scholarly journals Very Stable Two Mega Dalton High-Molecular-Mass Multiprotein Complex from Sea Cucumber Eupentacta fraudatrix

Molecules ◽  
2021 ◽  
Vol 26 (18) ◽  
pp. 5703
Author(s):  
Anna M. Timofeeva ◽  
Irina A. Kostrikina ◽  
Pavel S. Dmitrenok ◽  
Svetlana E. Soboleva ◽  
Georgy A. Nevinsky
Keyword(s):  
Protein Complexes ◽  
Whole Body ◽  
Multiprotein Complex ◽  
Internal Organs ◽  
Modern Biology ◽  
Sea Cucumbers ◽  
Small Proteins ◽  
Molecular Masses ◽  
Eupentacta Fraudatrix ◽  
Proteins And Peptides

In contrast to many human organs, only the human liver can self-regenerate, to some degree. Some marine echinoderms are convenient objects for studying the processes of regenerations of organs and tissues. For example, sea cucumbers Eupentacta fraudatrix can completely restore within several weeks, the internal organs and the whole body after their division into two or three parts. Therefore, these cucumbers are a very convenient model for studying the general mechanisms of regeneration. However, there is no literature data yet on which biomolecules of these cucumbers can stimulate the regeneration of organs and the whole-body processes. Studying the mechanisms of restoration is very important for modern biology and medicine, since it can help researchers to understand which proteins, enzymes, hormones, or possible complexes can play an essential role in regeneration. This work is the first to analyze the possible content of very stable protein complexes in sea cucumbers Eupentacta fraudatrix. It has been shown that their organisms contain a very stable multiprotein complex of about 2000 kDa. This complex contains 15 proteins with molecular masses (MMs) >10 kDa and 21 small proteins and peptides with MMs 2.0–8.6 kDa. It is effectively destroyed only in the presence of 3.0 M MgCl2 and, to a lesser extent, 3.0 M NaCl, while the best dissociation occurs in the presence of 8.0 M urea + 0.1 M EDTA. Our data indicate that forming a very stable proteins complex occurs due to the combination of bridges formed by metal ions, electrostatic contacts, and hydrogen bonds.

Rheumatoid Arthritis: History, Stages, Epidemiology, Pathogenesis, Diagnosis and Treatment

2017 ◽  
Vol 9 (02) ◽  
Author(s):  
Abeer Fauzi Al-Rubaye ◽  
Mohanad Jawad Kadhim ◽  
Imad Hadi Hameed
Keyword(s):  
Rheumatoid Arthritis ◽  
Medicinal Plants ◽  
Systemic Disease ◽  
Modern Medicine ◽  
Whole Body ◽  
Internal Organs ◽  
Synthetic Drugs ◽  
Relieve Pain ◽  
Medicinal Treatment ◽  
Natural Drugs

The pharmacological mechanisms of the medicinal plants traditionally used for RA in Persian medicine are discussed in the current review. Further investigations are mandatory to focus on bioefficacy of these phytochemicals for finding novel natural drugs. Rheumatoid arthritis is chronic, progressive, disabling autoimmune disease characterized by systemic inflammation of joints, damaging cartilage and bone around the joints. It is a systemic disease which means that it can affect the whole body and internal organs such as lungs, heart and eyes. Although numbers of synthetic drugs are being used as standard treatment for rheumatoid arthritis but they have adverse effect that can compromise the therapeutic treatment. Unfortunately, there is still no effective known medicinal treatment that cures rheumatoid arthritis as the modern medicine can only treat the symptoms of this disease that means to relieve pain and inflammation of joints. It is possible to use the herbs and plants in various forms in order to relieve the pain and inflammation in the joints. There are so many medicinal plants that have shown anti rheumatoid arthritis properties. So the plants and plant product with significant advantages are used for the treatment of rheumatoid arthritis. The present review is focused on the medicinal plants having anti rheumatoid arthritis activity

CURVILINEAR DYNAMICS OF PROTEIN COMPLEXES

2012 ◽  
Vol 11 (03) ◽  
pp. 675-696 ◽  
Author(s):  
K. O. E. HENRIKSSON ◽  
J. PESONEN ◽  
P. CHACON
Keyword(s):  
Molecular Dynamic ◽  
Protein Complexes ◽  
Molecular Dynamic Simulations ◽  
Dynamic Simulations ◽  
Small Proteins ◽  
Covalently Bonded

The suitability of a recently developed extension to the polyspherical parametrization of protein complexes has been investigated by molecular dynamic simulations. The extension makes it possible to study the motion of proteins consisting of several chains, which are internally covalently bonded. Tests indicate that time steps of up to at least 10 fs for simulations lasting up to 100 ps are possible, at least for small proteins.

