosis induced by BzATP. P2X7 was barely expressed in HMC and showed a relatively scarce functional activity, as assessed by monitoring nucleotide-induced intracellular calcium surge and plasma membrane depolarization by Fura-2/AM and bis[1,3-diethylthiobarbiturate]trimethineoxonal uptake, respectively. These data indicated a negligible role of P2X7 in eATP-mediated apoptosis and pointed to the involvement of other P2X receptor(s). Molecular and inhibitor studies suggested a main role for P2X4 receptor in nucleotide-induced apoptosis in HMC, indicating a relevant role for purinergic signaling in regulating death rate in these cells.

The role of CXCL16 and its processing metalloproteinases ADAM10 and ADAM17 in the proliferation and migration of human mesangial cells

2008 ◽  
Vol 370 (2) ◽  
pp. 311-316 ◽  
Author(s):  
Anja Schramme ◽  
Mohamed Sadek Abdel-Bakky ◽  
Nicole Kämpfer-Kolb ◽  
Josef Pfeilschifter ◽  
Paul Gutwein
Keyword(s):  
Mesangial Cells ◽  
Human Mesangial Cells ◽  
And Migration ◽  
Proliferation And Migration

scholarly journals Lipoprotein (a) stimulates mitogen activated protein kinase in human mesangial cells

FEBS Letters ◽  
1998 ◽  
Vol 441 (2) ◽  
pp. 205-208 ◽  
Author(s):  
Ulrich F. Mondorf ◽  
Albrecht Piiper ◽  
Martina Herrero ◽  
Michael Bender ◽  
Ernst H. Scheuermann ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mesangial Cells ◽  
Mitogen Activated Protein Kinase ◽  
Human Mesangial Cells ◽  
Lipoprotein A ◽  
Mitogen Activated Protein

Role of aldose reductase in TGF-β1-induced fibronectin synthesis in human mesangial cells

2009 ◽  
Vol 37 (6) ◽  
pp. 2735-2742 ◽  
Author(s):  
Yuejuan Zhang ◽  
Ping Huang ◽  
Tao Jiang ◽  
Jingjing Zhao ◽  
Nong Zhang
Keyword(s):  
Aldose Reductase ◽  
Mesangial Cells ◽  
Human Mesangial Cells ◽  
Tgf Β1

Role of aldose reductase in the high glucose induced expression of fibronectin in human mesangial cells

2009 ◽  
Vol 37 (6) ◽  
pp. 3017-3021 ◽  
Author(s):  
Ping Huang ◽  
Yuejuan Zhang ◽  
Tao Jiang ◽  
Wenjiao Zeng ◽  
Nong Zhang
Keyword(s):  
Aldose Reductase ◽  
High Glucose ◽  
Mesangial Cells ◽  
Induced Expression ◽  
Human Mesangial Cells

scholarly journals Regulation of capacitative calcium influx in cultured human mesangial cells: roles of protein kinase C and calmodulin.

1996 ◽  
Vol 7 (7) ◽  
pp. 983-990
Author(s):  
P Menè ◽  
F Pugliese ◽  
G A Cinotti
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mesangial Cells ◽  
Calcium Influx ◽  
Resting Cells ◽  
Cellular Mechanisms ◽  
Direct Role ◽  
Human Mesangial Cells ◽  
Kinase C

Sustained Ca2+ influx follows discharge of intracellularly stored Ca2+ in a variety of cell types previously equilibrated in Ca(2+)-free media, including cultured human mesangial cells. This Ca2+ influx pathway has been referred to as capacitative Ca2+ entry or Ca2+ release-activated Ca2+ influx (iCRAC). This study investigated two cellular mechanisms potentially controlling iCRAC in human mesangial cells, protein kinase C (PKC), a key signalling kinase activated by vasoconstrictors that release Ca2+ from internal stores, and calmodulin, a Ca(2+)-binding protein that may couple Ca2+ release to the putative channel(s). The PKC activator phorbol myristate acetate (PMA) dose-dependently inhibited both Ca2+ influx in resting cells and iCRAC, assessed by microfluorometry in fura-2-loaded monolayers, when added before or after 1 uM angiotensin II (AngII) (Ca2+ influx at 1 mM (Ca2+)e +278 +/- 56%/+80 +/- 8%, at 10 mM + 473 +/- 59%/+250 +/- 24% (Ca2+)e, -/+ PMA, respectively, P < 0.05). PMA did not affect 5 uM ionomycin-induced iCRAC, possibly because it downregulated Ca2+ release by AngII but not by ionomycin, suggesting a key role of released Ca2+ in triggering subsequent Ca2+ influx. This was confirmed by buffering the (Ca2+)i elevation induced by AngII with intracellularly trapped 1,2-bis-(0-Aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid (BAPTA), which abolished any subsequent iCRAC. Moreover, the calmodulin inhibitors calmidazolium (10 uM), trifluoperazine (0.1 mM), or W-7 (0.1 mM) significantly inhibited AngII- or ionomycin-activated iCRAC (+106 +/- 38/229 +/- 53, +58 +/- 9/195 +/- 29, +161 +/- 38/180 +/- 40% at 1/10 mM (Ca2+)e, all P < 0.05), but did not affect basal Ca2+ entry, consistent with a direct role of cytoplasmic Ca2+ in the regulation of ion gating. These results indicate that iCRAC is under the control of both PKC and calmodulin, and that the site of regulation is distal to the emptying of Ca2+ stores. iCRAC may represent a key mechanism for the control of Ca(2+)-regulated mesangial functions.

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