scholarly journals Drosophila paramyosin/miniparamyosin gene products show a large diversity in quantity, localization, and isoform pattern: a possible role in muscle maturation and function.

1996 ◽  
Vol 134 (1) ◽  
pp. 81-92 ◽  
Author(s):  
M Maroto ◽  
J Arredondo ◽  
D Goulding ◽  
R Marco ◽  
B Bullard ◽  
...  
Keyword(s):  
Wide Spectrum ◽  
Thick Filament ◽  
One Dimensional ◽  
Thick Filaments ◽  
Wide Ph Range ◽  
Muscle Types ◽  
Flight Muscles ◽  
Ph Range ◽  
And Function

The Drosophila paramyosin/miniparamyosin gene expresses two products of different molecular weight transcriptionally regulated from two different promoters. Distinct muscle types also have different relative amounts of myosin, paramyosin, and miniparamyosin, reflecting differences in the organization of their thick filaments. Immunofluorescence and EM data indicate that miniparamyosin is mainly located in the M line and at both ends of the thick filaments in Drosophila indirect flight muscles, while paramyosin is present all along the thick filaments. In the tergal depressor of the trochanter muscle, both proteins are distributed all along the A band. In contrast, in the waterbug, Lethocerus, both paramyosin and miniparamyosin are distributed along the length of the indirect flight and leg muscle thick filaments. Two-dimensional and one-dimensional Western blot analyses have revealed that miniparamyosin has several isoforms, focusing over a very wide pH range, all of which are phosphorylated in vivo. The changes in isoform patterns of miniparamyosin and paramyosin indicate a direct or indirect involvement of these proteins in muscle function and flight. This wide spectrum of potential regulatory characteristics underlines the key importance of paramyosin/miniparamyosin and its complex isoform pattern in the organization of the invertebrate thick filament.

scholarly journals THE EPIDEMIOLOGY OF PNEUMOCOCCUS INFECTION

1931 ◽  
Vol 53 (4) ◽  
pp. 535-552 ◽  
Author(s):  
Leslie T. Webster ◽  
Thomas P. Hughes
Keyword(s):  
Seasonal Variation ◽  
Host Resistance ◽  
The Other ◽  
Colony Morphology ◽  
Type Transformation ◽  
Wide Ph Range ◽  
Adults And Children ◽  
Nasal Passages ◽  
Ph Range

1. Pneumococci were obtained at one time or another from the nasal passages or throats of 80 per cent of 105 adults and children studied. In adults, they were obtained more frequently from the throat; in children, as often from the nasal passages as from the throat. 2. Of 500 pneumococcus strains studied, 97 per cent proved to be serologically specific. They formed smooth colonies and were for the most part avirulent for mice. Types I and II were obtained from one and two individuals respectively on one occasion only. Type III was obtained from nine individuals; Type XIII from nine individuals; Type XVI and Type XVIII from three individuals, for varying periods in each case. Atypical pneumococci were secured from 13 persons on single and scattered occasions. They varied in colony morphology, did not kill mice, or agglutinate in saline, but flocculated in all types of antipneumococcus sera employed and over a wide pH range in acid buffers. Their occurrence was apparently not associated with any type-transformation or virulence-enhancement process in vivo. 3. Strains of pneumococcus obtained on successive cultures from a given carrier were, with rare exceptions, of the same serological type and were similar in colony morphology, virulence for mice, and other tested biological characteristics. 4. Pneumococci of Types I and II were obtained under conditions suggestive that they lacked a capacity to spread readily; pneumococci of Types III and XIII, on the other hand, were obtained under conditions suggestive that they were spreading from person to person. 5. The persons studied differed consistently with respect to the occurrence of pneumococci. Some were pneumococcus-free, some were transient carriers, some periodic, and some chronic carriers. Data are given which suggest that the differences were due to variations in host resistance. 6. The incidence of pneumococci in all individuals studied underwent a seasonal variation paralleling that of coryza and sore throats in the same persons.

Cytoskeletal proteins of insect muscle: location of zeelins in Lethocerus flight and leg muscle

1994 ◽  
Vol 107 (5) ◽  
pp. 1115-1129 ◽  
Author(s):  
C. Ferguson ◽  
A. Lakey ◽  
A. Hutchings ◽  
G.W. Butcher ◽  
K.R. Leonard ◽  
...  
Keyword(s):  
Insect Flight ◽  
Regular Structure ◽  
Thick Filament ◽  
Cytoskeletal Proteins ◽  
Stretch Activation ◽  
Insect Muscle ◽  
Thick Filaments ◽  
Flight Muscles ◽  
Leg Muscle ◽  
Low Ionic Strength