Why Is the GFR So High?: Implications for the Treatment of Kidney Failure

2020 ◽  
Vol 16 (6) ◽  
pp. 980-987
Author(s):  
Timothy W. Meyer ◽  
Thomas H. Hostetter
Keyword(s):  
Energy Expenditure ◽  
Metabolic Rate ◽  
Kidney Failure ◽  
Tubular Secretion ◽  
Large Energy ◽  
Vertebrate Species ◽  
Fluid Stream ◽  
Toxic Compounds ◽  
Small Proteins ◽  
Proteins And Peptides

The high GFR in vertebrates obligates large energy expenditure. Homer Smith’s teleologic argument that this high GFR was needed to excrete water as vertebrates evolved in dilute seas is outdated. The GFR is proportional to the metabolic rate among vertebrate species and higher in warm-blooded mammals and birds than in cold-blooded fish, amphibians, and reptiles. The kidney clearance of some solutes is raised above the GFR by tubular secretion, and we presume secretion evolved to eliminate particularly toxic compounds. In this regard, high GFRs may provide a fluid stream into which toxic solutes can be readily secreted. Alternatively, the high GFR may be required to clear solutes that are too large or too varied to be secreted, especially bioactive small proteins and peptides. These considerations have potentially important implications for the understanding and treatment of kidney failure.

Wnt and frizzled expression during regeneration of internal organs in the holothurian Eupentacta fraudatrix

2017 ◽  
Vol 25 (5) ◽  
pp. 828-835 ◽  
Author(s):  
Alexander S. Girich ◽  
Marina P. Isaeva ◽  
Igor Yu. Dolmatov
Keyword(s):  
Internal Organs ◽  
Eupentacta Fraudatrix

Body composition of young sheep: I. Body composition in merino and Border Leicester × Merino hoggets in relation to and at common empty body weight

1969 ◽  
Vol 72 (1) ◽  
pp. 65-75 ◽  
Author(s):  
H. R. Gharaybeh ◽  
W. R. McManus ◽  
G. W. Arnold ◽  
M. L. Dudzinski
Keyword(s):  
Body Composition ◽  
Body Weight ◽  
Chemical Composition ◽  
Total Energy ◽  
Crude Protein ◽  
Whole Body ◽  
Ether Extract ◽  
Internal Organs ◽  
Breed Differences ◽  
Body Components

SUMMARYFlocks of 9-month-old Merino and Border Leicester & Merino sheep were sampled over the full range of body weights present within flocks. Six pairs of ewes and wethers of equal body weight were taken. The sheep were weighed and slaughtered after a 36 h fast. Total weights of blood, skin, head, feet, internal organs and carcasses were obtained for each animal. Each component was analysed for ash, crude protein, ether extract and total energy. Half of each carcass was dissected into bone, muscle, fat and waste.The compositions of the sheep were compared by regression analyses of weights of body components on empty body weight (EBW) between the four groups and by means of percentages of EBW. There were highly significant linear relationships between both fresh and dry weights of body components, carcass components, and chemical components with EBW; moisture content was not related to EBW. Rates of change with EBW in weights of body components, or in amounts of ash, crude protein, ether extract and energy were the same for all groups of sheep with the exceptions of bone and skin ether extract (EE) weight. However, intercepts of regression lines frequently differed, indicating that body composition differed between groups at the same EBW.All groups had the same dry weight of blood, internal organs and muscle, weight of ether extract, and total energy in the whole body at the same EBW. Border Leicester × Merinos had lighter skins with less wool, but their carcass weights were higher than Merinos. There were other differences between breeds in the chemical composition of individual components. Wethers had heavier head + feet weights and carcass bone than had ewes. There were also some sex differences in chemical composition of body components. In general, there were fewer sex than breed differences in body composition. The breed differences cannot be explained on the basis of early and later maturing types.

scholarly journals Drosophila laminin: characterization and localization.

1987 ◽  
Vol 105 (5) ◽  
pp. 2383-2391 ◽  
Author(s):  
L I Fessler ◽  
A G Campbell ◽  
K G Duncan ◽  
J H Fessler
Keyword(s):  
Basement Membrane ◽  
Polyclonal Antibodies ◽  
Lectin Binding ◽  
Gel Filtration ◽  
Basement Membranes ◽  
Velocity Sedimentation ◽  
Internal Organs ◽  
Differentiated Cells ◽  
Basement Membrane Component ◽  
Molecular Masses

Drosophila laminin was isolated from the medium of Drosophila Kc cell cultures. It was purified by velocity sedimentation, gel filtration, and chromatography. Drosophila laminin is a disulfide-linked molecule consisting of three chains with apparent molecular masses of 400, 215, and 185 kD. In electron micrographs, it has the cross-shaped appearance with globular domains characteristic of vertebrate laminin with closely similar dimensions. The amino acid composition and lectin-binding properties of Drosophila laminin are given. Polyclonal antibodies to Drosophila laminin were prepared and their specificity was established. In developing embryos immunofluorescence staining was detected between 6 and 8 h of development; and in sections of 8-9-h and older embryos immunostaining was seen at sites where basement membranes are present surrounding internal organs, muscles, underlying the hypodermal epithelium, and in the nervous system. Basement membrane staining was also seen in larva and adults. Cells from Drosophila embryos dissociated at the cellular blastoderm stage were grown in culture and some specific, differentiated cells synthesized laminin after several hours of culture as shown by immunofluorescence. The significance of the evolutionary conservation of the structure of this basement membrane component is discussed.

