R-Phycoerythrin from Colaconema formosanum (Rhodophyta), an Anti-Allergic and Collagen Promoting Material for Cosmeceuticals

2021 ◽  
Vol 11 (20) ◽  
pp. 9425
Author(s):  
Po-Tsang Lee ◽  
Han-Yang Yeh ◽  
Wei-Qing-Chloe Lung ◽  
Jing Huang ◽  
Yi-Jung Chen ◽  
...  
Keyword(s):  
Cell Lines ◽  
Mammalian Cell ◽  
Calcium Ionophore ◽  
Calcium Ionophore A23187 ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Suppression Effect ◽  
Mammalian Cell Lines ◽  
Pigment Complex ◽  
Nih 3T3

R-phycoerythrin (R-PE), a pigment complex found in red algae, was extracted and purified from a newly identified red alga, Colaconema formosanum, and its bioactivities were examined. It was revealed that R-PE treatment resulted in high cell viability (>70%) to the mammalian cell lines NIH-3T3, RBL-2H3, RAW264.7, and Hs68, and had no effect on cell morphology in NIH-3T3 cells. Its suppression effect was insignificant on the production of IL-6 and TNF-α in lipopolysaccharides-stimulated RAW264.7 cells. However, calcium ionophore A23187-induced β-hexosaminidase release was effectively inhibited in a dose-dependent manner in RBL-2H3 cells. Additionally, it was revealed to be non-irritating to bionic epidermal tissues. Notably, procollagen production was promoted in Hs68 cells. Overall, the data revealed that R-PE purified from C. formosanum exhibits anti-allergic and anti-aging bioactivities with no observed consequential toxicity on multiple mammalian cell lines as well as epidermal tissues, suggesting that this macromolecule is a novel material for potential cosmetic use.

Immunologic mast cell-mediated responses and histamine release are attenuated by heparin

1992 ◽  
Vol 73 (3) ◽  
pp. 1093-1101 ◽  
Author(s):  
J. Lucio ◽  
J. D'Brot ◽  
C. B. Guo ◽  
W. M. Abraham ◽  
L. M. Lichtenstein ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Histamine Release ◽  
Immunoglobulin E ◽  
Specific Antigen ◽  
Calcium Ionophore ◽  
Intradermal Injection ◽  
Calcium Ionophore A23187 ◽  
Ionophore A23187 ◽  
Dependent Manner

Heparin has been shown to act as a competitive inhibitor of inositol 1,4,5-triphosphate (InsP3) receptors in various cell types. Because InsP3 is one of the second messengers involved in stimulus-secretion coupling in mast cells, it is possible that heparin may inhibit mast cell-mediated reactions. Therefore, in allergic sheep, we tested this hypothesis in two mast cell-mediated reactions induced by immunologic and nonimmunologic stimuli: immediate cutaneous reaction (ICR) and acute bronchoconstrictor response (ABR). In 12 sheep allergic to Ascaris suum antigen, the surface area of the skin wheal was determined 20 min after intradermal injection (0.05 ml) of increasing concentrations of specific antigen, compound 48/80, and histamine, without and after pretreatment with heparin (100, 300, or 1,000 U/kg i.v.). Antigen, compound 48/80, and histamine produced concentration-dependent increases in ICR. Heparin “partially” inhibited the ICR to antigen and compound 48/80 in a dose-dependent manner without modifying the ICR to histamine. The heparin preservative benzyl alcohol was ineffective. In 11 additional sheep, specific lung resistance was measured before and after inhalation challenges with antigen, compound 48/80, and histamine without and with aerosol heparin pretreatment (1,000 U/kg). Heparin blocked the antigen- and compound 48/80-induced bronchoconstriction without modifying the airway effects of histamine. In isolated human uterine mast cells, heparin inhibited the anti-immunoglobulin E- but not the calcium ionophore- (A23187) induced histamine release. These data suggest that heparin inhibits the ICR and ABR induced by stimuli that produce immunologic and nonimmunologic mast cell degranulation without attenuating the effects of histamine.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Stable Expression of a Hepatitis E Virus (HEV) RNA Replicon in Two Mammalian Cell Lines to Assess Mechanism of Innate Immunity and Antiviral Response

