In Vivo and in Vitro Evidence for a Lysosomal Enzyme Uptake System in Macrophages

1980 ◽  
pp. 837-864 ◽  
Author(s):  
P. Stahl ◽  
R. Townsend ◽  
C. Tietze ◽  
P. Schlesinger ◽  
S. C. Silverstein ◽  
...  
Keyword(s):  
Lysosomal Enzyme ◽  
Uptake System

Stobadine inhibits lysosomal enzyme release in vivo and in vitro

Life Sciences ◽  
1999 ◽  
Vol 65 (18-19) ◽  
pp. 1905-1907 ◽  
Author(s):  
Jana Navarová ◽  
Tatiana Mačičková ◽  
Katarina Horáková ◽  
Miroslava Urbančíková
Keyword(s):  
Lysosomal Enzyme ◽  
Enzyme Release

Production of Peptides Inducing Chemotaxis and Lysosomal Enzyme Release in Human Neutrophils by Intestinal Bacteria in Vitro and in Vivo

1988 ◽  
Vol 23 (1) ◽  
pp. 121-128 ◽  
Author(s):  
V. S. Chadwick ◽  
D. M. Mellor ◽  
D. B. Myers ◽  
A. C. Selden ◽  
A. Keshavarzian ◽  
...  
Keyword(s):  
Lysosomal Enzyme ◽  
Intestinal Bacteria ◽  
Human Neutrophils ◽  
Enzyme Release

scholarly journals Analysis of pre- and postsynaptic factors of the serotonin system in rabbit retina.

1985 ◽  
Vol 100 (1) ◽  
pp. 64-73 ◽  
Author(s):  
C K Mitchell ◽  
D A Redburn
Keyword(s):  
Serotonin Receptor ◽  
Amacrine Cells ◽  
Uptake System ◽  
Rabbit Retina ◽  
Binding Studies ◽  
High Affinity ◽  
Serotonin System ◽  
Significant Difference

[3H]Serotonin is accumulated by a specific set of amacrine cells in the rabbit retina. These cells also accumulate the neurotoxin, 5,7-dihydroxytryptamine, and show signs of necrosis within 4 h of in vivo exposure to the drug. Biochemical analysis of [3H]serotonin uptake reveal a sodium- and temperature-dependent, high affinity uptake system with a Km of 0.94 microM and Vmax of 1.08 pmol/mg protein/min. [3H]Tryptophan is also accumulated in rabbit retinal homogenates by a high affinity process. Accumulated [3H]serotonin is released in response to potassium-induced depolarization of intact, isolated retinas. In vitro binding studies of rabbit retinal homogenate membranes demonstrate specific sets of binding sites with characteristics of the postsynaptic serotonin receptor. These data strongly suggest that rabbit retina contains virtually all of the molecular components required for a functional serotonergic neurotransmitter system. The only significant difference between the serotonin system in rabbit retina and that in the well-established serotonin transmitter systems in nonmammalin retinas and in brains of most species is the relatively low concentration of endogenous serotonin in rabbit retinas, as demonstrated by high-performance liquid chromatography, histofluorescence, or immunocytochemistry.

Insertion of a Lysosomal Enzyme Cleavage Site into the Sequence of a Radiolabeled Neuropeptide Influences Cell Trafficking In Vitro and In Vivo

2010 ◽  
Vol 25 (1) ◽  
pp. 89-95 ◽  
Author(s):  
Syed Ali Raza Naqvi ◽  
Torkjel Matzow ◽  
Ciara Finucane ◽  
Saeed A. Nagra ◽  
Malik M. Ishfaq ◽  
...  
Keyword(s):  
Lysosomal Enzyme ◽  
Cleavage Site ◽  
Cell Trafficking ◽  
Enzyme Cleavage ◽  
Enzyme Cleavage Site

scholarly journals EVALUATION OF IN VITRO IMMUNOMODULATORY ACTIVITY OF AQUEOUS AND ETHANOLIC EXTRACT OF EULOPHIA NUDA LINDL

2018 ◽  
Vol 11 (11) ◽  
pp. 352 ◽  
Author(s):  
Vanita Kanase ◽  
Diptesh T Patil
Keyword(s):  
Lysosomal Enzyme ◽  
Stimulation Index ◽  
Ethanolic Extract ◽  
In Vivo Studies ◽  
Phagocytic Index ◽  
Immunomodulatory Activity ◽  
Myeloperoxidase Activity ◽  
Enzyme Release

