scholarly journals Influence of hyaluronic acid transitions in tumor microenvironment on glioblastoma malignancy and invasive behavior

2018 ◽  
Author(s):  
Jee-Wei E Chen ◽  
Sara Pedron ◽  
Peter Shyu ◽  
Yuhang Hu ◽  
Jann N Sarkaria ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Hyaluronic Acid ◽  
Cell Activity ◽  
Invasive Phenotype ◽  
Molecular Weights ◽  
New Information ◽  
Matrix Bound ◽  
The Relationship ◽  
Polymerization Conditions

AbstractThe extracellular matrix (ECM) is critical in tumor growth and invasive potential of cancer cells. In glioblastoma tumors, some components of the native brain ECM such as hyaluronic acid (HA) have been suggested as key regulators of processes associated with poor patient outlook such as invasion and therapeutic resistance. Given the importance of cell-mediated remodeling during invasion, it is likely that the molecular weight of available HA polymer may strongly influence GBM progression. Biomaterial platforms therefore provide a unique opportunity to systematically examine the influence of the molecular weight distribution of HA on GBM cell activity. Here we report the relationship between the molecular weight of matrix-bound HA within a methacrylamide-functionalized gelatin (GelMA) hydrogel, the invasive phenotype of a patient-derived xenograft GBM population that exhibits significant in vivo invasivity, and the local production of soluble HA during GBM cell invasion. Hyaluronic acid of different molecular weights spanning a range associated with cell-mediated remodeling (10, 60, and 500 kDa) was photopolymerized into GelMA hydrogels, with cell activity compared to GelMA only conditions (-HA). Polymerization conditions were tuned to create a homologous series of GelMA hydrogels with conserved poroelastic properties (i.e. shear modulus, Poisson’s ratio, and diffusivity). GBM migration was strongly influenced by HA molecular weight. While markers associated with active remodeling of the HA content, hyaluronan synthase and hyaluronidase, were found to be insensitive to matrix immobilized HA content. These results provide new information regarding the importance of local hyaluronic acid content on the invasive phenotype of GBM.

scholarly journals Rheological Properties of Hyaluronic Acid Diluted Solutions as Components of Cosmetics

2021 ◽  
Vol 12 (2) ◽  
pp. 1907-1915
Keyword(s):  
Molecular Weight ◽  
Hyaluronic Acid ◽  
Viscous Flow ◽  
Ionization Mass ◽  
Rheological Analysis ◽  
Molecular Weights ◽  
Rational Development ◽  
Dilute Aqueous Solutions ◽  
Hyaluronic Acids ◽  
The Relationship

Rheological measurements were carried out on dilute aqueous solutions of high (HMW-HA, 1150 kDa) and low molecular weight hyaluronic acids (LMW-HA, 8 kDa) along with their mixtures to determine the relationship between the viscosity and concentration of the samples. Molecular weight and polydispersity of low molecular HA have been determined by matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS). HA diluted solutions were found to be weakly structured liquids with a slight viscosity anomaly. Critical values of concentration were determined at different ratios of HMW-HA and LMW-HA, leading to a sharp increase in the viscosity of solutions. Rheological studies have proved the pseudoplastic nature of the viscous flow of HMW-HA solutions. The possibility of using the Ostwald-de Waele equation for the mathematical description of a viscous flow was established. The results of the rheological analysis might be applied for the rational development of cosmetic formulations containing hyaluronic acid of various molecular weights.

Toxicity of Heparinoids, with Special Reference to the Precipitation of Fibrinogen

1964 ◽  
Vol 12 (01) ◽  
pp. 232-261 ◽  
Author(s):  
S Sasaki ◽  
T Takemoto ◽  
S Oka
Keyword(s):  
Molecular Weight ◽  
Dextran Sulfate ◽  
Anticoagulant Activity ◽  
Molecular Structures ◽  
Severe Reaction ◽  
Clinical Use ◽  
Molecular Weights ◽  
Close Relationship

