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At least 19 recordsLinked to original sources
PubMed1984

Fiber types and myosin types in human atrial and ventricular myocardium. An anatomical description.

Hybridomas were prepared from mice immunized with myosin from the enlarged left ventricle of a 53-year-old female with an obstructive cardiomyopathy. The specificity of 15 monoclonal antibodies to myosin heavy chains was assessed by the reactivity of muscle extracts and of chymotryptic myosin fragments of different sizes with these antibodies, as determined by the immune replicate technique; some of the monoclonal antibodies cross-reacted only with the ventricular V3-type myosin from hypothyroid rats, whereas the other antibodies cross-reacted both with the latter and with the ventricular V1-type myosins from normal young rats. Immunological heterogeneity of the fibers from human atrial muscles and from human ventricular muscles was detected by some of the antimyosin antibodies by means of indirect immunofluorescence. Histochemical fiber heterogeneity was also detected by adenosine triphosphatase staining of the same tissues. Because of the close correspondence observed between the immunological and histochemical responses of atrial fibers, it has been postulated that at least two distinct types of myosin exist in the human atrium, each myosin form being histochemically related to either alpha- or beta-like ventricular myosin heavy chains. In contrast, there was no direct correspondence between the two experimental approaches in human ventricles, and it is postulated that at least three distinct types of myosin exist within the human ventricles, one V1-type myosin, presumably corresponding to the very rare fibers with an alkaline-stable adenosine triphosphatase activity, and two other V3-type myosins corresponding to immunologically different fibers, each having an alkaline-labile adenosine triphosphatase activity. Monoclonal antibodies that can distinguish among the different myosin variants were further used to provide the basis for an anatomical description of fiber types and myosin types within the human atrial and ventricular myocardium in the whole hearts of two young boys who died sudden violent deaths. Small zones of myosin variation were seen to be scattered, but probably not randomly distributed, within large areas of myocardium in which the cellular distribution of myosin was constant; the large areas had one myosin distribution specific for each cardiac cavity. No clear-cut conclusions can yet be made concerning the physiological role of the regional variations observed in the distribution of the different molecular forms of myosin.

Adenosine Triphosphatases↗
PubMed2002

Regulation of arterial tone by smooth muscle myosin type II.

The initiation of contractile force in arterial smooth muscle (SM) is believed to be regulated by the intracellular Ca2+ concentration and SM myosin type II phosphorylation. We tested the hypothesis that SM myosin type II operates as a molecular motor protein in electromechanical, but not in protein kinase C (PKC)-induced, contraction of small resistance-sized cerebral arteries. We utilized a SM type II myosin heavy chain (MHC) knockout mouse model and measured arterial wall Ca2+ concentration ([Ca2+](i)) and the diameter of pressurized cerebral arteries (30-100 microm) by means of digital fluorescence video imaging. Intravasal pressure elevation caused a graded [Ca2+](i) increase and constricted cerebral arteries of neonatal wild-type mice by 20-30%. In contrast, intravasal pressure elevation caused a graded increase of [Ca2+](i) without constriction in (-/-) MHC-deficient arteries. KCl (60 mM) induced a further [Ca2+](i) increase but failed to induce vasoconstriction of (-/-) MHC-deficient cerebral arteries. Activation of PKC by phorbol ester (phorbol 12-myristate 13-acetate, 100 nM) induced a strong, sustained constriction of (-/-) MHC-deficient cerebral arteries without changing [Ca2+](i). These results demonstrate a major role for SM type II myosin in the development of myogenic tone and Ca2+ -dependent constriction of resistance-sized cerebral arteries. In contrast, the sustained contractile response did not depend on myosin and intracellular Ca2+ but instead depended on PKC. We suggest that SM myosin type II operates as a molecular motor protein in the development of myogenic tone but not in pharmacomechanical coupling by PKC in cerebral arteries. Thus PKC-dependent phosphorylation of cytoskeletal proteins may be responsible for sustained contraction in vascular SM.

Animals↗
PubMed1980

Myosin types in human skeletal muscle fibers.