2020 ◽  
Vol 11 ◽  
Author(s):  
Ling-Dong Xu ◽  
Fei Zhang ◽  
Lei Peng ◽  
Wen-Ting Luo ◽  
Chu Chen ◽  
...  
Keyword(s):  
Cell Lines ◽  
Mammalian Cell ◽  
Hepatitis E Virus ◽  
Hepatitis E ◽  
Innate Immune ◽  
Type I ◽  
Dependent Manner ◽  
Genotype 3 ◽  
Mammalian Cell Lines ◽  
Rna Replicon

Hepatitis E virus (HEV) is one of the major etiological agents responsible for acute hepatitis. Hepatitis E virus does not replicate efficiently in mammalian cell cultures, thus a useful model that mimics persistent HEV replication is needed to dissect the molecular mechanism of pathogenesis. Here we report a genotype-3 HEV RNA replicon expressing an EGFP-Zeocin (EZ) resistant gene (p6-EZ) that persistently self-replicated in cell lines of human (Huh-7-S10-3) or hamster (BHK-21) origin after transfection with in vitro RNA transcripts and subsequent drug screening. Two cell lines, S10-3-EZ and BHK-21-EZ, stably expressed EGFP in the presence of Zeocin during continuous passages. Both genomic and subgenomic HEV RNAs and viral replicase proteins were stably expressed in persistent HEV replicon cells. The values of the cell models in antiviral testing, innate immune RNA sensing and type I IFN in host defense were further demonstrated. We revealed a role of RIG-I like receptor-interferon regulatory factor 3 in host antiviral innate immune sensing during HEV replication. We further demonstrated that treatment with interferon (IFN-α) or ribavirin significantly reduced expression of replicon RNA in a dose-dependent manner. The availability of the models will greatly facilitate HEV-specific antiviral development, and delineate mechanisms of HEV replication.

Ca2+-dependent Activation of the 33-kDa Protein Kinase Transmits Thrombin Receptor Signals in Human Platelets

1996 ◽  
Vol 76 (03) ◽  
pp. 439-443 ◽  
Author(s):  
Masaru Ido ◽  
Shinya Kato ◽  
Hiroyuki Ogawa ◽  
Kenji Hayashi ◽  
Yoshihiro Komada ◽  
...  
Keyword(s):  
Kinase Inhibitor ◽  
Calcium Ionophore ◽  
Structural Analog ◽  
Human Platelets ◽  
Calcium Ionophore A23187 ◽  
Similar Degree ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Serine Threonine Kinase ◽  
Acetoxymethyl Ester

SummaryThrombin stimulation induces a dramatic increase in the activity of the 33-kDa serine/threonine kinase (PK33) in human platelets (10). The Arg-Gly-Asp (RGD) peptide, an inhibitor of the thrombin-mediated aggregation of platelets, did not affect the PK33 activation induced by thrombin suggesting that the activation of this kinase occurs independently from platelet aggregation. To identify a potential role of Ca2+ and calmodulin in the regulation of PK33, the effect of several Ca2+/calmodulin inhibitors on the thrombin-induced activation of PK33 was assessed using denaturation/renaturation method. Pretreatment of platelets with EGTA decreased the maximum PK33 activity induced by thrombin. The chelation of both the extra- and the intracellular Ca2+ by EGTA and by acetoxymethyl ester of 5,5′ -dimethyl-bis-(<9-aminophen-oxy) ethane-N,N,N′,N′-tetraacetic acid (BAPTA-AM) decreased further the PK33 activation by thrombin. Preincubation of platelets with the anticalmodulin agent, N-(4-aminobutyl)-5-chloro-2-naphtha-lenesulfonamide (W13), inhibited markedly the activation of PK33 by thrombin, whereas the inactive structural analog N-(4-aminobutyl)-2-naphthalenesulfonamide (W12) and the myosin light chain kinase inhibitor 1 -(5-chloronaphthalene-1 -sulfonyl)-1 H-hexahydro-1,4-diaze-pine (ML9) showed very weak inhibitory effects. Treatment of resting platelets with the calcium ionophore, A23187, activated PK33 in a dose-dependent manner; phorbol 12-myristate 13-acetate enhanced this effect. However, the two foregoing agents did not induce similar degree of PK33 activities as thrombin. These results indicate that the activation of PK33 is independent of the formation of the GPIIb/IIIa-fibrinogen complex and that it might be regulated by a Ca2+-dependent pathway.

