scholarly journals CD80 Expression Correlates with IL-6 Production in THP-1-Like Macrophages Costimulated with LPS and Dialyzable Leukocyte Extract (Transferon®)

2019 ◽  
Vol 2019 ◽  
pp. 1-9 ◽  
Author(s):  
Alexis P. Jiménez-Uribe ◽  
Hugo Valencia-Martínez ◽  
Gregorio Carballo-Uicab ◽  
Luis Vallejo-Castillo ◽  
Emilio Medina-Rivero ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Flow Cytometry ◽  
Viral Infections ◽  
Surface Expression ◽  
Low Molecular Weight ◽  
Activated Macrophages ◽  
Therapeutic Properties ◽  
And Function ◽  
Complex Drug ◽  
Stimulation Of

Transferon® is a complex drug based on a mixture of low molecular weight peptides. This biotherapeutic is employed as a coadjuvant in clinical trials of several diseases, including viral infections and allergies. Given that macrophages play key roles in pathogen recognition, phagocytosis, processing, and antigen presentation, we evaluated the effect of Transferon® on phenotype and function of macrophage-like cells derived from THP-1 monocytes. We determined the surface expression of CD80 and CD86 by flow cytometry and IL-1β, TNF-α, and IL-6 levels by ELISA. Transferon® alone did not alter the steady state of PMA-differentiated macrophage-like THP-1 cells. On the contrary, simultaneous stimulation of cells with Transferon® and LPS elicited a significant increase in CD80 (P≤0.001) and CD86 (P≤0.001) expression, as well as in IL-6 production (P≤0.05) compared to the LPS control. CD80 expression and IL-6 production exhibited a positive correlation (r=0.6, P≤0.05) in cells exposed to Transferon® and LPS. Our results suggest that the administration of Transferon® induces the expression of costimulatory molecules and the secretion of cytokines in LPS-activated macrophages. Further studies are necessary to determine the implication of these findings in the therapeutic properties of Transferon®.

scholarly journals R-MC46 monoclonal antibody stimulates adhesion and phagocytosis by rat macrophages

2004 ◽  
Vol 61 (6) ◽  
pp. 581-588
Author(s):  
Sonja Gasic ◽  
Dragana Vucevic ◽  
Petar Popovic ◽  
Sasa Vasilijic ◽  
Miodrag Colic
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Western Blot ◽  
Biochemical Characterization ◽  
Antigen Expression ◽  
Peritoneal Macrophages ◽  
Low Molecular Weight ◽  
And Function ◽  
Stimulation Of

Background. In our previous experiments it was shown that R-MC46 monoclonal antibody (mAb), produced at our Institute, stimulated homotypic aggregation of rat granulocytes and production of proinflammatory cytokines. The aim of this study was to examine antigen expression and function, recognized by R-MC46 mAb on macrophages. Methods. The expression of R-MC46 antigen on thymic and peritoneal macrophages was investigated using immunocytochemistry and flow cytometry methods. Its biochemical characterization was performed by Western blot. The ability of R-MC46 mAb to modulate adhesion and phagocytosis by macrophages was studied by using co-culture experiments with autologous thymocytes. Results. R-MC46 mAb stained thymic macrophages more strongly than peritoneal macrophages. After in vivo treatment of peritoneal macrophages with Pristane, a significant up-regulation of the R-MC46 antigen expression was observed. Western blot analysis showed that the mAb recognized a low molecular weight antigen of about 5.5 kDa. R-MC46 mAb significantly enhanced binding and phagocytosis of thymocytes by both thymic and peritoneal macrophages. These processes were completely blocked by WT.3 (anti-CD18) mAb. The stimulation of binding thymocyte to macrophages was higher with the use of thymic macrophages,while the phagocytosis of these cells was higher in the presence of peritoneal macrophages. Conclusion. R-MC46 mAb recognized a new molecule expressed by rat macrophages. The antigen is most probably involved in ?2 integrin-mediated adhesion and phagocytosis, as well as proinflammatory functions of macrophages.

Functional design of glycan-conjugated molecules using a chemoenzymatic approach

2021 ◽  
Author(s):  
Makoto Ogata
Keyword(s):  
Molecular Weight ◽  
Large Scale ◽  
Biological Activities ◽  
Natural Compounds ◽  
Low Molecular Weight ◽  
Functional Design ◽  
Enzymatic Method ◽  
Conjugated Molecules ◽  
Design Synthesis ◽  
And Function

Abstract Carbohydrates play important and diverse roles in the fundamental processes of life. We have established a method for accurately and a large scale synthesis of functional carbohydrates with diverse properties using a unique enzymatic method. Furthermore, various artificial glycan-conjugated molecules have been developed by adding these synthetic carbohydrates to macromolecules and to middle and low molecular weight molecules with different properties. These glycan-conjugated molecules have biological activities comparable to or higher than those of natural compounds, and present unique functions. In this review, several synthetic glycan-conjugated molecules are taken as examples to show design, synthesis and function.