Objective: The aim of this study was to evaluate the in vitro immunomodulatory activity of aqueous and ethanolic extract of dried tubers of Eulophia nuda.Methods: Effect of both the extracts was evaluated at various concentrations (832–6.5 μg/ml) for secretion of mediators such as nitric oxide (NO), superoxide, lysosomal enzyme, and myeloperoxidase activity of isolated murine peritoneal macrophages.Results: The extracts showed stimulation of NO, statistically significant at 832 μg/ml (SI 1.739) for ENA and at 832 μg/ml (stimulation index [SI] 1.662) for ENE; significant stimulation on lysosomal enzyme release for ENA at 832 μg/ml (SI 1.404) and ENE at 832 μg/ml (SI 1.513); myeloperoxidase activity was statistically significant for ENA at 832 μg/ml (SI 1.728) and ENE at 832 μg/ml (SI 1.770).Conclusion: In vitro phagocytic index showed significant results and thus proving the need for confirmation through in vivo studies.

scholarly journals Involvement of Streptococcus gordonii Beta-Glucoside Metabolism Systems in Adhesion, Biofilm Formation, and In Vivo Gene Expression

2004 ◽  
Vol 186 (13) ◽  
pp. 4246-4253 ◽  
Author(s):  
Ali O. Kiliç ◽  
Lin Tao ◽  
Yongshu Zhang ◽  
Yu Lei ◽  
Ali Khammanivong ◽  
...  
Keyword(s):  
Biofilm Formation ◽  
Heart Valves ◽  
Sugar Uptake ◽  
Uptake System ◽  
Streptococcus Gordonii ◽  
Induced Genes ◽  
In Vitro Adhesion ◽  
Plastic Surfaces

ABSTRACT Streptococcus gordonii genes involved in beta-glucoside metabolism are induced in vivo on infected heart valves during experimental endocarditis and in vitro during biofilm formation on saliva-coated hydroxyapatite (sHA). To determine the roles of beta-glucoside metabolism systems in biofilm formation, the loci of these induced genes were analyzed. To confirm the function of genes in each locus, strains were constructed with gene inactivation, deletion, and/or reporter gene fusions. Four novel systems responsible for beta-glucoside metabolism were identified, including three phosphoenolpyruvate-dependent phosphotransferase systems (PTS) and a binding protein-dependent sugar uptake system for metabolizing multiple sugars, including beta-glucosides. Utilization of arbutin and esculin, aryl-beta-glucosides, was defective in some mutants. Esculin and oligochitosaccharides induced genes in one of the three beta-glucoside metabolism PTS and in four other genetic loci. Mutation of genes in any of the four systems affected in vitro adhesion to sHA, biofilm formation on plastic surfaces, and/or growth rate in liquid medium. Therefore, genes associated with beta-glucoside metabolism may regulate S. gordonii in vitro adhesion, biofilm formation, growth, and in vivo colonization.

scholarly journals A Capsular Polysaccharide-Specific Antibody Alters Streptococcus pneumoniae Gene Expression during Nasopharyngeal Colonization of Mice

2018 ◽  
Vol 86 (7) ◽  
Author(s):  
Christopher R. Doyle ◽  
Jee-Young Moon ◽  
Johanna P. Daily ◽  
Tao Wang ◽  
Liise-anne Pirofski
Keyword(s):  
Oxidative Stress ◽  
Gene Expression ◽  
Streptococcus Pneumoniae ◽  
Capsular Polysaccharide ◽  
Vaccine Development ◽  
Lavage Fluid ◽  
Uptake System ◽  
Content Type

ABSTRACT Pneumococcal conjugate vaccines (PCV) elicit opsonophagocytic (opsonic) antibodies to pneumococcal capsular polysaccharides (PPS) and reduce nasopharyngeal (NP) colonization by vaccine-included Streptococcus pneumoniae serotypes. However, nonopsonic antibodies may also be important for protection against pneumococcal disease. For example, 1E2, a mouse IgG1 monoclonal antibody (MAb) to the serotype 3 (ST3) PPS (PPS3), reduced ST3 NP colonization in mice and altered ST3 gene expression in vitro . Here, we determined whether 1E2 affects ST3 gene expression in vivo during colonization of mice by performing RNA sequencing on NP lavage fluid from ST3-infected mice treated with 1E2, a control MAb, or phosphate-buffered saline. Compared to the results for the controls, 1E2 significantly altered the expression of over 50 genes. It increased the expression of the piuBCDA operon, which encodes an iron uptake system, and decreased the expression of dpr , which encodes a protein critical for resistance to oxidative stress. 1E2-mediated effects on ST3 in vivo required divalent binding, as Fab fragments did not reduce NP colonization or alter ST3 gene expression. In vitro , 1E2 induced dose-dependent ST3 growth arrest and altered piuB and dpr expression, whereas an opsonic PPS3 MAb, 5F6, did not. 1E2-treated bacteria were more sensitive to hydrogen peroxide and the iron-requiring antibiotic streptonigrin, suggesting that 1E2 may increase iron import and enhance sensitivity to oxidative stress. Finally, 1E2 also induced rapid capsule shedding in vitro , suggesting that this may initiate 1E2-induced changes in sensitivity to oxidative stress and gene expression. Our data reveal a novel mechanism of direct, antibody-mediated antibacterial activity that could inform new directions in antipneumococcal therapy and vaccine development.