By combining enzyme histochemistry for fiber typing with immunohistochemistry for slow and fast myosin a correlation between fiber type and myosin type was sought in human skeletal muscle. Fiber typing was done by staining for myofibrillar ATPases after preincubation at discriminating pH values. Myosin types were discriminated using type specific anti-rabbit myosin antibodies shown to cross-react with human myosin and were visualized by a protein A-peroxidase method. Type I fibers were shown to contain slow myosin only, type IIA and IIB fibers fast myosin only, and type IIC fibers both myosins in various proportions. When muscle biopsies from well-trained athletes were investigated essentially the same staining pattern was observed. However, rarely occurring type I fibers with high glycolytic activity were detected containing additional small amounts of fast myosin and occasional type IIA fibers had small amounts of slow myosin. Based on the observation of various fiber types in which slow and fast myosin coexist we propose a dynamic continuum of fibers encompassing all fiber types.

Adenosine Triphosphatases↗
PubMed1986

Myosin types and fiber types in cardiac muscle. III. Nodal conduction tissue.

The sinoatrial (SA) and atrioventricular (AV) nodes are specialized centers of the heart conduction system and are composed of muscle cells with distinctive morphological and electrophysiological properties. We report here results of immunofluorescence and immunoperoxidase studies on the bovine heart showing that a large number of SA and AV nodal cells share a distinct type of myosin heavy chain (MHC) which is not found in other myocardial cells and can thus be used as a cell-type-specific marker. The antibody used in this study was raised against fetal skeletal myosin and reacted with fetal skeletal but not with adult skeletal MHCs. Both atrial and ventricular fibers, as well as fibers of the ventricular conduction tissue were unlabeled by this antibody. Specific reactivity was exclusively seen in most cells in the central portions of the SA and AV nodes and rare cells in perinodal areas. However, a number of nodal cells, particularly those located in the peripheral nodal regions, were unreactive with this antibody. The myosin composition of nodal tissues was also explored using two antibodies reacting specifically with alpha-MHC, the predominant atrial isoform, and beta-MHC, the predominant ventricular isoform. Most nodal cells were reactive for alpha-MHC and a number of them also for beta-MHC. Variation in reactivity with the two antibodies was also observed in perinodal areas: at these sites a population of large fibers reacted exclusively for beta-MHC. These findings point to the existence of muscle cell heterogeneity with respect to myosin composition both in nodal and perinodal tissues.

Animals↗
PubMed2003

Expression of non-muscle type myosin heavy polypeptide 9 (MYH9) in mammalian cells.

Myosin is a functional protein associated with cellular movement, cell division, muscle contraction and other functions. Members of the myosin super-family are distinguished from the myosin heavy chains that play crucial roles in cellular processes. Although there are many studies of myosin heavy chains in this family, there are fewer on non-muscle myosin heavy chains than of muscle myosin heavy chains. Myosin is classified as type I (myosin I) or type II (myosin II). Myosin I, called unconventional myosin or mini-myosin, has one head, while myosin II, called conventional myosin, has two heads. We transfected myosin heavy polypeptide 9 (MYH9) into HeLa cells as a fusion protein with enhanced green fluorescent protein (EGFP) and analyzed the localization and distribution of MYH9 in parallel with those of actin and tubulin. The results indicate that MYH9 colocalizes with actin stress fibers. Since it has recently been shown by genetic analysis that autosomal dominant giant platelet syndromes are MYH9-related disorders, our development of transfected EGFP-MYH9 might be useful for predicting the associations between the function of actin polymerization, the MYH9 motor domain, and these disorders.

Actins↗
PubMed1989

Is the myosin type altered in the aging platysma?

The myosin light chains of platysma samples originating from 2 to 86 year old patients of the maxillo-facial surgery clinic were investigated. The platysma contained both fast and slow myosin. No change in the proportion of myosin type in relation to age was found. Female patients often displayed less fast myosin than male patients. Each time when the platysma muscle activity has been reduced a decrease in the amount of slow myosin light chains was observed. In the reported study, variations of the fast and slow myosin light chains resulted mainly from the platysma activity level, i.e. from the pathology requiring the surgery, rather than from the patients' age.

Adolescent↗
PubMed1988

Heterogeneity of beta-type myosin isozymes in the human heart and regulational mechanisms in their expression. Immunohistochemical study using monoclonal antibodies.

