Angiotensin II Enhances Glomerular Expression of a Nonmuscle Myosin Heavy Chain, SMemb, with Extracellular Matrix Accumulation

Nephron ◽  
2002 ◽  
Vol 90 (4) ◽  
pp. 477-483 ◽  
Author(s):  
Naobumi Mise ◽  
Kenjiro Kimura ◽  
Masahiko Kurabayashi ◽  
Ryozo Nagai ◽  
Toshihiro Okuda ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Angiotensin Ii ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Nonmuscle Myosin ◽  
Matrix Accumulation

B2 exon splicing of nonmuscle myosin heavy chain IIB is differently regulated in developing and adult rat brain

2000 ◽  
Vol 37 (4) ◽  
pp. 299-306 ◽  
Author(s):  
Taisuke Miyazaki ◽  
Masahiko Watanabe ◽  
Akihiko Yamagishi ◽  
Masayuki Takahashi
Keyword(s):  
Myosin Heavy Chain ◽  
Rat Brain ◽  
Heavy Chain ◽  
Nonmuscle Myosin ◽  
Adult Rat ◽  
Exon Splicing ◽  
Adult Rat Brain

Effects of triiodo-thyronine on angiotensin-induced cardiomyocyte hypertrophy: reversal of increased β-myosin heavy chain gene expression

2006 ◽  
Vol 84 (8-9) ◽  
pp. 935-941 ◽  
Author(s):  
Baohua Wang ◽  
Jingping Ouyang ◽  
Zhengyuan Xia
Keyword(s):  
Gene Expression ◽  
Angiotensin Ii ◽  
Thyroid Hormone ◽  
Cardiac Hypertrophy ◽  
Atpase Activity ◽  
Mrna Expression ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Ang Ii ◽  
Hypertrophic Growth

Thyroid hormone-induced cardiac hypertrophy is similar to that observed in physiological hypertrophy, which is associated with high cardiac contractility and increased α-myosin heavy chain (α-MHC, the high ATPase activity isoform) expression. In contrast, angiotensin II (Ang II) induces an increase in myocardial mass with a compromised contractility accompanied by a shift from α-MHC to the fetal isoform β-MHC (the low ATPase activity isoform), which is considered as a pathological hypertrophy and inevitably leads to the development of heart failure. The present study is designed to assess the effect of thyroid hormone on angiotensin II-induced hypertrophic growth of cardiomyocytes in vitro. Cardiomyocytes were prepared from hearts of neonatal Wistar rats. The effects of Ang II and 3,3′,5-triiodo-thyronine (T3) on incorporations of [3H]-thymine and [3H]-leucine, MHC isoform mRNA expression, PKC activity, and PKC isoform protein expression were studied. Ang II enhanced [3H]-leucine incorporation, β-MHC mRNA expression, PKC activity, and PKCε expression and inhibited α-MHC mRNA expression in cardiomyocytes. T3 treatment prevented Ang II-induced increases in PKC activity, PKCε, and β-MHC mRNA overexpression and favored α-MHC mRNA expression. Thyroid hormone appears to be able to reprogram gene expression in Ang II-induced cardiac hypertrophy, and a PKC signal pathway may be involved in such remodeling process.

In Situ Interleukin-6 Transcription in Embryonic Nonmuscle Myosin Heavy Chain Expressing Immature Mesenchyme Cells of Cardiac Myxoma

2000 ◽  
Vol 9 (1) ◽  
pp. 33-37 ◽  
Author(s):  
Jun-ichi Suzuki ◽  
Kei Takayama ◽  
Fujio Mitsui ◽  
Tetsuya Kono ◽  
Yoshikazu Yazaki ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Interleukin 6 ◽  
Cardiac Myxoma ◽  
Nonmuscle Myosin ◽  
Mesenchyme Cells

scholarly journals Many chronic lymphocytic leukemia antibodies recognize apoptotic cells with exposed nonmuscle myosin heavy chain IIA: implications for patient outcome and cell of origin