Asynchronous insect flight muscles produce oscillatory contractions and can contract at high frequency because they are activated by stretch as well as by Ca2+. Stretch activation depends on the high stiffness of the fibres and the regular structure of the filament lattice. Cytoskeletal proteins may be important in stabilising the lattice. Two proteins, zeelin 1 (35 kDa) and zeelin 2 (23 kDa), have been isolated from the cytoskeletal fraction of Lethocerus flight muscle. Both zeelins have multiple isoforms of the same molecular mass and different charge. Zeelin 1 forms micelles and zeelin 2 forms filaments when renatured in low ionic strength solutions. Filaments of zeelin 2 are ribbons 10 nm wide and 3 nm thick. The position of zeelins in fibres from Lethocerus flight and leg muscle was determined by immunofluorescence and immunoelectron microscopy. Zeelin 1 is found in flight and leg fibres and zeelin 2 only in flight fibres. In flight myofibrils, both zeelins are in discrete regions of the A-band in each half sarcomere. Zeelin 1 is across the whole A-band in leg myofibrils. Zeelins are not in the Z-disc, as was thought previously, but migrate to the Z-disc in glycerinated fibres. Zeelins are associated with thick filaments and analysis of oblique sections showed that zeelin 1 is closer to the filament shaft than zeelin 2. The antibody labelling pattern is consistent with zeelin molecules associated with myosin near the end of the rod region. Alternatively, the position of zeelins may be determined by other A-band proteins. There are about 2.0 to 2.5 moles of myosin per mole of each zeelin. The function of these cytoskeletal proteins may be to maintain the ordered structure of the thick filament.

scholarly journals In vitro and in vivo activities of flavonoids – apigenin, baicalin, chrysin, scutellarin – in regulation of hypertension – a review for their possible effects in pregnancy-induced hypertension

2019 ◽  
Vol 65 (1) ◽  
pp. 55-70 ◽  
Author(s):  
Marcin Ożarowski ◽  
Radosław Kujawski ◽  
Przemysław Ł. Mikołajczak ◽  
Karolina Wielgus ◽  
Andrzej Klejewski ◽  
...  
Keyword(s):  
Ex Vivo ◽  
Biological Activities ◽  
Wide Spectrum ◽  
Chemical Compounds ◽  
New Drugs ◽  
Future Application ◽  
Mediators Of Inflammation ◽  
And Function

Summary Flavonoids and their conjugates are the most important group of natural chemical compounds in drug discovery and development. The search for pharmacological activity and new mechanisms of activity of these chemical compounds, which may inhibit mediators of inflammation and influence the structure and function of endothelial cells, can be an interesting pharmacological strategy for the prevention and adjunctive treatments of hypertension, especially induced by pregnancy. Because cardiovascular diseases have multi-factorial pathogenesis these natural chemical compounds with wide spectrum of biological activities are the most interesting source of new drugs. Extracts from one of the most popular plant used in Traditional Chinese Medicine, Scutellaria baicalensis Georgi could be a very interesting source of flavonoids because of its exact content in quercetin, apigenin, chrysin and scutellarin as well as in baicalin. These flavonoids exert vasoprotective properties and many activities such as: anti-oxidative via several pathways, anti-in-flammatory, anti-ischaemic, cardioprotective and anti-hypertensive. However, there is lack of summaries of results of studies in context of potential and future application of flavonoids with determined composition and activity. Our review aims to provide a literature survey of in vitro, in vivo and ex vivo pharmacological studies of selected flavonoids (apigenin, chrysin and scutellarin, baicalin) in various models of hypertension carried out in 2008–2018.

scholarly journals Surface engineering-modulated porous N-doped rod-like molybdenum phosphide catalysts: towards high activity and stability for hydrogen evolution reaction over a wide pH range

RSC Advances ◽  
2018 ◽  
Vol 8 (47) ◽  
pp. 26871-26879 ◽  
Author(s):  
Liying Chai ◽  
Wenyu Yuan ◽  
Xue Cui ◽  
Haiying Jiang ◽  
Junwang Tang ◽  
...  
Keyword(s):  
Hydrogen Evolution Reaction ◽  
Surface Engineering ◽  
Cyclic Stability ◽  
One Dimensional ◽  
Nitrogen Doped ◽  
Catalytic Activities ◽  
Synthetic Strategy ◽  
Molybdenum Phosphide ◽  
Wide Ph Range ◽  
Ph Range

Porous one-dimensional (1D) nitrogen-doped molybdenum phosphide (N-MoP) nanorods can be produced via a two-step synthetic strategy. The prepared N-MoP catalysts show high HER catalytic activities and cyclic stability over a wide pH range.

scholarly journals Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly in Caenorhabditis elegans.