Proteome Organization in a Genome-Reduced Bacterium

Science ◽  
2009 ◽  
Vol 326 (5957) ◽  
pp. 1235-1240 ◽  
Author(s):  
Sebastian Kühner ◽  
Vera van Noort ◽  
Matthew J. Betts ◽  
Alejandra Leo-Macias ◽  
Claire Batisse ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Affinity Purification ◽  
Biological Processes ◽  
Multiprotein Complex ◽  
Data Set ◽  
Basic Principles ◽  
A Genome ◽  
Structural Details ◽  
Cellular Machinery ◽  
Affinity Purification Mass Spectrometry

The genome of Mycoplasma pneumoniae is among the smallest found in self-replicating organisms. To study the basic principles of bacterial proteome organization, we used tandem affinity purification–mass spectrometry (TAP-MS) in a proteome-wide screen. The analysis revealed 62 homomultimeric and 116 heteromultimeric soluble protein complexes, of which the majority are novel. About a third of the heteromultimeric complexes show higher levels of proteome organization, including assembly into larger, multiprotein complex entities, suggesting sequential steps in biological processes, and extensive sharing of components, implying protein multifunctionality. Incorporation of structural models for 484 proteins, single-particle electron microscopy, and cellular electron tomograms provided supporting structural details for this proteome organization. The data set provides a blueprint of the minimal cellular machinery required for life.

scholarly journals Getting more out of co-immunoprecipitation mass spectrometry experiments by reducing interference using FAIMS.

2021 ◽  
Author(s):  
Ching-Seng Ang ◽  
Joanna Sacharz ◽  
Michael G Leeming ◽  
Shuai Nie ◽  
Swati Varshney ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Protein Complexes ◽  
Affinity Purification ◽  
Mass Spectrometry Analysis ◽  
Modern Biology ◽  
Spectrometry Analysis ◽  
Affinity Enrichment ◽  
Unbiased Manner ◽  
Gas Phase Ion

Co-immunoprecipitation of proteins coupled to mass spectrometry has transformed modern biology understanding of protein interaction networks. These approaches exploit the selective isolation of tagged proteins by affinity enrichment / purification to identify protein binding partners at scale and in an unbiased manner. In instances where a suitable antibody is not be available it is common to graft synthetic tags such as FLAG or His Tags onto target protein sequences allowing the use of commercially available and validated antibodies for affinity purification. To allow the selective elution of protein complexes competitive displacement using a large molar excess of the tag peptide is widely used. Yet, this creates downstream challenges for the mass spectrometry analysis due to the presence of large quantities of a contaminating peptide. Here, we demonstrate that Field Asymmetric Ion Mobility Spectrometry (FAIMS), a gas phase ion separation device can be applied to FLAG-Tag and His-Tag pull down assay to increase the depth of protein coverage in these experiments. By excluding tag peptides based on their ion mobility profiles we demonstrate that single compensation voltage, or stepped compensation voltages strategies can significantly increase the coverage of total proteins by up to 2.5-fold and unique proteins by up to 15-fold versus experiments that do not use FAIMS. Combined these results highlight FAIMS is able to improve proteome depth by excluding interfering peptides without the need for additional sample handling or altering sample preparation protocols.

scholarly journals Towards the application of Tc toxins as a universal protein translocation system

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Daniel Roderer ◽  
Evelyn Schubert ◽  
Oleg Sitsel ◽  
Stefan Raunser
Keyword(s):  
Protein Translocation ◽  
Protein Complexes ◽  
Target Cells ◽  
X Ray Crystallography ◽  
Tev Protease ◽  
Small Proteins ◽  
Simplex Virus ◽  
In Vitro Translocation ◽  
Universal Protein

AbstractTc toxins are bacterial protein complexes that inject cytotoxic enzymes into target cells using a syringe-like mechanism. Tc toxins are composed of a membrane translocator and a cocoon that encapsulates a toxic enzyme. The toxic enzyme varies between Tc toxins from different species and is not conserved. Here, we investigate whether the toxic enzyme can be replaced by other small proteins of different origin and properties, namely Cdc42, herpes simplex virus ICP47, Arabidopsis thaliana iLOV, Escherichia coli DHFR, Ras-binding domain of CRAF kinase, and TEV protease. Using a combination of electron microscopy, X-ray crystallography and in vitro translocation assays, we demonstrate that it is possible to turn Tc toxins into customizable molecular syringes for delivering proteins of interest across membranes. We also infer the guidelines that protein cargos must obey in terms of size, charge, and fold in order to apply Tc toxins as a universal protein translocation system.

Sign in / Sign up

Export Citation Format

Share Document