To investigate the existence of heterogeneity of beta-type myosin isozymes (HC beta) in human hearts, immunohistochemical studies using monoclonal antibodies (MoAbs) raised against human ventricular myosin heavy chains were performed. Two types of MoAbs recognized some muscle fibers in the atrium, whereas both reacted with all ventricular muscle fibers. Since atrial muscle fibers reactive with each MoAb were found to be clearly different, the existence of two immunologically distinct HC beta (beta 1, and beta 2) was suggested in the atrium. By using affinity chromatography, two molecular variants of HC beta were isolated from the bovine atrium, and differences in the primary structure of beta 1 and beta 2 were confirmed by analysis of peptides produced by chymotryptic digestion. In pressure-overloaded human atria, myofibers containing beta 1 and/or beta 2 increased in accordance with decrement of myofibers containing alpha-type myosin isozyme (P less than 0.01). But they differed in expression during the developmental stage, since beta 2 did not exist in the early embryonic bovine heart, but beta 1 did. Thus, there are two distinct HC beta whose expression is regulated by at least two factors: pressure overload and developmental stage.

Adult↗
PubMed1998

Glomerular nonmuscle-type myosin heavy-chain isoform gene expression in glomerulosclerosis.

This study was designed to assess how the glomerular expression of the nonmuscle-type myosin heavy-chain isoform, SMemb, is regulated in rats with focal glomerulosclerosis induced by puromycin aminonucleoside. SMemb was barely detectable in control glomeruli. On day 48 of focal glomerulosclerosis, SMemb was expressed in mesangial area and glomerular epithelial cells. When glomerulosclerosis became prominent on day 80, SMemb stained immunohistochemically in a focal segmental pattern in the sclerotic glomeruli. SMemb-expressing cells did not always express alpha-smooth muscle actin. In Northern blot analysis, SMemb mRNA was not detected in control glomeruli, whereas it was transiently upregulated in glomeruli on day 48 in rats with focal glomerulosclerosis. The mRNA levels of SMemb were thereafter gradually downregulated by day 80; however, they remained higher than those of control glomeruli. These data suggest that glomerular embryonic nonmuscle-type myosin heavy chain is abnormally regulated in glomerulosclerosis and that glomerulosclerosis may be associated with dedifferentiation of not only the mesangial cells, but also the other resident glomerular cells.

Animals↗
PubMed1977

Myosin types during the development of embryonic chicken fast and slow muscles.

We have studied the myosin types present in developing fast and slow muscles of the chicken embryo. Myosin light chains were characterized by their mobility on sodium dodecyl sulfate/polyacrylamide gels; myosin heavy chains were identified by their reaction with antibodies specific for adult fast or adult slow myosin heavy chains. During development, the pectoralis muscle, a fast muscle in the adult, contains heavy chains and two of the three light chains characteristic of adult fast muscle myosin. However, the anterior latissimus dorsi muscle, a slow muscle in the adult, also contains fast myosin light and heavy chains during early development. Only after the time of innervation does this muscle begin synthesizing predominantly the slow myosin heavy and light chains. We hypothesize that the synthesis of fast myosin in both early fast and slow muscles is the result of the endogenous program for muscle development; initiation of the synthesis of slow myosin, however, is dependent upon exogenous factors.

Aging↗
PubMed1978

The influence of aging on the myosin type of the rabbit soleus and longissimus dorsi muscles.

The influence of aging on the myosin type, and on the fibre composition of both the slowly contracting ("red") M. soleus and the fast ("white") M. longissimus dorsi was examined in the rabbit. For myosin characterization isolated myofibrils were electrophoresed on SDS-polyacrylamide gels, and the fibre pattern within the respective muscles was analyzed with an immunocytochemical method. Antisera against either fast or slow rabbit myosin were collected from guinea pigs after longterm immunization. After incubation of the paraformaldehyde-fixed muscle thin sections the fibres containing either fast or slow myosin could be distinguished from each other by indirect immunofluorescence. The soleus muscles of 1 day old rabbits were composed of 25% slow and 75% fast fibres. In young-adult (5--8 mo.) rabbits the fibres were mostly slow (over 90%), while in old age (4--7 y.) again up to 50% of the soleus fibres contained fast myosin. In contrast, in the longissimus dorsi muscle constantly around 95% of the fibres contained fast myosin. In accordance with the immunocytochemical finding of an increase of fast fibres in the aging soleus muscle, the presence of fast myosin could also be demonstrated electrophoretically. With this method, soleus myofibrils from young-adult animals were observed to contain virtually slow myosin only. No slow, but only fast myosin was identified in SDS-gels of longissimus dorsi myofibrils at all ages. These results are discussed in relation to the well known metabolic alterations occurring in the mammalian skeletal muscle during aging.