scholarly journals The Role of Rhodomyrtus tomentosa (Aiton) Hassk. Fruits in Downregulation of Mast Cells-Mediated Allergic Responses

2019 ◽  
Vol 2019 ◽  
pp. 1-7 ◽  
Author(s):  
Thanh Sang Vo ◽  
Young-Sang Kim ◽  
Dai-Nghiep Ngo ◽  
Dai-Hung Ngo
Keyword(s):  
Mast Cells ◽  
Biological Activities ◽  
Interleukin 1 ◽  
Reactive Oxygen Species Generation ◽  
Calcium Ionophore ◽  
Calcium Ionophore A23187 ◽  
Flowering Plant ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Rhodomyrtus Tomentosa

Rhodomyrtus tomentosa, a flowering plant of Myrtaceae family from southern and southeastern Asia, was known to possess a rich source of structurally diverse and various biological activities. In this study, the inhibitory effect of R. tomentosa fruit extract (RFE) on allergic responses in calcium ionophore A23187-activated RBL-2H3 mast cells was investigated. The result showed that RFE was able to inhibit mast cell degranulation via decreasing β-hexosaminidase release and intracellular Ca2+ elevation at the concentration of 400 μg/ml. Moreover, the suppressive effects of RFE on the production of interleukin-1β (IL-1β) and tumor necrosis factor-α (TNF-α) were evidenced. In addition, RFE effectively scavenged DPPH radical and suppressed the reactive oxygen species generation in a dose-dependent manner. Notably, the pretreatment of RFE caused the downregulation of tyrosine kinase Fyn phospholipid enzyme phospholipase Cγ (PLCγ), extracellular-signal-regulated kinase (ERK), and nuclear factor kappa B (NF-κB) phosphorylation. These results indicated that RFE could be a promising inhibitor of allergic responses and may be developed as bioactive ingredient for prevention or treatment of allergic diseases.

Canine jejunal submucosa cultures: characterization and release of neural somatostatin

1990 ◽  
Vol 68 (6) ◽  
pp. 705-710 ◽  
Author(s):  
A. M. J. Buchan ◽  
A. D. Doyle ◽  
E. Accili
Keyword(s):  
Substance P ◽  
Calcium Ionophore ◽  
Calcium Ionophore A23187 ◽  
Neuronal Cultures ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Cell Content ◽  
Cell Extracts

A primary culture of the canine jejunal submucosa has been established and used to investigate neuronal somatostatin release. Immunocytochemical characterization of the cultures demonstrated the presence of the following peptidergic neurons: neurotensin (30%), somatostatin (27%), vasoactive intestinal polypeptide (14%), neuropeptide Y (10%), and substance P (5%). No immunoreactive neurons were observed with the available antisera to galanin, gastrin-releasing peptide, and motilin. The concentration of somatostatin-like immunoreactivity, as determined by radioimmunoassay of cell extracts, was 358 ± 105 pmol/well. Basal release of somatostatin was 4.4 ± 0.9% total cell content and was significantly inhibited by the addition of substance P at 1 and 100 nM. The addition of the calcium ionophore, A23187, with phorbol 12-myristate 13-acetate stimulated somatostatin release in a concentration-dependent manner. These data indicate that short-term cultures of the jejunal submucosal plexus will be an excellent model for determination of the factors influencing the release of neural somatostatin.Key words: immunocytochemistry, neuronal cultures, neurofilament, substance P.

