Early diagnosis of cardiac rejection by in situ detection of nonmuscle myosin heavy chain transcription

SUMMARY The axial muscle of most teleost species consists of a deep bulk of fast-contracting white fibres and a superficial strip of slow-contracting red fibres. To investigate the embryological development of fast and slow muscle in trout embryos, we carried out single and double in situ hybridisation with fast and slow myosin heavy chain (MyHC)-isoform-specific riboprobes. This showed that the slow-MyHC-positive cells originate in a region of the somite close to the notochord. As the somite matures in a rostrocaudal progression, the slow-MyHC-positive cells appear to migrate radially away from the notochord to the lateral surface of the myotome, where they form the superficial strip of slow muscle. Surprisingly, the expression pattern of the fast MyHC showed that the differentiation of fast muscle commences in the medial domain of the somite before the differentiation and migration of the slow muscle precursors. Later, as the differentiation of fast muscle progressively spreads from the inside to the outside of the myotome, slow-MyHC-expressing cells become visible medially. Our observations that the initial differentiation of fast muscle takes place in proximity to axial structures and occurs before the differentiation and migration of slow muscle progenitors are not in accord with the pattern of muscle formation in teleosts previously described in the zebrafish Danio rerio, which is often used as the model organism in fishes.

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

Nephrology Dialysis Transplantation ◽

10.1093/ndt/gft350 ◽

2013 ◽

Vol 28 (12) ◽

pp. 2993-3003 ◽

Cited By ~ 12

Author(s):

Kenichiro Miura ◽

Hidetake Kurihara ◽

Shigeru Horita ◽

Hiroko Chikamoto ◽

Motoshi Hattori ◽

...

Keyword(s):

Nephrotic Syndrome ◽

Myosin Heavy Chain ◽

Focal Segmental Glomerulosclerosis ◽

Heavy Chain ◽

Idiopathic Nephrotic Syndrome ◽

Nonmuscle Myosin ◽

Segmental Glomerulosclerosis

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

Neuroscience Research ◽

10.1016/s0168-0102(00)00130-9 ◽

2000 ◽

Vol 37 (4) ◽

pp. 299-306 ◽

Cited By ~ 14

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

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Neuronal Cell Expression of Inserted Isoforms of Vertebrate Nonmuscle Myosin Heavy Chain II-B

Journal of Biological Chemistry ◽

10.1074/jbc.270.24.14533 ◽

1995 ◽

Vol 270 (24) ◽

pp. 14533-14540 ◽

Cited By ~ 56

Author(s):

Kazuyuki Itoh ◽

Robert S. Adelstein

Keyword(s):

Myosin Heavy Chain ◽

Heavy Chain ◽

Neuronal Cell ◽

Nonmuscle Myosin ◽

Cell Expression

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Kinetic microphotometric evaluation of in situ hybridization for mRNA of slow myosin heavy chain in type I and C fibres of rabbit muscle

Histochemistry ◽

10.1007/bf00269014 ◽

1994 ◽

Vol 102 (2) ◽

pp. 105-112 ◽

Cited By ~ 5

Author(s):

T. Leeuw ◽

D. Pette

Keyword(s):

In Situ Hybridization ◽

Myosin Heavy Chain ◽

Heavy Chain ◽

Type I ◽

Rabbit Muscle ◽

Slow Myosin ◽

Slow Myosin Heavy Chain

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

Blood ◽

10.1182/blood-2009-09-244251 ◽

2010 ◽

Vol 115 (19) ◽

pp. 3907-3915 ◽

Cited By ~ 117

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.

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

Molecular Biology of the Cell ◽

10.1091/mbc.e05-10-0997 ◽

2006 ◽

Vol 17 (5) ◽

pp. 2138-2149 ◽

Cited By ~ 33

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.

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