1996 ◽  
Vol 135 (2) ◽  
pp. 371-382 ◽  
Author(s):  
P E Hoppe ◽  
R H Waterston
Keyword(s):  
Caenorhabditis Elegans ◽  
Striated Muscle ◽  
Coiled Coil ◽  
Thick Filament ◽  
Surface Hydrophobicity ◽  
Filament Assembly ◽  
Thick Filaments ◽  
Characteristic Variation ◽  
Muscle Myosin

Caenorhabditis elegans body wall muscle contains two isoforms of myosin heavy chain, MHC A and MHC B, that differ in their ability to initiate thick filament assembly. Whereas mutant animals that lack the major isoform, MHC B, have fewer thick filaments, mutant animals that lack the minor isoform, MHC A, contain no normal thick filaments. MHC A, but not MHC B, is present at the center of the bipolar thick filament where initiation of assembly is thought to occur (Miller, D.M.,I. Ortiz, G.C. Berliner, and H.F. Epstein. 1983. Cell. 34:477-490). We mapped the sequences that confer A-specific function by constructing chimeric myosins and testing them in vivo. We have identified two distinct regions of the MHC A rod that are sufficient in chimeric myosins for filament initiation function. Within these regions, MHC A displays a more hydrophobic rod surface, making it more similar to paramyosin, which forms the thick filament core. We propose that these regions play an important role in filament initiation, perhaps mediating close contacts between MHC A and paramyosin in an antiparallel arrangement at the filament center. Furthermore, our analysis revealed that all striated muscle myosins show a characteristic variation in surface hydrophobicity along the length of the rod that may play an important role in driving assembly and determining the stagger at which dimers associate.

scholarly journals THE FILAMENT LATTICE OF COCKROACH THORACIC MUSCLE

1968 ◽  
Vol 36 (3) ◽  
pp. 433-442 ◽  
Author(s):  
Martin Hagopian ◽  
David Spiro
Keyword(s):  
Fine Structure ◽  
Electron Microscope ◽  
Flight Muscle ◽  
Insect Flight ◽  
Thick Filament ◽  
Leucophaea Maderae ◽  
Thick Filaments ◽  
Femoral Muscle ◽  
Flight Muscles ◽  
Characteristic 3

The fine structure of the tergo-coxal muscle of the cockroach, Leucophaea maderae, has been studied with the electron microscope. This muscle differs from some other types of insect flight muscles inasmuch as the ratio of thin to thick filaments is 4 instead of the characteristic 3. The cockroach flight muscle also differs from the cockroach femoral muscle in thin to thick filament ratios and diameters and in lengths of thick filaments. A comparison of these latter three parameters in a number of vertebrate and invertebrate muscles suggests in general that the diameters and lengths of the thick filaments and thin to thick filament ratios are related.

A structural perspective on lactoferrin function1This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal's usual peer review process.

2012 ◽  
Vol 90 (3) ◽  
pp. 320-328 ◽  
Author(s):  
Heather M. Baker ◽  
Edward N. Baker
Keyword(s):  
Peer Review Process ◽  
Iron Binding ◽  
Multifunctional Protein ◽  
Wide Ph Range ◽  
Iron Binding Protein ◽  
Productive Research ◽  
Ph Range ◽  
The Many ◽  
And Function

The 3-D structure of human lactoferrin was first solved in atomic detail in 1987. Since that time, a variety of proven and postulated activities have been added to the original annotation of lactoferrin as an iron-binding protein. Structural studies have also expanded to include iron-bound and iron-free (apo) forms, mutants, and the lactoferrins of different species. In this review, we take the current information on both structure and function and show that the 3-D structure provides a useful framework for understanding some activities and also points to productive research directions that could help elucidate other reported functions. Some functions relate to iron binding where the role of lactoferrin is to scavenge and retain iron across a wide pH range. We specifically focus on functions that depend on the surface structure of the molecule, identifying features that may determine the many other protective properties of this multifunctional protein.

scholarly journals Distinct Expression and Function of Alternatively Spliced Tbx5 Isoforms in Cell Growth and Differentiation

2008 ◽  
Vol 28 (12) ◽  
pp. 4052-4067 ◽  
Author(s):  
Romain Georges ◽  
Georges Nemer ◽  
Martin Morin ◽  
Chantal Lefebvre ◽  
Mona Nemer
Keyword(s):  
Heart Development ◽  
Wide Spectrum ◽  
Protein A ◽  
Growth Stimulation ◽  
Underlying Mechanism ◽  
Experimental Models ◽  
Dependent Manner ◽  
Dominant Disease ◽  
And Function