Inhibition of Human Platelet Functions by Verapamil

1981 ◽  
Vol 45 (02) ◽  
pp. 158-161 ◽  
Author(s):  
Y Ikeda ◽  
M Kikuchi ◽  
K Toyama ◽  
K Watanabe ◽  
Y Ando
Keyword(s):  
Platelet Aggregation ◽  
Calcium Ionophore ◽  
Serotonin Release ◽  
Calcium Ionophore A23187 ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Dependent Inhibition ◽  
Platelet Functions

SummaryThe effects of verapamil, a coronary vasodilator, on platelet functions were studied.Platelet aggregation induced by ADP, epinephrine or collagen was inhibited by verapamil in vitro. Calcium ionophore A23187-induced platelet aggregation was also inhibited by verapamil in a concentration dependent manner. In washed platelets, verapamil caused a dose-dependent inhibition of serotonin release induced either by thrombin or A23187 in the absence of extracellular calcium. Addition of 1 mM CaCl2 with A23187 or thrombin partially overcame this inhibition. Addition of 1 mM CaCl2 in the absence of verapamil had no effect on thrombin- or A23187-induced secretion. When verapamil was administered to the healthy volunteers at the dosage commonly used, inhibition of platelet aggregation was observed 2 hrs after the drug ingestion. It is of great interest that verapamil potentiated the anti-aggregating activity of prostacyclin in vitro.Our results may suggest a potential role for verapamil in the treatment of thrombotic disorders.

scholarly journals Mechanical stimulation induces formin-dependent assembly of a perinuclear actin rim

2015 ◽  
Vol 112 (20) ◽  
pp. E2595-E2601 ◽  
Author(s):  
Xiaowei Shao ◽  
Qingsen Li ◽  
Alex Mogilner ◽  
Alexander D. Bershadsky ◽  
G. V. Shivashankar
Keyword(s):  
Actin Polymerization ◽  
Genetic Diseases ◽  
Calcium Ionophore ◽  
Calcium Ionophore A23187 ◽  
Actin Dynamics ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Mechanical Stimuli ◽  
Actin Assembly ◽  
Force Application

Cells constantly sense and respond to mechanical signals by reorganizing their actin cytoskeleton. Although a number of studies have explored the effects of mechanical stimuli on actin dynamics, the immediate response of actin after force application has not been studied. We designed a method to monitor the spatiotemporal reorganization of actin after cell stimulation by local force application. We found that force could induce transient actin accumulation in the perinuclear region within ∼2 min. This actin reorganization was triggered by an intracellular Ca2+ burst induced by force application. Treatment with the calcium ionophore A23187 recapitulated the force-induced perinuclear actin remodeling. Blocking of actin polymerization abolished this process. Overexpression of Klarsicht, ANC-1, Syne Homology (KASH) domain to displace nesprins from the nuclear envelope did not abolish Ca2+-dependent perinuclear actin assembly. However, the endoplasmic reticulum- and nuclear membrane-associated inverted formin-2 (INF2), a potent actin polymerization activator (mutations of which are associated with several genetic diseases), was found to be important for perinuclear actin assembly. The perinuclear actin rim structure colocalized with INF2 on stimulation, and INF2 depletion resulted in attenuation of the rim formation. Our study suggests that cells can respond rapidly to external force by remodeling perinuclear actin in a unique Ca2+- and INF2-dependent manner.

scholarly journals Increased expression of procoagulant activity on the surface of human platelets exposed to heavy-metal compounds