Aging↗
PubMed1994

Characterization of human oro-facial and masticatory muscles with respect to fibre types, myosins and capillaries. Morphological, enzyme-histochemical, immuno-histochemical and biochemical investigations.

This study provides a comparative characterization of four human oro-facial muscles, one masticatory muscle (the masseter) and two limb muscles, with respect to muscle fibre types, myosin isoforms and capillary supply. Enzyme-histochemical methods were used to evaluate the myofibrillar ATPase fibre type composition. Immuno-histochemical techniques were used to determine the expression of myosin heavy chain (MHC) isoforms in the different fibre types. The contents of MHCs and myosin light chains (MLC) in different muscles were analysed with electrophoretic methods. In addition, the capillary bed of the muscles was evaluated using both enzyme- and immuno-histochemical techniques. The fibre type compositions of the oro-facial and masseter muscles were found to be qualitatively and quantitatively different from each other and from those of limb muscles. In general, the oro-facial muscles contained a predominance of unusually high oxidative type II fibres, with a staining reaction for ATPase in between that of type IIA and type IIB fibres, termed type IIAB. In fact, one of the oro-facial muscles, the zygomatic minor, showed the highest type II fibre proportion ever reported in humans. This fibre type pattern is in contrast to that of the masseter muscle, which contains a majority of type I fibres, small diameter low oxidative type IIB fibres and a significant proportion of ATPase-intermediately stained fibres, termed IM, and IIC. Inter- and intra-muscular variability in fibre size and shape was considerable in both the oro-facial and masseter muscles. The oro-facial muscles were devoid of muscle spindles. The immuno-histochemical and biochemical analyses showed a characteristic myosin composition of each muscle. Notably, the results indicated the presence of a previously undetected fast MHC isoform in the oro-facial muscles, tentatively termed "fast F". The masseter contained unusual myosin isoforms, such as fetal and alpha-cardiac MHCs, and unique combinations of MHC isoforms which were not found in the limb or oro-facial muscles. The type IM and IIC fibres co-expressed slow and fast A MHCs in the oro-facial and limb muscles, but slow and a "fast B like" MHC in the masseter. Individual fibres in the oro-facial and limb muscles contained one or two MHC isoforms, whereas individual fibres in the masseter co-expressed up to four different MHC isoforms. On the basis of their pattern of expression of MHC isoforms, up to five fibre types could be distinguished in the oro-facial and limb muscles and eight in the masseter.(ABSTRACT TRUNCATED AT 400 WORDS)

Adenosine Triphosphatases↗
PubMed2005

The MYO1F, unconventional myosin type 1F, gene is fused to MLL in infant acute monocytic leukemia with a complex translocation involving chromosomes 7, 11, 19 and 22.

We analysed a complex translocation involving chromosomes 7, 11, 19 and 22 in infant acute monocytic leukemia, and identified that the MLL gene on 11q23 was fused to the unconventional myosin type 1F, MYO1F, gene on 19p13.2-13.3. MYO1F consists of at least 28 exons and was predicted to encode a 1098-amino-acid with an N-terminal head domain containing both ATP-binding and actin-binding sequences, a neck domain with a single IQ motif, and a tail with TH1, TH2 and SH3 domains. Northern blot analysis of RNAs prepared from multiple tissues showed that the expression of approximately 4-kb transcripts appeared constant in most tissues examined. However, MYO1F was expressed in only three of 22 leukemic cell lines. The MLL-MYO1F fusion protein contains almost the entire MYO1F, however, C-terminal MYO1F has neither the transactivation domain nor the dimerization domain found in various MLL fusion partners. Further analysis of this novel type of MLL fusion protein would provide new insights into leukemogenesis. MYO1F is the fourth partner gene of MLL on 19p13. At the cytogenetic level, it may be difficult to distinguish MLL-ENL, MLL-ELL, MLL-EEN and MLL-MYO1F fusions created by t(11;19)(q23;p13), and it is likely that cases of t(11;19) lacking a known fusion gene may result in this gene fusion.