Polyamine metabolism and function

1982 ◽  
Vol 243 (5) ◽  
pp. C212-C221 ◽  
Author(s):  
A. E. Pegg ◽  
P. P. McCann
Keyword(s):  
Molecular Weight ◽  
Tissue Growth ◽  
Polyamine Metabolism ◽  
Organic Cations ◽  
Low Molecular Weight ◽  
Polyamine Biosynthesis ◽  
Polyamine Content ◽  
And Function ◽  
Specific Inhibitors

Polyamines are ubiquitous organic cations of low molecular weight. The content of these amines is closely regulated by the cell according to the state of growth. The reactions responsible for the biosynthesis and interconversion of the polyamines and their precursor putrescine are described and the means by which polyamine content can be varied in response to exogenous stimuli are discussed. The role of polyamines in the cell cycle, cell division, tissue growth, and differentiation is considered. Recent studies using highly specific inhibitors of polyamine biosynthesis such as alpha-difluoromethylornithine to prevent accumulation of polyamines have indicated that the synthesis of polyamines is intimately associated with these processes. Such inhibitors have great potential for investigation of the cellular role of polyamines.

Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor

1987 ◽  
Vol 247 (1) ◽  
pp. 187-193 ◽  
Author(s):  
U. Rausch ◽  
G. Adler ◽  
H. Weidenbach ◽  
F. Weidenbach ◽  
D. Rudolff ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Secretory Process ◽  
Low Molecular Weight ◽  
Stimulation Of

scholarly journals Incidental Detection of Dent-2 Disease in an Infant with Febrile Proteinuria

2018 ◽  
Vol 27 (4) ◽  
pp. 392-395 ◽  
Author(s):  
Shpetim Salihu ◽  
Katerina Tosheska ◽  
Svetlana Cekovska ◽  
Velibor Tasic
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Clinical Presentation ◽  
Viral Infections ◽  
Sodium Dodecyl ◽  
Febrile Illness ◽  
Low Molecular Weight ◽  
Acute Febrile Illness ◽  
Low Molecular Weight Proteinuria ◽  
Sds Page

Objective: Febrile proteinuria is functional proteinuria and is seen as a transitory phenomenon during acute febrile illness, mainly viral infections. It is a benign phenomenon and clears promptly with resolution of the infection. Clinical Presentation and Intervention: In this report, we present a patient who was thought to have febrile proteinuria. Persistence of significant proteinuria after resolution of the infection prompted biochemical and genetic workup which led to the diagnosis of Dent-2 disease. Conclusion: We recommend the use of SDS-PAGE (sodium dodecyl sulfate electropheresis) for the detection of low molecular weight proteinuria.

scholarly journals In Vitro Evaluation of the Effects of Cadmium on Endocytic Uptakes of Proteins into Cultured Proximal Tubule Epithelial Cells

Toxics ◽  
2020 ◽  
Vol 8 (2) ◽  
pp. 24
Author(s):  
Hitomi Fujishiro ◽  
Hazuki Yamamoto ◽  
Nobuki Otera ◽  
Nanae Oka ◽  
Mei Jinno ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Flow Cytometry ◽  
Tubular Reabsorption ◽  
In Vitro Assay ◽  
Low Molecular Weight ◽  
S2 Cells ◽  
Vitro Assay ◽  
Renal Tubular ◽  
Low Molecular Weight Proteins

Cadmium (Cd) is an environmental pollutant known to cause dysfunctions of the tubular reabsorption of biomolecules in the kidney. Elevated levels of urinary excretion of low-molecular-weight proteins such as β2-microglobulin (β2-MG) have been used as an indicator of Cd-induced renal tubular dysfunctions. However, very few studies have examined the direct effects of Cd on the reabsorption efficiency of proteins using cultured renal cells. Here, we developed an in vitro assay system for quantifying the endocytic uptakes of fluorescent-labeled proteins by flow cytometry in S1 and S2 cells derived from mouse kidney proximal tubules. Endocytic uptakes of fluorescent-labeled albumin, transferrin, β2-MG, and metallothionein into S1 cells were confirmed by fluorescence imaging and flow cytometry. The exposure of S1 and S2 cells to Cd at 1 and 3 µM for 3 days resulted in significant decreases in the uptakes of β2-MG and metallothionein but not in those of albumin or transferrin. These results suggest that Cd affects the tubular reabsorption of low-molecular-weight proteins even at nonlethal concentrations. The in vitro assay system developed in this study to evaluate the endocytic uptakes of proteins may serve as a useful tool for detecting toxicants that cause renal tubular dysfunctions.

scholarly journals Characterization of 83-kilodalton nonmuscle caldesmon from cultured rat cells: stimulation of actin binding of nonmuscle tropomyosin and periodic localization along microfilaments like tropomyosin.

