scholarly journals Identification of two intermediates during processing of profilaggrin to filaggrin in neonatal mouse epidermis.

1984 ◽  
Vol 99 (4) ◽  
pp. 1372-1378 ◽  
Author(s):  
K A Resing ◽  
K A Walsh ◽  
B A Dale
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Tandem Repeats ◽  
Peptide Mapping ◽  
Two Dimensional ◽  
Major Event ◽  
Mouse Epidermis ◽  
Cell Stage ◽  
Processing Steps

A major event in the keratinization of epidermis is the production of the histidine-rich protein filaggrin (26,000 mol wt) from its high molecular weight (greater than 350,000) phosphorylated precursor (profilaggrin). We have identified two nonphosphorylated intermediates (60,000 and 90,000 mol wt) in NaSCN extracts of epidermis from C57/Bl6 mice by in vivo pulse-chase studies. Results of peptide mapping using a two-dimensional technique suggest that these intermediates consist of either two or three copies of filaggrin domains. Each of the intermediates has been purified. The ratios of amino acids in the purified components are unusual and essentially identical. The data are discussed in terms of a precursor containing tandem repeats of similar domains. In vivo pulse-chase experiments demonstrate that the processing of the high molecular weight phosphorylated precursor involves dephosphorylation and proteolytic steps through three-domain and two-domain intermediates to filaggrin. These processing steps appear to occur as the cell goes through the transition cell stage to form a cornified cell.

Novel concatameric heparin-binding peptides reverse heparin and low-molecular-weight heparin anticoagulant activities in patient plasma in vitro and in rats in vivo

Blood ◽  
2004 ◽  
Vol 103 (4) ◽  
pp. 1356-1363 ◽  
Author(s):  
Barbara P. Schick ◽  
David Maslow ◽  
Adrianna Moshinski ◽  
James D. San Antonio
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight Heparin ◽  
Tandem Repeats ◽  
Factor Xa ◽  
Low Molecular Weight ◽  
Heparin Binding ◽  
High Affinity ◽  
Binding Peptides

Abstract Patients given unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH) for prophylaxis or treatment of thrombosis sometimes suffer serious bleeding. We showed previously that peptides containing 3 or more tandem repeats of heparin-binding consensus sequences have high affinity for LMWH and neutralize LMWH (enoxaparin) in vivo in rats and in vitro in citrate. We have now modified the (ARKKAAKA)n tandem repeat peptides by cyclization or by inclusion of hydrophobic tails or cysteines to promote multimerization. These peptides exhibit high-affinity binding to LMWH (dissociation constant [Kd], ≈ 50 nM), similar potencies in neutralizing anti–Factor Xa activity of UFH and enoxaparin added to normal plasma in vitro, and efficacy equivalent to or greater than protamine. Peptide (ARKKAAKA)3VLVLVLVL was most effective in all plasmas from enoxaparin-treated patients, and was 4- to 20-fold more effective than protamine. Several other peptide structures were effective in some patients' plasmas. All high-affinity peptides reversed inhibition of thrombin-induced clot formation by UFH. These peptides (1 mg/300 g rat) neutralized 1 U/mL anti–Factor Xa activity of enoxaparin in rats within 1 to 2 minutes. Direct blood pressure and heart rate measurements showed little or no hemodynamic effect. These heparin-binding peptides, singly or in combination, are potential candidates for clinical reversal of UFH and LMWH in humans.

Linear and high-molecular-weight poly-porphyrins for efficient photodynamic therapy

2021 ◽  
Author(s):  
Nan Zheng ◽  
Xiahui Li ◽  
Shangwei Huangfu ◽  
Kangkai Xia ◽  
Ruofei Yue ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Photodynamic Therapy ◽  
Quantum Yield ◽  
Singlet Oxygen ◽  
High Molecular Weight ◽  
Linear Poly ◽  
High Molecular Weight Poly

A linear poly-porphyrin with high Mw and conjugated by PEG and acetazolamide was developed with enhanced singlet oxygen quantum yield, improved photo-toxicity and excellent in vivo photodynamic therapy.

scholarly journals The interrelations between high- and low-molecular-weight forms of normal and mutant (Krabbe-disease) galactocerebrosidase

1980 ◽  
Vol 189 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Yoav Ben-Yoseph ◽  
Melinda Hungerford ◽  
Henry L. Nadler
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Active Form ◽  
Sodium Dodecyl ◽  
Krabbe Disease ◽  
Low Molecular Weight ◽  
Molecular Weight Form

Galactocerebrosidase (β-d-galactosyl-N-acylsphingosine galactohydrolase; EC 3.2.1.46) activity of brain and liver preparations from normal individuals and patients with Krabbe disease (globoid-cell leukodystrophy) have been separated by gel filtration into four different molecular-weight forms. The apparent mol.wts. were 760000±34000 and 121000±10000 for the high- and low-molecular-weight forms (peaks I and IV respectively) and 499000±22000 (mean±s.d.) and 256000±12000 for the intermediate forms (peaks II and III respectively). On examination by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the high- and low-molecular-weight forms revealed a single protein band with a similar mobility corresponding to a mol.wt. of about 125000. Antigenic identity was demonstrated between the various molecular-weight forms of the normal and the mutant galactocerebrosidases by using antisera against either the high- or the low-molecular-weight enzymes. The high-molecular-weight form of galactocerebrosidase was found to possess higher specific activity toward natural substrates when compared with the low-molecular-weight form. It is suggested that the high-molecular-weight enzyme is the active form in vivo and an aggregation process that proceeds from a monomer (mol.wt. approx. 125000) to a dimer (mol.wt. approx. 250000) and from the dimer to either a tetramer (mol.wt. approx. 500000) or a hexamer (mol.wt. approx. 750000) takes place in normal as well as in Krabbe-disease tissues.