Blood ◽  
2010 ◽  
Vol 115 (19) ◽  
pp. 3907-3915 ◽  
Author(s):  
Charles C. Chu ◽  
Rosa Catera ◽  
Lu Zhang ◽  
Sebastien Didier ◽  
Briana M. Agagnina ◽  
...  
Keyword(s):  
Chronic Lymphocytic Leukemia ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Lymphocytic Leukemia ◽  
Apoptotic Cells ◽  
Nonmuscle Myosin ◽  
Cell Of Origin ◽  
Poor Clinical Outcome ◽  
Mutation Status ◽  
Poor Patient Survival

Abstract Many B-cell chronic lymphocytic leukemia (CLL) monoclonal antibodies (mAbs) can be grouped into subsets based on nearly identical stereotyped sequences. Subset 6 CLL mAbs recognize nonmuscle myosin heavy chain IIA (MYHIIA). Herein, we report that during apoptosis, MYHIIA becomes exposed on the cell surface of a subgroup of apoptotic cells, allowing subset 6 CLL mAbs to bind with it. Because other non–subset 6 CLL mAbs interact with apoptotic cells, 26 CLL mAbs, including 24 not belonging to subset 6, were tested for reactivity with MYHIIA-exposed apoptotic cells (MEACs). More than 60% of CLL mAbs bound MEACs well; most of these mAbs expressed unmutated IGHV (15 of 16) and belonged to a stereotyped subset (14 of 16). Binding to MEACs inversely correlated with the degree of IGHV mutation. Interestingly, high binding to MEACs significantly correlated with poor patient survival, suggesting that the basis of IGHV mutation status as a CLL prognostic factor reflects antigen binding. Finally, natural antibodies from human serum also reacted with MEACs. Taken together, our data indicate that a large proportion of CLL clones emerge from natural antibody-producing cells expressing immunoglobulins that recognize MEACs, and that this reactivity is associated with poor clinical outcome.

scholarly journals Function of the Neuron-specific Alternatively Spliced Isoforms of Nonmuscle Myosin II-B during Mouse Brain Development

2006 ◽  
Vol 17 (5) ◽  
pp. 2138-2149 ◽  
Author(s):  
Xuefei Ma ◽  
Sachiyo Kawamoto ◽  
Jorge Uribe ◽  
Robert S. Adelstein
Keyword(s):  
Amino Acids ◽  
Myosin Heavy Chain ◽  
Purkinje Cells ◽  
Heavy Chain ◽  
Myosin Ii ◽  
Nonmuscle Myosin ◽  
Binding Region ◽  
Alternatively Spliced ◽  
Cerebellar Purkinje Cells ◽  
Mouse Brain Development

We report that the alternatively spliced isoforms of nonmuscle myosin heavy chain II-B (NHMC II-B) play distinct roles during mouse brain development. The B1-inserted isoform of NMHC II-B, which contains an insert of 10 amino acids near the ATP-binding region (loop 1) of the myosin heavy chain, is involved in normal migration of facial neurons. In contrast, the B2-inserted isoform, which contains an insert of 21 amino acids near the actin-binding region (loop 2), is important for postnatal development of cerebellar Purkinje cells. Deletion of the B1 alternative exon, together with reduced expression of myosin II-B, results in abnormal migration and consequent protrusion of facial neurons into the fourth ventricle. This protrusion is associated with the development of hydrocephalus. Restoring the amount of myosin II-B expression to wild-type levels prevents these defects, showing the importance of total myosin activity in facial neuron migration. In contrast, deletion of the B2 alternative exon results in abnormal development of cerebellar Purkinje cells. Cells lacking the B2-inserted isoform show reduced numbers of dendritic spines and branches. Some of the B2-ablated Purkinje cells are misplaced in the cerebellar molecular layer. All of the B2-ablated mice demonstrated impaired motor coordination.

Sign in / Sign up

Export Citation Format

Share Document