scholarly journals Astrocytic Swelling Due to Hypotonic or High K+ Medium Causes Inhibition of Glutamate and Aspartate Uptake and Increases Their Release

1995 ◽  
Vol 15 (3) ◽  
pp. 409-416 ◽  
Author(s):  
Harold K. Kimelberg ◽  
Eric Rutledge ◽  
Susan Goderie ◽  
Carol Charniga
Keyword(s):  
Short Circuit ◽  
Amino Acid Uptake ◽  
Significant Inhibition ◽  
Acid Uptake ◽  
Uptake System ◽  
Hypotonic Medium ◽  
Astrocytic Swelling ◽  
High K

Astrocytic swelling occurs readily in ischemia and traumatic brain injury (TBI) as part of the cytotoxic or cellular edema response. Ischemia is known to produce large extracellular increases in both [K+] and excitatory amino acids (EAA) in vivo, and astrocytic swelling in vitro leads to marked release of EAA. In this study we compared the effect of swelling due to hypotonic media and high K+ medium on the uptake and release of EAA by rat primary astrocyte cultures in vitro. In both cases, there was a significant inhibition of uptake of [3H]l-glutamate and [3H]d-aspartate, and increased release of preloaded [3H]d-aspartate. The kinetics of the increased efflux was very different in response to hypotonic or high K+ media. In hypotonic medium there was a rapid initial release followed by a decline in the rate of release over time. This release was independent of whether Na+ was present. Upon exposure to high K+ medium there was a slow progressive increase in release of [3H]d-aspartate, which never showed any subsequent decline until the media was returned to normal [K+]. In high K+ media there was also an initial transient increase in [3H]d-aspartate release, which we attribute to reversal of the amino acid uptake system. The increased release due to hypotonic medium was not affected by a drop in temperature from 37 to 26°C, while the increased release due to high K+ medium was completely inhibited. The decreased uptake and increased release of EAA when astrocytes swell will short-circuit a presumed important, protective uptake system for EAA and may contribute to the increased levels of extracellular EAA seen during ischemia, TBI, and other pathologic states.

scholarly journals Physiological Response of Corynebacterium glutamicum to Indole

2020 ◽  
Vol 8 (12) ◽  
pp. 1945
Author(s):  
Tatjana Walter ◽  
Kareen H. Veldmann ◽  
Susanne Götker ◽  
Tobias Busche ◽  
Christian Rückert ◽  
...  
Keyword(s):  
Corynebacterium Glutamicum ◽  
Intracellular Signaling ◽  
Physiological Response ◽  
Iron Reduction ◽  
Iron Homeostasis ◽  
Uptake System ◽  
Adaptive Laboratory Evolution ◽  
Mobility Shift

The aromatic heterocyclic compound indole is widely spread in nature. Due to its floral odor indole finds application in dairy, flavor, and fragrance products. Indole is an inter- and intracellular signaling molecule influencing cell division, sporulation, or virulence in some bacteria that synthesize it from tryptophan by tryptophanase. Corynebacterium glutamicum that is used for the industrial production of amino acids including tryptophan lacks tryptophanase. To test if indole is metabolized by C. glutamicum or has a regulatory role, the physiological response to indole by this bacterium was studied. As shown by RNAseq analysis, indole, which inhibited growth at low concentrations, increased expression of genes involved in the metabolism of iron, copper, and aromatic compounds. In part, this may be due to iron reduction as indole was shown to reduce Fe3+ to Fe2+ in the culture medium. Mutants with improved tolerance to indole were selected by adaptive laboratory evolution. Among the mutations identified by genome sequencing, mutations in three transcriptional regulator genes were demonstrated to be causal for increased indole tolerance. These code for the regulator of iron homeostasis DtxR, the regulator of oxidative stress response RosR, and the hitherto uncharacterized Cg3388. Gel mobility shift analysis revealed that Cg3388 binds to the intergenic region between its own gene and the iolT2-rhcM2D2 operon encoding inositol uptake system IolT2, maleylacetate reductase, and catechol 1,2-dioxygenase. Increased RNA levels of rhcM2 in a cg3388 deletion strain indicated that Cg3388 acts as repressor. Indole, hydroquinone, and 1,2,4-trihydroxybenzene may function as inducers of the iolT2-rhcM2D2 operon in vivo as they interfered with DNA binding of Cg3388 at physiological concentrations in vitro. Cg3388 was named IhtR.

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