SummaryTo demonstrate whether the intravascular precipitation of fibrinogen is responsible for the toxicity of heparinoid, the relation between the toxicity of heparinoid in vivo and the precipitation of fibrinogen in vitro was investigated, using dextran sulfate of various molecular weights and various heparinoids.1. There are close relationships between the molecular weight of dextran sulfate, its toxicity, and the quantity of fibrinogen precipitated.2. The close relationship between the toxicity and the precipitation of fibrinogen found for dextran sulfate holds good for other heparinoids regardless of their molecular structures.3. Histological findings suggest strongly that the pathological changes produced with dextran sulfate are caused primarily by the intravascular precipitates with occlusion of the capillaries.From these facts, it is concluded that the precipitates of fibrinogen with heparinoid may be the cause or at least the major cause of the toxicity of heparinoid.4. The most suitable molecular weight of dextran sulfate for clinical use was found to be 5,300 ~ 6,700, from the maximum value of the product (LD50 · Anticoagulant activity). This product (LD50 · Anticoagulant activity) can be employed generally to assess the comparative merits of various heparinoids.5. Clinical use of the dextran sulfate prepared on this basis gave satisfactory results. No severe reaction was observed. However, two delayed reactions, alopecia and thrombocytopenia, were observed. These two reactions seem to come from the cause other than intravascular precipitation.

scholarly journals Autonomous splicing and complementation of in vivo-assembled spliceosomes.

1989 ◽  
Vol 108 (3) ◽  
pp. 765-777 ◽  
Author(s):  
S Zeitlin ◽  
R C Wilson ◽  
A Efstratiadis
Keyword(s):  
Nuclear Extract ◽  
Physiological Concentration ◽  
Ribonucleoprotein Complexes ◽  
Matrix Bound ◽  
The Relationship ◽  
Matrix Preparation ◽  
Cell Nuclear Extract ◽  
Biochemical Features

We have used an in vivo system generating assayable amounts of a specific pre-mRNA to study the relationship between splicing and an operationally defined nuclear matrix preparation (NM). When NM is prepared by extraction of DNase I-treated nuclei with an approximately physiological concentration of KCl (0.1 M), a portion of NM-associated precursor can be spliced in vitro in the presence of ATP and Mg2+ and in the absence of splicing extract ("autonomous splicing"). We propose that the autonomous reaction, which does not exhibit a temporal lag and is half-complete in 5 min, occurs in fully assembled, matrix-bound ribonucleoprotein complexes (in vivo spliceosomes). Extraction of the NM with concentrations of KCl greater than 0.4 M eliminates autonomous splicing but leaves behind preassembled complexes that can be complemented for splicing with HeLa cell nuclear extract. The splicing complementing factor, representing one or more activities present in the nuclear extract and also in the cytoplasmic S100 fraction, is relatively heat resistant, devoid of an RNA component, and does not bind to DEAE-Sepharose in 0.1 M KCl. It exists in the nucleus in two forms; bound to autonomous spliceosomes and free in the nucleoplasm. Biochemical features of the complementation reaction, and conditions for reversible uncoupling of the two splicing steps are described and discussed.

Molecular Weight of GR-S Fractions. Simple Glass Osmometer for Use in Hydrocarbon Solvents

1947 ◽  
Vol 20 (4) ◽  
pp. 984-989
Author(s):  
David M. French ◽  
Roswell H. Ewart
Keyword(s):  
Molecular Weight ◽  
Molecular Weights ◽  
Hydrocarbon Solvents ◽  
The Relationship

Abstract Osmotic molecular weight measurements have been made on a sample of unfractionated GR-S and on eight fractions of this material. The molecular weights ranged from 10,000 to approximately 1,000,000, with a number average at 92,000. The relationship between molecular weight and viscosity for GR-S was determined. A simple all-glass osmometer for use in hydrocarbon solvents is described, and information on its use and the membranes employed is given.

scholarly journals Anticoagulant Properties of a Green Algal Rhamnan-type Sulfated Polysaccharide and Its Low-molecular-weight Fragments Prepared by Mild Acid Degradation

Marine Drugs ◽  
2018 ◽  
Vol 16 (11) ◽  
pp. 445 ◽  
Author(s):  
Xue Liu ◽  
Peng Du ◽  
Xiao Liu ◽  
Sujian Cao ◽  
Ling Qin ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Anticoagulant Activity ◽  
Sulfated Polysaccharide ◽  
Low Molecular Weight ◽  
Thrombin Time ◽  
Acid Degradation ◽  
Molecular Weights ◽  
Green Algal

