Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.27.1 (RNase)
16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To examine how nascent myosin heavy chains associate with the cytoskeletons of developing muscle cells, we used pulse labeling, cell fractionation, and immunoprecipitation. More than 80% of nascent myosin heavy chains associate with the cytoskeleton. More than one-third of these nascent chains are not released by puromycin and/or RNase. The fraction of nascent heavy chains that resists release increases during development of muscle cells in culture. Treatment with cytochalasin D but not nocodazole decreases myosin heavy chain cotranslational assembly. These results indicate that (i) cotranslational assembly of myosin heavy chains is developmentally regulated, (ii) structures containing actin and not microtubules may mediate initial association of the heavy chains with the cytoskeleton, and (iii) the site of translation dictates where a significant fraction of the heavy chains will be inserted into the cytoskeleton.
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PMID:Cotranslational assembly of myosin heavy chain in developing cultured skeletal muscle. 347 39

The first results are reported with a magnetic suspension instrument for determination of the viscosity and density concurrently on small volumes (0.2 ml) of protein solution. Reasonable agreement was obtained with literature values for the intrinsic viscosities and specific volumes (partial or isopotential) of serum albumin and ribonuclease in native solvents, and in 6 M guanidinium chloride with or without 2-mercaptoethanol. Turnip Yellow Mosaic virus and myosin were also studied, the results with the virus being related to hydration and structure data and those with myosin to the dissociative character of the protein. The possibility of using this approach to follow the time course of viscosity and density changes during reactions is shown.
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PMID:Simultaneous determination of viscosity and density of protein solutions by magnetic suspension. 450 95

When the nuclear matrix from bovine lymphocytes was digested by RNase-depleted trypsin, the bulk of the matrix proteins, except actin, were hydrolyzed. The digestion left rapidly sedimented spherical structures (trypsin-treated nuclear matrix), which mainly were composed of actin (Nakayasu, H. and K. Ueda. Exp. Cell Res. 143, 55-62, 1983). Almost all the small nuclear RNAs of the original nuclear matrix remained associated with these actin spheres after trypsin digestion. By sonication, the small nuclear RNPs (snRNPs) in both untreated and trypsin-treated nuclear matrices were solubilized in association with proteinous filaments of various size. The sedimentation pattern of these snRNP complexes was not changed by the digestion of the bulk of the proteins. The snRNP complex was adsorbed on rabbit muscle myosin-Sepharose then eluted by the addition of 5 mM ATP. We concluded that snRNPs are associated with actin filaments in the nuclear matrix of bovine lymphocytes.
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PMID:Small nuclear RNA-protein complex anchors on the actin filaments in bovine lymphocyte nuclear matrix. 624 3

Mammalian heart has been reported to express AC isozymes (types V and VI) that are inhibited by < microM [Ca2+]; avian heart has been reported to express adenylyl cyclase activity that is inhibited by < microM [Ca2]. We have used reverse transcription polymerase chain reaction (RT-PCR) to determine that type V and VI AC mRNAs are present in freshly isolated ventricular myocytes. Subsequent RNase protection assays revealed that that the type V signal is 4-5 times that for the type VI isozyme. In situ hybridization with high specific activity cRNA probes combined with immunocytochemistry with a chick anti-myosin antibody was used to probe the cellular origins of type V and type VI AC signals. These studies show that myocytes contain messages for both the type V and VI isozymes but that AC V is the major isoform. Interestingly, while the type V AC mRNA appears to be localized primarily, if not exclusively, in myocytes, the signal for type AC VI mRNA in non-myocytes is stronger than in myocytes.
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PMID:Determination and cellular localization of adenylyl cyclase isozymes expressed in embryonic chick heart. 758 20

