Podocyte expression of nonmuscle myosin heavy chain-IIA decreases in idiopathic nephrotic syndrome, especially in focal segmental glomerulosclerosis

Miura, Kenichiro; Kurihara, Hidetake; Horita, Shigeru; Chikamoto, Hiroko; Hattori, Motoshi; Harita, Yutaka; Tsurumi, Haruko; Kajiho, Yuko; Sawada, Yoko; Sasaki, Satoshi; Igarashi, Takashi; Kunishima, Shinji; Sekine, Takashi

doi:10.1093/ndt/gft350

Cited by 20 publications

(15 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our data are consistent with 2 recent reports indicating that myosin IIA might be in the major processes but not in the foot processes (18,19). This suggests a system in which the contractile forces distal to the capillary wall generate tension by pulling the noncontractile actin fibers anchored to adhesion complexes at the GBM and to the slit diaphragms that link adjacent foot processes.…”

Section: Discussionsupporting

confidence: 93%

See 1 more Smart Citation

Injury-induced actin cytoskeleton reorganization in podocytes revealed by super-resolution microscopy

et al. 2017

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 93%

“…The interaction between actin fibers and myosin motor proteins plays a critical role in generating mechanical stress, allowing for distinct cell shapes. Exactly how the actomyosin network is organized in podocytes is not known (17)(18)(19).…”

Section: Introductionmentioning

confidence: 99%

Injury-induced actin cytoskeleton reorganization in podocytes revealed by super-resolution microscopy

et al. 2017

View full text Add to dashboard Cite

“…; Miura et al. ), we are unaware of any studies that have undertaken the task of colocalizing each of the NM2 isoforms with renal tubule‐specific markers. In this study, we utilized unique markers that are expressed within specific segments of the adult mouse renal tubules (megalin: proximal tubule; uromodulin: loop of Henle; calbindin D‐28K: distal tubule; aquaporin 2: collecting duct) and determined the expression and localization profile of NM2 isoforms.…”

Section: Discussionmentioning

confidence: 99%

“…; Miura et al. ). Several groups have used murine models of Myh9 deletion in the glomerulus to uncover the mechanism of kidney disease in patients with MYH9 ‐related disorders; however, these models have failed to provide clear evidence of disease development (Johnstone et al.…”

Section: Introductionmentioning

confidence: 96%

Nonmuscle myosin 2 proteins encoded by Myh9 , Myh10 , and Myh14 are uniquely distributed in the tubular segments of murine kidney

et al. 2017

View full text Add to dashboard Cite

The diverse epithelial cell types of the kidneys are segregated into nephron segments and the collecting ducts in order to endow each tubular segment with unique functions. The rich diversity of the epithelial cell types is highlighted by the unique membrane channels and receptors expressed within each nephron segment. Our previous work identified a critical role for Myh9 and Myh10 in mammalian endocytosis. Here, we examined the expression patterns of Nonmuscle myosin 2 (NM2) heavy chains encoded by Myh9, Myh10, and Myh14 in mouse kidneys as these genes may confer unique nephron segment‐specific membrane transport properties. Interestingly, we found that each segment of the renal tubules predominately expressed only two of the three NM2 isoforms, with isoform‐specific subcellular localization, and different levels of expression within a nephron segment. Additionally, we identify Myh14 to be restricted to the intercalated cells and Myh10 to be restricted to the principal cells within the collecting ducts and connecting segments. We speculate that the distinct expression pattern of the NM2 proteins likely reflects the diversity of the intracellular trafficking machinery present within the different renal tubular epithelial segments.

show abstract

“…However, NMIIA directs convergence and extension tissue movements during the development of the kidney tubules ( Lienkamp et al, 2012 ), accounting for nephropathy in some MYH9-RD cases, characterized by altered NMIIA localization in renal structures and reduced NMIIA expression in podocytes ( Ghiggeri et al, 2003 ). Altered NMII expression has been reported for several glomerular diseases ( Hiroi et al, 1996 ; Miura et al, 2013 ). In addition to regulating tissue patterning, PCP-mediated NMII activity might also contribute to cancer progression, with more aggressive ovarian cancers showing increased PCP signaling pathways corresponding with changes in actomyosin organization ( Feske et al, 2009 ).…”

Section: Nmii In Other Diseasesmentioning

confidence: 98%

Non-muscle myosin II in disease: mechanisms and therapeutic opportunities

Litwa

Horwitz

Lamers

2015

Disease Models &Amp; Mechanisms

123

115

View full text Add to dashboard Cite

The actin motor protein non-muscle myosin II (NMII) acts as a master regulator of cell morphology, with a role in several essential cellular processes, including cell migration and post-synaptic dendritic spine plasticity in neurons. NMII also generates forces that alter biochemical signaling, by driving changes in interactions between actin-associated proteins that can ultimately regulate gene transcription. In addition to its roles in normal cellular physiology, NMII has recently emerged as a critical regulator of diverse, genetically complex diseases, including neuronal disorders, cancers and vascular disease. In the context of these disorders, NMII regulatory pathways can be directly mutated or indirectly altered by disease-causing mutations. NMII regulatory pathway genes are also increasingly found in disease-associated copy-number variants, particularly in neuronal disorders such as autism and schizophrenia. Furthermore, manipulation of NMII-mediated contractility regulates stem cell pluripotency and differentiation, thus highlighting the key role of NMII-based pharmaceuticals in the clinical success of stem cell therapies. In this Review, we discuss the emerging role of NMII activity and its regulation by kinases and microRNAs in the pathogenesis and prognosis of a diverse range of diseases, including neuronal disorders, cancer and vascular disease. We also address promising clinical applications and limitations of NMII-based inhibitors in the treatment of these diseases and the development of stem-cell-based therapies.

show abstract

Podocyte expression of nonmuscle myosin heavy chain-IIA decreases in idiopathic nephrotic syndrome, especially in focal segmental glomerulosclerosis

Cited by 20 publications

References 41 publications

Injury-induced actin cytoskeleton reorganization in podocytes revealed by super-resolution microscopy

Injury-induced actin cytoskeleton reorganization in podocytes revealed by super-resolution microscopy

Nonmuscle myosin 2 proteins encoded by Myh9 , Myh10 , and Myh14 are uniquely distributed in the tubular segments of murine kidney

Non-muscle myosin II in disease: mechanisms and therapeutic opportunities

Contact Info

Product

Resources

About