The active sulfated polysaccharide from seaweed possesses important pharmaceutical and biomedical potential. In the study, Monostroma sulfated polysaccharide (MSP) was obtained from Monostroma angicava, and the low-molecular-weight fragments of MSP (MSP-Fs: MSP-F1–MSP-F6) were prepared by controlled acid degradation. The molecular weights of MSP and MSP-F1–MSP-F6 were 335 kDa, 240 kDa, 90 kDa, 40 kDa, 24 kDa, 12 kDa, and 6.8 kDa, respectively. The polysaccharides were sulfated rhamnans that consisted of →3)-α-l-Rhap-(1→ and →2)-α-l-Rhap-(1→ units with partial sulfation at C-2 of →3)-α-l-Rhap-(1→ and C-3 of →2)-α-l-Rhap-(1→. Anticoagulant properties in vitro of MSP and MSP-F1–MSP-F6 were evaluated by studying the activated partial thromboplastin time, thrombin time, and prothrombin time. Anticoagulant activities in vivo of MSP and MSP-F4 were further evaluated; their fibrin(ogen)olytic activities in vivo and thrombolytic properties in vitro were also assessed by D-dimer, fibrin degradation products, plasminogen activator inhibitior-1, and clot lytic rate assays. The results showed that MSP and MSP-F1–MSP-F4 with molecular weights of 24–240 kDa had strong anticoagulant activities. A decrease in the molecular weight of MSP-Fs was accompanied by a decrease in the anticoagulant activity, and higher anticoagulant activity requires a molecular weight of over 12 kDa. MSP and MSP-F4 possessed strong anticoagulant activities in vivo, as well as high fibrin(ogen)olytic and thrombolytic activities. MSP and MSP-F4 have potential as drug or helpful food supplements for human health.

scholarly journals Human Endothelial Cells in Culture and In Vivo Express on Their Surface All Four Components of the Glycoprotein Ib/IX/V Complex

Blood ◽  
1997 ◽  
Vol 90 (7) ◽  
pp. 2660-2669 ◽  
Author(s):  
Guoxin Wu ◽  
David W. Essex ◽  
Frank J. Meloni ◽  
Toshiro Takafuta ◽  
Kingo Fujimura ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Endothelial Cells ◽  
Umbilical Vein ◽  
Platelet Glycoprotein ◽  
Glycoprotein Ib ◽  
Molecular Weights ◽  
Hel Cells ◽  
Umbilical Vein Endothelial Cells ◽  
Von Willebrand

The platelet glycoprotein Ib (GpIb) complex is composed of four polypeptides: the disulfide-linked GpIbα and GpIbβ and the noncovalently associated GpIX and GpV. GpIbα contains binding sites for von Willebrand factor and for thrombin and mediates platelet adhesion to the subendothelium under conditions of high shear stress. We have previously shown the presence of GpIbα and GpIbβ mRNA and protein in cultured human umbilical vein endothelial cells (HUVECs) as well as the presence of GpIbα mRNA and protein in tonsillar endothelium. We, therefore, probed ECs for the presence of the other components of the GpIb/IX/V complex. We have identified the presence of GpIX and GpV mRNA in cultured HUVEC monolayers. The sequence of HUVEC GpIX cDNA was identical to the previously published human erythroleukemia (HEL) cell GpIX cDNA sequence. Two species of GpV mRNA, one of 3 kb and one of 4.4 kb, were found in HUVECs, whereas HEL cells displayed only the 4.4-kb species and the megakaryocytic cell line CHRF-288 contained only the 3-kb species. We previously showed that EC GpIbα protein is identical in molecular weight to platelet GpIbα. HUVEC GpIbβ, in contrast to its platelet counterpart, has a molecular weight of 50 kD and forms a correspondingly larger disulfide-bonded complex with EC GpIbα. The molecular weights of GpIX and GpV were 22 and 88 kD, respectively, identical to the corresponding platelet polypeptides. Furthermore, we have identified all four components of the complex in tonsillar vessels. Using flow cytometry, we have established that all four polypeptides of the GpIb/IX/V complex are expressed on the surface membranes of cultured HUVECs and adult aortic ECs. Furthermore, using two-color fluorescence, we have shown that all ECs expressing GpIbα also express GpIX and GpV on their surface. The ratio of GpIbα:GpIX:GpV is 1:1:0.5, which is identical to the ratio present in platelets. None of the polypeptides of the GpIb complex could be identified on the surface of human smooth muscle cells or lymphocytes. The presence of all members of the GpIb complex in the EC membrane suggests that this complex may play a role in endothelial function in vivo.

scholarly journals Characterization of proteins from the cytoskeleton of Giardia lamblia

1983 ◽  
Vol 59 (1) ◽  
pp. 81-103 ◽  
Author(s):  
R. Crossley ◽  
D.V. Holberton
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Giardia Lamblia ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Molecular Size ◽  
Molecular Weights

