Parasites, Hosts and Diseases

"degranulation"

Original Article

Activation of MAPK Is Required for ROS Generation and Exocytosis in HMC-1 Cells Induced by Trichomonas vaginalis-Derived Secretory Products: Giimaa Narantsogt, Arim Min, Young Hee Nam, Young Ah Lee, Kyeong Ah Kim, Gurbadam Agvaandaram, Temuulen Dorjsuren, Jamel El-Benna, Myeong Heon Shin; Korean J Parasitol 2015;53(5):597-603.
Published online October 29, 2015; DOI: https://doi.org/10.3347/kjp.2015.53.5.597

Abstract
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Trichomonas vaginalis is a flagellated protozoan parasite that causes vaginitis and cervicitis in women and asymptomatic urethritis and prostatitis in men. Mast cells have been reported to be predominant in vaginal smears and vaginal walls of patients infected with T. vaginalis. Mitogen-activated protein kinase (MAPK), activated by various stimuli, have been shown to regulate the transcriptional activity of various cytokine genes in mast cells. In this study, we investigated whether MAPK is involved in ROS generation and exocytotic degranulation in HMC-1 cells induced by T. vaginalis-derived secretory products (TvSP). We found that TvSP induces the activation of MAPK and NADPH oxidase in HMC-1 cells. Stimulation with TvSP induced phosphorylation of MAPK and p47^phox in HMC-1 cells. Stimulation with TvSP also induced up-regulation of CD63, a marker for exocytosis, along the surfaces of human mast cells. Pretreatment with MAPK inhibitors strongly inhibited TvSP-induced ROS generation and exocytotic degranulation. Finally, our results suggest that TvSP induces intracellular ROS generation and exocytotic degranulation in HMC-1 via MAPK signaling.

Citations

Citations to this article as recorded by

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SNAP23-Dependent Surface Translocation of Leukotriene B 4 (LTB 4 ) Receptor 1 Is Essential for NOX2-Mediated Exocytotic Degranulation in Human Mast Cells Induced by Trichomonas vaginalis-Secrete
Arim Min, Young Ah Lee, Kyeong Ah Kim, Jamel El-Benna, Myeong Heon Shin, Judith A. Appleton
Infection and Immunity.2017;[Epub] CrossRef
Explore the variation of MMP3, JNK, p38 MAPKs, and autophagy at the early stage of osteoarthritis
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Brief Communications

A 27 kDa Cysteine Protease Secreted by Newly Excysted Paragonimus westermani Metacercariae Induces Superoxide Anion Production and Degranulation of Human Eosinophils: Young-Bae Chung, Hirohito Kita, Myeong Heon Shin; Korean J Parasitol 2008;46(2):95-99.
Published online June 20, 2008; DOI: https://doi.org/10.3347/kjp.2008.46.2.95

Abstract
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Eosinophil degranulation plays a crucial role in tissue inflammatory reactions associated with helminth parasitic infections and allergic diseases. Paragonimus westermani, a lung fluke causing human paragonimiasis, secretes a large amount of cysteine proteases, which are involved in nutrient uptake, tissue invasion, and modulation of hos's immune responses. There is, however, limited information about the response of eosinophils to direct stimulation by cysteine proteases (CP) secreted by P. westermani. In the present study, we tested whether degranulation and superoxide production from human eosinophils can be induced by stimulation of the 2 CP (27 kDa and 28 kDa) purified from excretory-secretory products (ESP) of P. westermani newly excysted metacercariae (PwNEM). A large quantity of eosinophil-derived neurotoxin (EDN) was detected in the culture supernatant when human eosinophils isolated from the peripheral blood were incubated with the purified 27 kDa CP. Furthermore, the 27 kDa CP induced superoxide anion production by eosinophils in time- and dose-dependent manners. In contrast, the purified 28 kDa CP did not induce superoxide production and degranulation. These findings suggest that the 27 kDa CP secreted by PwNEM induces superoxide production and degranulation of human eosinophils, which may be involved in eosinophil-mediated tissue inflammatory responses during the larval migration in human paragonimiasis.

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Degranulation of human eosinophils induced by Paragonimus westermani-secreted protease: Myeong Heon Shin, Young-Bae Chung, Hirohito Kita; Korean J Parasitol 2005;43(1):33-37.
Published online March 20, 2005; DOI: https://doi.org/10.3347/kjp.2005.43.1.33

Abstract
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Eosinophil degranulation is considered to be a key effector function for the killing of helminthic worms and tissue inflammation at worm-infected lesion sites. However, relatively little data are available with regard to eosinophil response after stimulation with worm-secreted products which contain a large quantity of cysteine proteases. In this study, we attempted to determine whether the degranulation of human eosinophils could be induced by the direct stimulation of the excretory-secretory products (ESP) of Paragonimus westermani, which causes pulmonary paragonimiasis in human beings. Incubation of eosinophils for 3 hr with Paragonimus-secreted products resulted in marked degranulation, as evidenced by the release of eosinophil-derived neurotoxin (EDN) in the culture supernatants. Moreover, superoxide anion was produced by eosinophils after stimulation of the ESP. The ESP-induced EDN release was found to be significantly inhibited when the ESP was pretreated with protease inhibitor cocktail or the cysteine protease inhibitor, E-64. These findings suggest that human eosinophils become degranulated in response to P. westermani-secreted proteases, which may contribute to in vivo tissue inflammation around the worms.

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Experimental Parasitology.2011; 127(3): 693. CrossRef
Eosinophil and Tissue-invasive Parasitic Helminth
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Hanyang Medical Reviews.2010; 30(3): 238. CrossRef
Eosinophil-Mediated Tissue Inflammatory Responses in Helminth Infection
Myeong Heon Shin, Young Ah Lee, Duk-Young Min
The Korean Journal of Parasitology.2009; 47(Suppl): S125. CrossRef
A 27 kDa Cysteine Protease Secreted by Newly Excysted Paragonimus westermani Metacercariae Induces Superoxide Anion Production and Degranulation of Human Eosinophils
Young-Bae Chung, Hirohito Kita, Myeong Heon Shin
The Korean Journal of Parasitology.2008; 46(2): 95. CrossRef
Cloning and characterization of cathepsin L-like peptidases of Echinococcus multilocularis metacestodes
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