Immune interactions in the heart were studied using a murine model of myosin-induced autoimmune myocarditis. A T cell hybridoma specific for mouse cardiac myosin was generated from A/J mice and used to demonstrate that endogenous myosin/I-Ak complexes are constitutively expressed on antigen-presenting cells in the heart. This T cell hybridoma, Seu.5, was used as a functional probe to identify a myocarditis-inducing epitope of cardiac myosin. Overlapping peptides based on the cardiac myosin heavy chain alpha (myhc alpha) sequences were synthesized and tested for their ability to stimulate Seu.5 T cells. One peptide, myhc alpha (325-357) strongly stimulated the Seu.5 T cells, localizing the epitope to this region of the myhc alpha molecule. Using truncated peptides, the epitope was further localized to residues 334-352. The myhc alpha (334-352) peptide strongly induced myocarditis when administered to A/J mice, which was histologically indistinguishable from that induced by myosin. The myhc alpha (334-352) epitope was present in cardiac myosin and not skeletal muscle myosins, providing a biochemical basis for the cardiac specificity of this autoimmune disease. Induction of myocarditis by this epitope was restricted to the myhc alpha isoform and not the myhc beta isoform, suggesting there may be a difference in the efficiency of generating tolerance to these isoforms of cardiac myosin, which are differentially developmentally regulated. The myhc alpha (334-352) epitope bound to purified I-Ak molecules in a similar manner to other I-Ak-restricted immunogenic epitopes, HEL(48-61) and RNase(43-56). Importantly, the myhc alpha (334-352) epitope was able to bind to I-Ak molecules on the surface of antigen-presenting cells in a stable manner. These findings demonstrate that autoantigenic epitopes can behave in a dominant manner and constitutively bind to class II molecules in the target organ in a similar manner to foreign immunogenic epitopes.
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PMID:Myocarditis-inducing epitope of myosin binds constitutively and stably to I-Ak on antigen-presenting cells in the heart. 759

Hypertrophic cardiomyopathy (HCM) is defined as an idiopathic heart muscle disorder which characterised by the presence of left and/or right ventricular hypertrophy in the absence of a systemic or cardiac cause. At post mortem examination the characteristic histology shows myocyte disarray surrounding areas of increased loose connective tissue. The spectrum of disease is wider than the phenotype which relies on the diagnostic presence of unexplained left ventricular hypertrophy. During the past 5 years, one of the genes which causes HCM has been discovered, several additional loci have been identified, disease causing mutations are being introduced into transgenic animals and functional studies of disease muscle have revealed abnormalities in the sarcomere function. RNase protection and various other methods can be used to screen an individual HCM patient for myosin mutations. To date 17 missense mutations have been identified. They have only been found in individuals affected with hypertrophic cardiomyopathy and they have not been detected in unaffected relatives or in over 200 other unrelated individuals. We have screened the beta cardiac myosin heavy chain gene in individuals with sporadic hypertrophic cardiomyopathy. In 2 of 7 probands who had typical clinical features of HCM, but unaffected parents, de novo missense mutations were identified (Arg723Cys and Glu924Lys). In one of the probands the disease was passed on in the germline to her daughter. De novo mutations, then, can cause both the familial and sporadic forms of hypertrophic cardiomyopathy. This indicates that sporadic and familial hypertrophic cardiomyopathy represent different parts of the spectrum of the same condition and this has important implications for management in relation to genetic counseling and risk factor stratification.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Hypertrophic cardiomyopathy: an update. 802 27

Myosin diversity in the human epithelial cell line Caco-2BBe, the porcine epithelial cell line LLC-PK1 (CL-4), human peripheral blood leukocytes, and human liver was analyzed. PCR amplification yielded 8-11 putative myosins (depending on the cDNA source) representing six distinct myosin classes. Analysis of clones obtained by hybridization screening demonstrated that the original PCR products correspond to bona fide myosins, based on the presence of sequences highly conserved in other myosins. RNase protection analysis confirmed mRNA expression of 11 myosins in Caco-2BBe cells. Immunoblot analysis showed that at least 6 myosin immunogens are expressed in Caco-2BBe cells. The results reveal the existence of at least 11 unconventional human myosin genes, most of which are expressed in an overlapping fashion in different cell types. The abundance of myosins suggests that the myosin I vs. myosin II paradigm is inadequate to explain actin-based cellular motility.
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PMID:Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. 797 38

Based on previous immunological data, cross-reactivity of myosin heavy chain (MHC) with the ventricular (V) isoform was observed in primordia of avian skeletal muscles and in regenerating adult anterior latissimus dorsi (ALD) muscle. To determine whether this primordial (P) MHC is identical to adult V-MHC gene product, we have cloned and characterized the 3' portion of MHC cDNA that is expressed in ALD muscle at 3 d of regeneration. Comparison of nucleotide sequences between adult V-MHC and P-MHC cDNAs revealed more than 98% homology in the 3'-untranslated (UT) portions of these genes. The expression pattern of P-MHC was analyzed in adult regenerating muscles using total RNA from two fast muscles, posterior latissimus dorsi (PLD) and pectoralis major (PM), as well as from slow ALD and mixed fast/slow gastrocnemius muscles at 0, 1, 3, 4, 6, 9, and 14 d after cold injury. Identical results were obtained by RNase protection assays using either a probe specifying the coding region of adult V-MHC or a P-MHC probe encoding the carboxy end plus the 3'-UT region. The expected protected fragments were detected early from day 2 up to day 6 in ALD muscle. Similar rate of appearance, reaching the highest level at day 3, was observed in PLD, PM, and gastrocnemius muscles. However, the amount and the kinetics of disappearance differed among the various muscles analyzed. In contrast, during development, steady-state levels and kinetics of V-MHC mRNA expression were found to be alike in axial and appendicular muscles. These data strongly suggest the identity of P-MHC as the ventricular isoform and support the concept that expression of P-MHC mRNA is a common feature of developing as well as of all regenerating adult skeletal muscles. Interestingly, no expression of cardiac specific myosin light chain (MLC) 2A was observed after cold injury, suggesting independent regulatory pathways for the two kinds of myosin subunits.
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PMID:Differential expression of ventricular-like myosin heavy chain mRNA in developing and regenerating avian skeletal muscles. 817 88