1988 ◽  
Vol 106 (6) ◽  
pp. 1973-1983 ◽  
Author(s):  
S Yamashiro-Matsumura ◽  
F Matsumura
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Actin Filaments ◽  
Binding Constant ◽  
Reducing Agents ◽  
Actin Binding ◽  
Low Molecular Weight ◽  
Tropomyosin Isoforms ◽  
Apparent Binding Constant ◽  
Stimulation Of

Nonmuscle caldesmon purified from cultured rat cells shows a molecular weight of 83,000 on SDS gels, Stokes radius of 60.5 A, and sedimentation coefficient (S20,w) of 3.5 in the presence of reducing agents. These values give a native molecular weight of 87,000 and a frictional ratio of 2.04, suggesting that the molecule is a monomeric, asymmetric protein. In the absence of reducing agents, the protein is self-associated, through disulfide bonds, into oligomers with a molecular weight of 230,000 on SDS gels. These S-S oligomers appear to be responsible for the actin-bundling activity of nonmuscle caldesmon in the absence of reducing agents. Actin binding is saturated at a molar ratio of one 83-kD protein to six actins with an apparent binding constant of 5 X 10(6) M-1. Because of 83-kD nonmuscle caldesmon and tropomyosin are colocalized in stress fibers of cultured cells, we have examined effects of 83-kD protein on the actin binding of cultured cell tropomyosin. Of five isoforms of cultured rat cell tropomyosin, tropomyosin isoforms with high molecular weight values (40,000 and 36,500) show higher affinity to actin than do tropomyosin isoforms with low molecular weight values (32,400 and 32,000) (Matsumura, F., and S. Yamashiro-Matsumura. 1986. J. Biol. Chem. 260:13851-13859). At physiological concentration of KCl (100 mM), 83-kD nonmuscle caldesmon stimulates binding of low molecular weight tropomyosins to actin and increases the apparent binding constant (Ka from 4.4 X 10(5) to 1.5 X 10(6) M-1. In contrast, 83-kD protein has slight stimulation of actin binding of high molecular weight tropomyosins because high molecular weight tropomyosins bind to actin strongly in this condition. As the binding of 83-kD protein to actin is regulated by calcium/calmodulin, 83-kD protein regulates the binding of low molecular weight tropomyosins to actin in a calcium/calmodulin-dependent way. Using monoclonal antibodies to visualize nonmuscle caldesmon along microfilaments or actin filaments reconstituted with purified 83-kD protein, we demonstrate that 83-kD nonmuscle caldesmon is localized periodically along microfilaments or actin filaments with similar periodicity (36 +/- 4 nm) as tropomyosin. These results suggest that 83-kD protein plays an important role in the organization of microfilaments, as well as the control of the motility, through the regulation of the binding of tropomyosin to actin.

scholarly journals Bioorganic studies on the venom from duckbill platypus

2012 ◽  
Vol 84 (6) ◽  
pp. 1317-1328 ◽  
Author(s):  
Masaki Kita
Keyword(s):  
Molecular Weight ◽  
Guinea Pig ◽  
Structure And Function ◽  
Low Molecular Weight ◽  
Tissue Kallikrein ◽  
Guinea Pig Ileum ◽  
Porcine Pancreas ◽  
Human Neuroblastoma ◽  
Ornithorhynchus Anatinus ◽  
And Function

Venomous mammals are rare, and only a few species in the orders Insectivora and Monotremata produce toxic venom. Among them, the duckbill platypus (Ornithorhynchus anatinus) is one of the two venomous Australian mammals. The adult male platypus carries a spur on each hind leg, which it uses to inject competitors with poison. However, the structure and function of the poison’s active compounds are still imcompletely characterized. We found that crude platypus venom produced potent Ca2+influx in human neuroblastoma IMR-32 cells. Guided by this assay, we identified 11 unique peptides, including peptide H–His–Asp–His–Pro–Asn–Pro–Arg–OH, which coincided with the N-terminal domain residues ofOrnithorhynchusvenom C-type natriuretic peptide (OvCNP). This heptapeptide induced a significant increase in [Ca2+]iin IMR-32 cells at 75 μM; had relatively specific affinities for glutamate, histamine, and GABAAreceptors; and facilitated neurogenic twitching in guinea pig ileum specimens at 30 μM. We also established that its proteinous venom fraction strongly hydrolyzed Pro–Phe–Arg–MCA and cleaved a human low-molecular-weight kininogen (LK), similar to porcine pancreas kallikrein. These results strongly indicated that platypus venom contains tissue kallikrein-like protease(s), and its proteolytic activity might synergistically contribute to toxicity through the specific cleavage of other venom constituents.

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