Amino Acid Sequence↗
PubMed1994

Transformation of Drosophila melanogaster with the wild-type myosin heavy-chain gene: rescue of mutant phenotypes and analysis of defects caused by overexpression.

We have transformed Drosophila melanogaster with a genomic construct containing the entire wild-type myosin heavy-chain gene, Mhc, together with approximately 9 kb of flanking DNA on each side. Three independent lines stably express myosin heavy-chain protein (MHC) at approximately wild-type levels. The MHC produced is functional since it rescues the mutant phenotypes of a number of different Mhc alleles: the amorphic allele Mhc1, the indirect flight muscle and jump muscle-specific amorphic allele Mhc10, and the hypomorphic allele Mhc2. We show that the Mhc2 mutation is due to the insertion of a transposable element in an intron of Mhc. Since a reduction in MHC in the indirect flight muscles alters the myosin/actin protein ratio and results in myofibrillar defects, we determined the effects of an increase in the effective copy number of Mhc. The presence of four copies of Mhc results in overabundance of the protein and a flightless phenotype. Electron microscopy reveals concomitant defects in the indirect flight muscles, with excess thick filaments at the periphery of the myofibrils. Further increases in copy number are lethal. These results demonstrate the usefulness and potential of the transgenic system to study myosin function in Drosophila. They also show that overexpression of wild-type protein in muscle may disrupt the function of not only the indirect flight but also other muscles of the organism.

Alleles↗
PubMed1997

Oestrogen-dependent expression of the SM2 smooth muscle-type myosin isoform in rabbit myometrium.

Ovarectomized rabbits displayed a decreased SM1 to SM2 ratio of smooth muscle-type myosin heavy chain isoforms compared to unoperated, virgin females which was reversed after 17beta-oestradiol administration to a value similar to that of control animals. When this steroid was given to sexually immature animals or to adult virgin rabbits, SM2 expression was not induced, as also happened with proliferating myometrial smooth muscle cells grown in vitro. In growing rabbit, the 17beta-oestradiol administration induced the formation of the circular and the longitudinal muscle layers, characteristics of sexually competent females. The SM2 isoform was up-regulated during postnatal development and the SM1 to SM2 ratio changed during pregnancy and post-partum period but not with human gonadotropin treatment which increases the level of circulating progesterone. Immunofluorescence staining of adult myometrium with anti-SM2 antibody indicated that this isoform is localized to the longitudinal layer exclusively and, in contrast to the circular layer, its expression was independent of oestrogen level. Difference in oestrogen sensitivity between the two layers was also detected for the expression of the intermediate filament protein vimentin and the thin filament protein calponin. Changes of SM2 expression in the myometrium correlated with variations in the oestrogen receptor density as also confirmed by decreased SM2 content/oestrogen receptor density in the circular layer when ovarectomized females were treated with the oestrogen antagonist ICI 182,780. Our results indicate that: (1) a specific distribution of myosin heavy chain exists within rabbit myometrium, and (2) SM2 myosin expression in this smooth muscle is under oestrogen control.

Animals↗
PubMed1996

Effect of a low-protein diet on expression of non-muscle type myosin heavy-chain isoforms in glomeruli of rats with puromycin aminonucleoside nephrosis.