In the companion paper (M. D. Peterson and M. S. Mooseker (1993). J. Cell Sci. 105, 445-460) we describe a method for modeling brush border assembly in the Caco-2BBe clones. In this study we have examined the molecular changes accompanying cell contact-induced brush border assembly. A subset of brush border proteins was tracked throughout brush border assembly by immunoblotting and by immunofluorescent localization using laser scanning confocal microscopy. Actin, fodrin, villin and presumptive unconventional myosin immunogens were distributed at the periphery of depolarized cells. All proteins partitioned primarily with the membrane fraction upon differential sedimentation of depolarized cell lysates; the fractionation patterns were comparable to those of confluent cells. After a monolayer had formed, each protein showed a redistribution to the apical domain in a discrete sequence. Actin and villin began to shift apically at 2 d, while fodrin and the unconventional myosin immunogens did not redistribute until 3 d. Enterocyte-like localization was observed by 5 d for all proteins. Sucrase-isomaltase was not reliably detectable until 9 d by immunofluorescence, after brush border assembly was complete. Quantitative immunoblot analysis of total cell extracts demonstrated an average 10-fold increase in villin levels, while fodrin levels appeared to remain unchanged. Three putative unconventional myosin immunogens of 140 kDa, 130 kDa, and 110 kDa have been detected previously in the C2BBe cells with a head-specific monoclonal antibody to avian brush border myosin I (M. D. Peterson and M. S. Mooseker (1992) J. Cell Sci. 102, 581-600). Each of these immunogens displayed distinct expression patterns during brush border assembly. The 140 kDa species decreased by half, while the 130 kDa immunogen(s) did not change in any consistent fashion. The 110 kDa protein, presumed to be human brush border myosin I, rose on average 8-fold. A ribonuclease protection assay was also performed using a probe for human brush border myosin I. Equal amounts of total RNA from depolarized and confluent cells were assayed; the level of protected product was approximately 9-fold greater in the confluent cells. The expression patterns of the brush border proteins, coupled with the correlation to the ultrastructural features during brush border assembly in C2BBe cells, show that differentiation of the C2BBe cells closely resembles the changes that occur during human fetal intestinal differentiation.
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PMID:An in vitro model for the analysis of intestinal brush border assembly. II. Changes in expression and localization of brush border proteins during cell contact-induced brush border assembly in Caco-2BBe cells. 840 77

Previous work demonstrated that the rabbit smooth muscle myosin heavy chain gene showed sequence divergence at the 25kDa/50kDa junction of the S1 subfragment when compared to chicken gizzard and chicken epithelial nonmuscle myosin. RNase protection analysis with a probe spanning this region detected two partially protected fragments which were not present in RNA from vascular tissue and only found in RNA from visceral tissue. The polymerase chain reaction was used to amplify a 162bp product from primers spanning the putative region of divergence and DNA sequence analysis revealed a seven amino acid insertion not previously detected in other characterised cDNA clones. RNase protection analysis using the PCR product as probe showed that the inserted sequence was expressed exclusively in RNA from visceral tissue. Similar RNA analysis showed that the visceral isoform was not expressed in 20 day fetal rabbit smooth muscle tissues. These results indicated that the new visceral isoform was expressed in a tissue-specific and developmentally regulated manner. Genomic DNA sequencing and mapping of the exon-intron boundaries showed that the visceral isoform was the product of cassette-type alternative splicing. The inclusion of a visceral-specific sequence near the Mg-ATPase domain and at the 25kDa/50kDa junction suggests that the visceral isoform may be important for myosin function in smooth muscle cells.
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PMID:Tissue-specific and developmentally regulated alternative splicing of a visceral isoform of smooth muscle myosin heavy chain. 846 39


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