scholarly journals Complex Formation of Covalently Crosslinked Fibrin Oligomers with Agarose Coupled Fibrinogen and Fibrin

1977 ◽  
Author(s):  
R. von Hugo ◽  
R. Hafter ◽  
A. Stemberger ◽  
H. Graeff
Keyword(s):  
Molecular Weight ◽  
Complex Formation ◽  
Affinity Chromatography ◽  
High Molecular Weight ◽  
Calcium Chloride ◽  
Gel Filtration ◽  
Void Volume ◽  
Soluble Fibrin ◽  
Derivatives Of

Crosslinked high molecular weight derivatives of fibrin (fibrinoligomers) were observed during intravascular coagulation. It was the purpose of this study to investigate the complex formation of fibrin oligomers with fibrinogen and fibrinmonomer. Fibrinogen coupled to agarose (Fg-ag) as well as fi-brinmonomer coupled to agarose (Fm-ag) was used as substrate. Soluble oligomers of fibrin were produced by incubating fibrinogen with thrombin, calcium-chloride, cystein and F XIII. They were separated from fibrinogen by gel filtration. Γ-dimers were demonstrated in fractions from the void volume and the shoulder prior to the fibrinogen peak. These fractions were subjected to affinity chromatography. Crosslinked oligomers of fibrin were not adsorbed on Fg-ag, yet adsorption occured on Fm-ag. This indicates that fibrin oligomers have no affinity to fibrinogen, yet readily form complexes with fibrin. This could mean that in vivo they compete with fibrinogen for the fibrinmonomer part of soluble fibrin monomer complexes, and hence have a tendency to increase in size.

In Vitro and in Vivo Antigen-Induced Release of High-Molecular Weight Neutrophil Chemotactic Activity from Human Nasal Tissue

1988 ◽  
Vol 2 (1) ◽  
pp. 7-11 ◽  
Author(s):  
T. Nagakura ◽  
T. Onda ◽  
Y. likura ◽  
T. Endo ◽  
H. Nagakura ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Nasal Polyps ◽  
Gel Filtration ◽  
Chemotactic Activity ◽  
Nasal Tissue ◽  
Nasal Secretions ◽  
Neutrophil Chemotactic Activity

High molecular weight neutrophil chemotactic activity has been identified in resected human nasal polyps, inferior turbinates, and nasal secretions following antigen challenge. The estimated molecular weight, by gel filtration chromatography, was approximately 600,000. However, a heterogeneity of molecular weight in some patients was recognized. Our results suggest a possible role for high molecular weight-neutrophil chemotactic activity in the pathogenesis of hypersensitivity in the human nasal cavity.

Nanometer size wear debris generated from ultra high molecular weight polyethylene in vivo

Wear ◽  
2009 ◽  
Vol 266 (1-2) ◽  
pp. 349-355 ◽  
Author(s):  
Monika Lapcikova ◽  
Miroslav Slouf ◽  
Jiri Dybal ◽  
Eva Zolotarevova ◽  
Gustav Entlicher ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Wear Debris ◽  
Nanometer Size ◽  
Ultra High Molecular Weight

scholarly journals Nanoparticles coated with high molecular weight PEG penetrate mucus and provide uniform vaginal and colorectal distribution in vivo

Nanomedicine ◽  
2016 ◽  
Vol 11 (11) ◽  
pp. 1337-1343 ◽  
Author(s):  
Katharina Maisel ◽  
Mihika Reddy ◽  
Qingguo Xu ◽  
Sumon Chattopadhyay ◽  
Richard Cone ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight

scholarly journals An Assessment of the Bioactivity of Coffee Silverskin Melanoidins

Foods ◽  
2019 ◽  
Vol 8 (2) ◽  
pp. 68 ◽  
Author(s):  
Silvia Tores de la Cruz ◽  
Amaia Iriondo-DeHond ◽  
Teresa Herrera ◽  
Yolanda Lopez-Tofiño ◽  
Carlos Galvez-Robleño ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Dietary Fiber ◽  
High Molecular Weight ◽  
Research Work ◽  
Weight Fraction ◽  
High Molecular Weight Fraction ◽  
Total Dietary Fiber ◽  
Coffee Silverskin

Melanoidins present in coffee silverskin, the only by-product of the roasting process, are formed via the Maillard reaction. The exact structure, biological properties, and mechanism of action of coffee silverskin melanoidins, remain unknown. This research work aimed to contribute to this novel knowledge. To achieve this goal, melanoidins were obtained from an aqueous extract of Arabica coffee silverskin (WO2013004873A1) and was isolated through ultrafiltration (>10 kDa). The isolation protocol was optimized and the chemical composition of the high molecular weight fraction (>10 kDa) was evaluated, by analyzing the content of protein, caffeine, chlorogenic acid, and the total dietary fiber. In addition, the structural analysis was performed by infrared spectroscopy. Antioxidant properties were studied in vitro and the fiber effect was studied in vivo, in healthy male Wistar rats. Melanoidins were administered to animals in the drinking water at a dose of 1 g/kg. At the fourth week of treatment, gastrointestinal motility was evaluated through non-invasive radiographic means. In conclusion, the isolation process was effective in obtaining a high molecular weight fraction, composed mainly of dietary fiber, including melanoidins, with in vitro antioxidant capacity and in vivo dietary fiber effects.

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