ABSTRACT Mutations in the T-box transcription factor Tbx5 cause Holt-Oram syndrome, an autosomal dominant disease characterized by a wide spectrum of cardiac and upper limb defects with variable expressivity. Tbx5 haploinsufficiency has been suggested to be the underlying mechanism, and experimental models are consistent with a dosage-sensitive requirement for Tbx5 in heart development. Here, we report that Tbx5 levels are regulated through alternative splicing that generates, in addition to the known 518-amino-acid protein, a C-terminal truncated isoform. This shorter isoform retains the capacity to bind DNA, but its interaction with Tbx5 collaborators such as GATA-4 is altered. In vivo, the two spliced isoforms are oppositely regulated in a temporal and growth factor-dependent manner and are present in distinct DNA-binding complexes. The expression of the long isoform correlates with growth stimulation, and its reexpression in postnatal transgenic mouse hearts promotes hypertrophy. Conversely, the upregulation of the short but not the long isoform in C2C12 myoblasts leads to growth arrest and cell death. The results provide novel insight into posttranscriptional Tbx5 regulation and point to an important role not only in cell differentiation but also in cell proliferation and organ growth. The data may help analyze genotype-phenotype relations in patients with Holt-Oram syndrome.

scholarly journals CryoEM Structure of Drosophila Flight Muscle Thick Filaments at 7Å Resolution

2020 ◽  
Author(s):  
Nadia Daneshparvar ◽  
Dianne W. Taylor ◽  
Thomas S. O’Leary ◽  
Hamidreza Rahmani ◽  
Fatemeh Abbasi Yeganeh ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Striated Muscle ◽  
Flight Muscle ◽  
Coiled Coil ◽  
Thick Filament ◽  
Fruit Fly ◽  
Actin Binding ◽  
Thick Filaments ◽  
Flight Muscles ◽  
Lethocerus Indicus

AbstractStriated muscle thick filaments are composed of myosin II and several non-myosin proteins. Myosin II’s long α-helical coiled-coil tail forms the dense protein backbone of filaments while its N-terminal globular head containing the catalytic and actin binding activities extends outward from the backbone. Here we report the structure of thick filaments of the flight muscle of the fruit fly Drosophila melanogaster at 7 Å resolution. Its myosin tails are arranged in curved molecular crystalline layers identical to flight muscles of the giant waterbug Lethocerus indicus. Four non-myosin densities are observed, three of which correspond to ones found in Lethocerus; one new density, possibly stretchin-Mlck, is found on the backbone outer surface. Surprisingly, the myosin heads are disordered rather than ordered along the filament backbone. Our results show striking myosin tail similarity within flight muscle filaments of two insect orders separated by several hundred million years of evolution.Significance StatementMyosin thick filaments are one of striated muscle’s key structures, but also one of its least understood. A key question is how the myosin a-helical coiled-coil tail is arranged in the backbone. At 7Å resolution, sufficient to resolve individual a-helices, the myosin tail arrangement in thick filaments from the flight muscle of the fruit fly Drosophila melanogaster is strikingly similar to the myosin tail arrangement in flight muscles of the giant waterbug Lethocerus indicus. Nearly every other thick filament feature is different. Drosophila and Lethocerus evolved separately >245 million years ago suggesting myosin tail packing into curved molecular crystalline layers forms a highly conserved thick filament building block and different properties are obtained by alterations in non-myosin proteins.

scholarly journals Myosin light chain phosphorylation facilitates in vivo myosin filament reassembly after mechanical perturbation

2002 ◽  
Vol 282 (6) ◽  
pp. C1298-C1305 ◽  
Author(s):  
D. Qi ◽  
R. W. Mitchell ◽  
T. Burdyga ◽  
L. E. Ford ◽  
K.-H. Kuo ◽  
...  
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Isometric Force ◽  
Thick Filament ◽  
Myosin Filament ◽  
Mechanical Perturbation ◽  
Cross Sectional ◽  
Thick Filaments ◽  
Mlc Phosphorylation

Phosphorylation of the 20-kDa regulatory myosin light chain (MLC) of smooth muscle is known to cause monomeric myosins in solution to self-assemble into thick filaments. The role of MLC phosphorylation in thick filament formation in intact muscle, however, is not clear. It is not known whether the phosphorylation is necessary to initiate thick filament assembly in vivo. Here we show, by using a potent inhibitor of MLC kinase (wortmannin), that the MLC phosphorylation and isometric force in trachealis muscle could be abolished without affecting calcium transients. By measuring cross-sectional densities of the thick filaments electron microscopically, we also show that inhibition of MLC phosphorylation alone did not cause disassembly of the filaments. The unphosphorylated thick filaments, however, partially dissolved when the muscle was subjected to oscillatory strains (which caused a 25% decrease in the thick filament density). The postoscillation filament density recovered to the preoscillation level only when wortmannin was removed and the muscle was stimulated. The data suggest that in vivo thick filament reassembly after mechanical perturbation is facilitated by the cyclic MLC phosphorylation associated with repeated stimulation.

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