Expression of α-Actinin-1 in Human Glomerular Mesangial Cells <i>In Vivo</i> and <i>In Vitro</i>

Yang, Chong‐Ren; Glass, William F.

doi:10.3181/0710-rm-279

Cited by 12 publications

(12 citation statements)

References 25 publications

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“…Isolation of primary human renal glomerular mesangial cells (HMC) was done previously [37;38]. For this study cells were taken from previously prepared frozen stock and were maintained in RPMI 1640 containing 16.7% FBS and 100ug/ml penicillin and streptomycin as previously described [37;38].…”

Section: Methodsmentioning

confidence: 99%

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Prostaglandin E2 modifies SMAD2 and promotes SMAD2–SMAD4 complex formation

Yang

Chen

Sorokin

2014

Prostaglandins, Leukotrienes and Essential Fatty Acids

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We report that PGE2 promotes Smad2-Smad4 complex formation and this phenomenon could be blocked by DIDS, an anion transporter inhibitor. Our data suggest that PGE2 had no effects on Smad2 phosphorylation, suggesting that PGE2-mediated Smad2-Smad4 complex formation is independent of TGF-β signaling and that PGE2 induced Smad2 modification which is different from TGF-β-mediated phosphorylation. We demonstrate that in primary human glomerular mesangial cells PGE2 caused modification of Smad2 as detected by Smad2N antibody, raised against a peptide near the N-terminus of Smad2. We hypothesize that Smad2 protein is post-translationaly modified by PGE2. Direct evidence of Smad2 modification by PGE2 was achieved by avidin pulldown assay which showed that endogenous Smad2 and recombinant Smad2 protein were attached by biotin-labeled PGE2. Taken together, our results provided evidence that post-translational modification of Smad2 could be a mechanism for the action of PGE2 in the pathogenesis of human pathologies.

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Section: Methodsmentioning

confidence: 99%

“…For this study cells were taken from previously prepared frozen stock and were maintained in RPMI 1640 containing 16.7% FBS and 100ug/ml penicillin and streptomycin as previously described [37;38]. HMC at passages 5 through 8 were used.…”

Section: Methodsmentioning

confidence: 99%

Prostaglandin E2 modifies SMAD2 and promotes SMAD2–SMAD4 complex formation

Yang

Chen

Sorokin

2014

Prostaglandins, Leukotrienes and Essential Fatty Acids

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“…α-actinin-1 regulates gene expression, thus accelerating ECM accumulation in glomerular disease (40). α-actinin-1 has been documented to be a prognostic factor in leiomyosarcoma survival (24).…”

Section: Discussionmentioning

confidence: 99%

“…Another downregulated protein is α-actinin-1, an actinbinding protein with multiple roles in different cell types (40), including the connection between the cytoskeleton and diverse signaling pathways (41). α-actinin-1 regulates gene expression, thus accelerating ECM accumulation in glomerular disease (40).…”

Section: Discussionmentioning

confidence: 99%

Two-dimensional gel electrophoresis analysis of the leiomyoma interstitial fluid reveals altered protein expression with a possible involvement in pathogenesis

et al. 2015

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Abstract. Uterine leiomyoma is the most common smooth benign neoplasm. In the present study, we analyzed the global interstitial fluid (IF) profile of leiomyoma vs. normal myometrium to identify protein dysregulation involved in leiomyoma pathogenesis. Two-dimensional gel electrophoresis and mass spectrometry were used to generate and compare the global interstitial fluid profiles of the leiomyoma and of the normal tissue. Two proteins were validated by immunohistochemistry. By comparing the interstitial fluid profile of the leiomyoma with that of the normal myometrium, the levels of seven proteins were found to be significantly different: four structural organization proteins (desmin, prelamin-A/C, transgelin and α-actinin-1), an inflammatory response (α1-antitrypsin), a response to oxidative stress (peroxiredoxin-2), and a folding protein (heat shock 70 kDa protein 1A/1B). Desmin, α1-antitrypsin and peroxiredoxin-2 were upregulated in the leiomyoma, whereas heat shock 70 kDa protein 1A/1B, α-actinin-1, prelamin-A/C and transgelin were downregulated. Desmin and α1-antitrypsin were further validated by immunohistochemistry. By identifying proteins with altered expression levels compared to the myometrium from several pathways of the leiomyoma pathogenesis, we found the leiomyoma interstitial fluid to have a characteristic proteomic profile. A better appreciation of the pathophysiology of the disease can be useful in the development of conservative treatments that serve as viable alternatives to hysterectomy.

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“…Moreover, PAI-1 is also a component of the ECM, where it seems to bind tightly to the somatomedin B domain of vitronectin [42] . In pathological conditions in vivo, human mesangial cells overexpress PAI-1, and this upregulation may be related to the stimulation by various cytokines or growth factors such as TNF-␣ [43] and TGF-␤ [44] . In the present study, we have found the molecular mechanisms involved in a beneficial effect that PARP-1 inhibition decreased Ang II-induced upregulation of PAI-1 and FN expression in cultured RMCs.…”

Section: Discussionmentioning

confidence: 99%

Poly(ADP-Ribose) Polymerase-1 Mediates Angiotensin II-Induced Expression of Plasminogen Activator Inhibitor-1 and Fibronectin in Rat Mesangial Cells

Zhu¹,

Jiang²,

Lei³

et al. 2011

Kidney Blood Press Res

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Objective: To investigate the effects of poly(ADP-ribose) polymerase-1 (PARP-1) on angiotensin II (Ang II)-induced plasminogen activator inhibitor-1 (PAI-1) and fibronectin (FN) in rat mesangial cells (RMCs). Methods: Followed by serum starvation for 16 h, RMCs were exposed to Ang II for an indicated time to examine the protein expression of PARP-1. The cells were treated with or without Ang II for 12–24 h in the presence or absence of an inhibitor of PARP, N-(6-oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochloride (PJ34) or small interfering RNA (siRNA) duplexes targeting PARP-1. The mRNA and protein expressions of PARP-1, PAI-1 and FN were determined by real-time RT-PCR and Western blot, respectively. The activity of PARP-1 was examined by colorimetric assay. Results: Ang II did not only significantly induce PARP-1 expression and activity, but also increased PAI-1 and FN expression in RMCs. All these responses induced by Ang II were significantly inhibited by both the PARP inhibitor PJ34 and downregulating PARP-1 with the siRNA technique. Conclusions: Our data suggest that PARP-1 mediates Ang II-induced PAI-1 and FN in RMCs and may thus represent a potential therapeutic target in the treatment of glomerular disease.

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Expression of α-Actinin-1 in Human Glomerular Mesangial Cells In Vivo and In Vitro

Cited by 12 publications

References 25 publications

Prostaglandin E2 modifies SMAD2 and promotes SMAD2–SMAD4 complex formation

Prostaglandin E2 modifies SMAD2 and promotes SMAD2–SMAD4 complex formation

Two-dimensional gel electrophoresis analysis of the leiomyoma interstitial fluid reveals altered protein expression with a possible involvement in pathogenesis

Poly(ADP-Ribose) Polymerase-1 Mediates Angiotensin II-Induced Expression of Plasminogen Activator Inhibitor-1 and Fibronectin in Rat Mesangial Cells

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