Proteins from the axonemes and disc cytoskeleton of Giardia lamblia have been examined by sodium dodecyl sulphate/polyacrylamide gel electrophoresis. In addition to tubulin and the 30 X 10(3) molecular weight disc protein, at least 18 minor components copurify with the two major proteins in Triton-insoluble structures. The most prominent minor bands have the apparent molecular weights of 110 X 10(3), 95 X 10(3) and 81 X 10(3). Protein of 30 X 10(3) molecular weight accounts for about 20% of organelle protein on gels. In continuous 25 mM-Tris-glycine buffer it migrates mostly as a close-spaced doublet of polypeptides, which are here given the name giardins. Giardia tubulin and giardin have been purified by gel filtration chromatography in the presence of sodium dodecyl sulphate. Well-separated fractions were obtained that could be further characterized. Both proteins are heterogeneous when examined by isoelectric focusing. Five tubulin chains were detected by PAGE Blue 83 dye-binding after focusing in a broad-range ampholyte gel. Giardin is slightly less acidic than tubulin. On gels it splits into four major and four minor chains with isoelectric points in the pI range from 5.8 to 6.2. The amino acid composition of the giardin fraction has been determined, and compared to Giardia tubulin and a rat brain tubulin standard. Giardins are rich in helix-forming residues, particularly leucine. They have a low content of proline and glycine; therefore they may have extensive alpha-helical regions and be rod-shaped. As integral proteins of disc microribbons, giardins in vivo associate closely with tubulin. The properties of giardins indicate that in a number of respects - molecular size, charge, stoichiometry - their structural interaction with tubulin assemblies will be different from other tubulin-accessory protein copolymers studied in vitro.

FRACTIONATION OF LIVER SOMATOMEDIN ACTIVITY BY ULTRAFILTRATION

1974 ◽  
Vol 62 (2) ◽  
pp. 355-361 ◽  
Author(s):  
JENNIFER M. DEHNEL ◽  
P. D. McCONAGHEY ◽  
M. J. O. FRANCIS
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Weight Fraction ◽  
Low Molecular Weight ◽  
High Molecular Weight Fraction ◽  
Cartilage Growth ◽  
The Relationship ◽  
Somatomedin Inhibitors

SUMMARY Plasma somatomedin is the intermediary through which growth hormone (GH) exerts its effects on the growing skeleton. Somatomedin activity may be produced in vitro by perfusion of the liver and kidneys of rats with Waymouth's medium containing GH. The relationship between the activity of plasma somatomedin and somatomedin of hepatic and renal origin has yet to be clarified. Somatomedin from plasma can be separated into active fractions of both high and low molecular weight. Similarly, ultrafiltration of medium containing somatomedin of hepatic origin indicates the existence of two active fractions, one of high molecular weight (greater than 50000) and one of low molecular weight (less than 1000). The latter can be attributed to the release of amino acids, such as serine and glutamine, by the perfused tissue. The high molecular weight fraction is believed to represent GH-dependent somatomedin. Fractions that inhibit production of cartilage matrix are present in liver perfusates as well as in plasma. These results provide further evidence that the liver is a source of GH-dependent somatomedin in vivo. Furthermore, cartilage growth may be controlled not only by the GH-stimulated release of somatomedin by the liver, but also by its release of acid-labile somatomedin inhibitors.

Production of multiple forms of glucoamylase in Aspergillus awamori

1987 ◽  
Vol 65 (8) ◽  
pp. 762-765 ◽  
Author(s):  
Resham S. Bhella ◽  
Illimar Altosaar
Keyword(s):  
Molecular Weight ◽  
Northern Blot Analysis ◽  
De Novo ◽  
In Vitro Translation ◽  
Aspergillus Awamori ◽  
Multiple Forms ◽  
Molecular Weights ◽  
Specific Mrnas

The biosynthesis of glucoamylases in Aspergillus awamori was studied by in vivo protein labelling and analysis of glucoamylase-specific mRNAs. Two types of glucoamylases with molecular weights of 100 000 and 82 000 were shown to be synthesized de novo. Deglycosylation of the 100 000 molecular weight glucoamylase type resulted in the formation of another glucoamylase form with molecular weight of about 94 000. De novo synthesis of two types of glucoamylases was further confirmed by the existence of two types of glucoamylase-specific mRNAs, as demonstrated by in vitro translation and Northern blot analysis studies.

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