Correlation between the clinical phenotype of MYH9 -related disease and tissue distribution of class II nonmuscle myosin heavy chains

Marigo, Valeria; Nigro, Alessandra; Pecci, Alessandro; Montanaro, Donatella; Stazio, Mariateresa Di; Balduini, Carlo L.; Savoia, Anna

doi:10.1016/j.ygeno.2003.12.012

Cited by 70 publications

(62 citation statements)

References 32 publications

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“…Although degradation of the cardiac jelly by hyaluronidase allows looping to continue in the rat and chick models (Baldwin and Solursh, 1989;Linask et al, 2003b), this enzyme exposure would be expected to break down proteoglycans, but would not be expected to degrade integrin-glycoprotein interactions within the myocardial basal lamina that becomes closely apposed to the endocardium in these experimentally treated embryos. The association of NMHC-II proteins with mechanotransduction is seen in other systems, as for example, in relation to cilia in the inner ear for transmission of sound waves and in relation to afferent and efferent arterioles in the kidney in detection of blood flow pressure (Shiraishi et al, 2003;Marigo et al, 2004). Recently, with regard to mesenchymal stem cells the nonmuscle myosins are shown to .5 hearts of Nodal ϩ/ϩ and Nodal ⌬600/⌬600 embryos.…”

Section: Nonmuscle Myosin II Proteins and Heart Loopingmentioning

confidence: 99%

Cellular nonmuscle myosins NMHC‐IIA and NMHC‐IIB and vertebrate heart looping

Lu¹,

Seeholzer²,

Han³

et al. 2008

Developmental Dynamics

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Flectin, a protein previously described to be expressed in a left-dominant manner in the embryonic chick heart during looping, is a member of the nonmuscle myosin II (NMHC-II) protein class. During looping, both NMHC-IIA and NMHC-IIB are expressed in the mouse heart on embryonic day 9.5. The patterns of localization of NMHC-IIB, rather than NMHC-IIA in the mouse looping heart and in neural crest cells, are equivalent to what we reported previously for flectin. Expression of full-length human NMHC-IIA and -IIB in 10 T1/2 cells demonstrated that flectin antibody recognizes both isoforms. Electron microscopy revealed that flectin antibody localizes in short cardiomyocyte cell processes extending from the basal layer of the cardiomyocytes into the cardiac jelly. Flectin antibody also recognizes stress fibrils in the cardiac jelly in the mouse and chick heart; while NMHC-IIB antibody does not. Abnormally looping hearts of the Nodal ⌬ 600 homozygous mouse embryos show decreased NMHC-IIB expression on both the mRNA and protein levels. These results document the characterization of flectin and extend the importance of NMHC-II and the cytoskeletal actomyosin complex to the mammalian heart and cardiac looping. Developmental Dynamics 237:3577-3590, 2008.

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Section: Nonmuscle Myosin II Proteins and Heart Loopingmentioning

confidence: 99%

Cellular nonmuscle myosins NMHC‐IIA and NMHC‐IIB and vertebrate heart looping

Lu¹,

Seeholzer²,

Han³

et al. 2008

Developmental Dynamics

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“…MYH9 mutations are related to four autosomal dominant disorders characterized by platelet formation defects (Even-Ram and Yamada, 2007;Kunishima and Saito, 2010). NMHC IIA, but not IIB or IIC could be detected in megakaryocytes and platelets (Marigo et al, 2004;Maupin et al, 1994) where NMHC IIA is crucial for organelle distribution (Pertuy et al, 2014). Enucleation of erythroid cells is promoted by actinomyosin ring contraction between the incipient reticulocyte and the nucleus that is induced by Rac-GTPase-dependent myosin regulatory light chain phosphorylation (Ji et al, 2008;Konstantinidis et al, 2012;Koury et al, 1989).…”

Section: Differential Hnrnp-k−rna Binding In Erythroid Maturationmentioning

confidence: 99%

Translational control mediated by hnRNP K links NMHC IIA to erythroid enucleation

Vries

Brendle

Bähr-Ivacevic

et al. 2016

Journal of Cell Science

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Post-transcriptional regulation is crucial for structural and functional alterations in erythropoiesis. Enucleation of erythroid progenitors precedes reticulocyte release into circulation. In enucleated cells, reticulocyte 15-lipoxygenase (r15-LOX, also known as ALOX15) initiates mitochondria degradation. Regulation of r15-LOX mRNA translation by hnRNP K determines timely r15-LOX synthesis in terminal maturation. K562 cells induced for erythroid maturation recapitulate enucleation and mitochondria degradation. HnRNP K depletion from maturing K562 cells results in enhanced enucleation, which even occurs independently of maturation. We performed RIP-Chip analysis to identify hnRNP K-interacting RNAs comprehensively. Non-muscle myosin heavy chain (NMHC) IIA (also known as MYH9) mRNA co-purified with hnRNP K from noninduced K562 cells, but not from mature cells. NMHC IIA protein increase in erythroid maturation at constant NMHC IIA mRNA levels indicates post-transcriptional regulation. We demonstrate that binding of hnRNP K KH domain 3 to a specific sequence element in the NMHC IIA mRNA 3′UTR mediates translation regulation in vitro. Importantly, elevated NMHC IIA expression results in erythroidmaturation-independent enucleation as shown for hnRNP K depletion. Our data provide evidence that hnRNP-K-mediated regulation of NMHC IIA mRNA translation contributes to the control of enucleation in erythropoiesis.

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“…5 It should therefore be noted that while elevated transaminases were present even in our youngest patients, no evolution toward liver insufficiency has been identified. Given the expanding appreciation of MYH9 function in different cell types, 6 it may therefore be of interest to examine the role of MYH9 genetic variation in individuals with abnormal liver-enzyme results but without other known etiologies. Table 1 …”

Section: A New Feature Of the Myh9-related Syndrome: Chronic Transamimentioning

confidence: 99%