BACKGROUND: We reported that an embryonic type of non-muscle-type myosin heavy-chain isoform (SMemb) may be a molecular marker for phenotypic alteration in initial glomerular injury and that methyl-prednisolone has no effect on SMemb expression in glomeruli of rats with puromycin aminonucleoside (PAN) nephrosis. The present study was designed to assess whether SMemb mRNA and protein expression in glomeruli are affected by a low-protein diet in rats with PAN-induced nephrosis and in control rats. METHODS: Rats were divided into four groups: group 1, PAN-injected rats fed a standard diet containing 22% protein; group 2, PAN-injected rats fed a low-protein diet containing 6% protein, starting on the day of PAN injection; group 3, control rats fed a standard diet; group 4, control rats fed a low-protein diet for the same period. We prepared glomerular RNA and performed Northern blot analysis and immunohistochemistry in all groups. RESULTS: Glomerular SMemb mRNA increased on days 2 and 4 (prior to and soon after the onset of proteinuria), but declined on day 8 (the peak of proteinuria). Myosin heavy-chain protein expression was evaluated immunohistochemically by use of three antibodies against SM1, SM2, and SMemb. SM1 and SM2 were absent from the glomeruli of rats with PAN nephrosis until day 20. The SMemb isoform was barely detectable in normal glomeruli, but substantial amounts of SMemb were demonstrated in the glomeruli of rats with PAN nephrosis. In the latter condition, the number of SMemb-positive glomerular epithelial cells increased on days 3 and 4, then decreased in subsequent days. Moreover, some mesangial cells became SMemb-positive transiently, returning to barely detectable levels on day 20. In addition, alpha-smooth-muscle actin, type I and III collagens were absent from the glomeruli of rats with PAN nephrosis until day 20. Urinary protein excretion was markedly suppressed by the 6% protein diet in PAN nephrosis. The low-protein diet reduced the increased mRNA expression of SMemb as well as the increased number of SMemb-positive cells in the glomeruli of rats with PAN nephrosis. However, the low-protein diet did not affect SMemb mRNA and protein levels in the glomeruli of control rats. CONCLUSIONS: In rats with PAN nephrosis, findings suggest that restriction of dietary protein leads to a reduction in glomerular SMemb expression.

Animals↗
PubMed1999

Size and charge requirements for kinetic modulation and actin binding by alkali 1-type myosin essential light chains.

The alkali 1-type isoforms of myosin essential light chains from vertebrate striated muscles have an additional 40 or so amino acids at their N terminus compared with the alkali 2-type. Consequently two light chain isoenzymes of myosin subfragment-1 can be isolated. Using synthesized peptide mimics of the N-terminal region of alkali 1-type essential light chains, we have found by 1H NMR that the major actin binding region occurred in the N-terminal four residues, APKK. These results were confirmed by mutating this region of the human atrial essential light chain, resulting in altered actin-activated MgATPase kinetics when the recombinant light chains were hybridized into rabbit skeletal subfragment 1. Substitution of either Lys3 or Lys4 with Ala resulted in increased Km and kcat and decreased actin binding (as judged by chemical cross-linking). Replacement of Lys4 with Asp reduced actin binding and increased Km and kcat still further. Alteration of Ala1 to Val did not alter the kinetic parameters of the hybrid subfragment 1 or the essential light chain's ability to bind actin. Furthermore, we found a significant correlation between the apparent Km for actin and the kcat for MgATP turnover for each mutant hybrid, strengthening our belief that the binding of actin by alkali 1-type essential light chains results directly in modulation of the myosin motor.

Actins↗
PubMed1996

Smooth muscle-type myosin heavy chain isoforms in bovine smooth muscle and non-muscle tissues.

The distribution of smooth muscle (SM)-type myosin heavy chain isoforms in several bovine muscular and non-muscular (NM) tissues was evaluated by immunofluorescence tests using monoclonal antibodies SM-E7, reactive with 204 (SM1) and 200 (SM2) kDa isoforms, and SM-F11, specific for SM2 isoform. SM-E7 reacted equally with vascular, respiratory and intestinal SM tissues, whereas SM-F11 stained heterogeneously SM cells in the various muscular systems examined and in some peculiar tissues was unreactive (perisinusoidal cells of hepatic lobule, pulmonary interstitial cells and intestinal muscularis mucosae) or uniquely reactive (nerve cells). On the whole, our findings indicate that SM1 and SM2 isoforms are unequally distributed at the cellular level in various SM and NM tissues and support previous results obtained with tissue extracts and electrophoretic procedures.

Animals↗
PubMed1997

The rôle of the proline-rich region in A1-type myosin essential light chains: implications for information transmission in the actomyosin complex.

The proline-rich region of A1-type myosin essential light chains functions as a spacer arm separating an actin binding site at the extreme N-terminus from the remainder of the protein. Alteration of the length of this region leaving the actin binding site intact results in altered actin-activated MgATPase kinetics when these light chains are hybridised into myosin subfragment-1. In the case of a mutant in which the length of the proline-rich region was doubled, actin binding by the light chain was uncoupled from kinetic modulation. The implications of this result for information transmission in the actomyosin complex are discussed.

Actins↗