1995 ◽  
Vol 308 (1) ◽  
pp. 15-21 ◽  
Author(s):  
C A Goodwin ◽  
C P D Wheeler-Jones ◽  
S Namiranian ◽  
S Bokkala ◽  
V V Kakkar ◽  
...  
Keyword(s):  
Heavy Metal ◽  
Calcium Ionophore ◽  
Calcium Ionophore A23187 ◽  
Procoagulant Activity ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Anionic Phospholipid ◽  
Metal Compounds ◽  
Platelet Surface ◽  
Thrombin Formation

One of the essential roles for platelets in haemostasis is in the potentiation of blood clotting due to the contribution of anionic phospholipid from the surface of the cells, as an essential cofactor to the proteolytic reactions of coagulation (platelet procoagulant activity). Only a limited number of agonists are known to initiate platelet procoagulant activity. In this study the rate of thrombin formation on the platelet surface was observed to increase in a dose-dependent manner upon treatment of washed platelets with heavy-metal compounds. Unlike the immediate increase observed upon treatment of platelets with calcium ionophore, A23187, the change due to these agents was progressive, approaching a maximum after 10 min. The maximum-fold acceleration of the rate of thrombin formation compared with control platelets was calculated for HgCl2 (56-fold), AgNO3 (42-fold) phenylmercuriacetate (24-fold) and thimerosal (14-fold), compared with 70-fold observed for calcium ionophore. The increase in procoagulant activity due to HgCl2 coincided with a large increase in intracellular calcium and phosphorylation of 22 and 45 kDa proteins. It is considered that the mechanism responsible for the increase in procoagulant activity is exposure of anionic phospholipids. This was detected by a 2-fold increase in the binding of 125I-annexin V upon addition of HgCl2, compared with resting platelets (3-fold on treatment of platelets with calcium ionophore). In contrast to the generation of activity by A23187 and other known agonists of this reaction, heavy-metal compounds appeared to cause little or no release of microparticles from the platelet surface. Since HgCl2 did not cause aggregation of platelets or significant release of serotinin, these findings may give further support to the need for exposure and ligation of glycoprotein IIb:IIIa for vesiculization to occur. Treatment of platelets with heavy metals may constitute a new approach to investigating the early changes in the cell membrane which lead to increased expression of anionic phospholipid.

Effect of the calcium ionophore A23187 on superoxide generation in phorbol ester stimulated human neutrophils

1985 ◽  
Vol 63 (12) ◽  
pp. 1543-1546 ◽  
Author(s):  
Colette F. Strnad ◽  
Kenneth Wong
Keyword(s):  
Protein Kinase C ◽  
Calcium Ionophore ◽  
Calcium Ionophore A23187 ◽  
Superoxide Production ◽  
Human Neutrophils ◽  
Ionophore A23187 ◽  
Dependent Manner ◽  
Superoxide Generation ◽  
Kinase C ◽  
Dose Dependent

The calcium ionophore, A23187, and the tumor-promoting phorbol ester, phorbol 12-myristate 13-acetate (PMA), interacted synergistically to elicit an accelerated superoxide production response in human neutrophils. The lag period preceding PMA-induced superoxide generation was decreased in a dose-dependent manner by A23187 at a concentration range from 1.0 × 10−8 to 1.0 × 10−5 M. Superoxide production rate, however, was subject to biphasic effects. While the rate was potentiated in a dose-dependent manner at A23187 concentrations below 1.0 × 10−6 M, inhibitory influences became manifest at higher concentrations. Total superoxide production was subject to inhibitory effects, characterized by a mean inhibitory dose of 1.3 × 10−6 M. The synergistic interaction of A23187 with PMA is consistent with a role for protein kinase C in neutrophil activation. Inhibition at high A23187 concentrations appeared to result from the effects of elevated intracellular Ca2+ levels on either NADPH oxidase itself, or some step in the transduction process linking protein kinase C to the oxidase complex.

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