scholarly journals Expression of Tocopherol-Associated Protein in Mast Cells

2004 ◽  
Vol 11 (6) ◽  
pp. 1189-1191 ◽  
Author(s):  
Teruo Ikeda ◽  
Masaru Murakami ◽  
Masayuki Funaba
Keyword(s):  
Mast Cells ◽  
Subcellular Localization ◽  
Physiological Role

ABSTRACT Tocopherol-associated protein (TAP) was expressed in mouse mast cells. TAP was predominantly localized in the cytoplasm, and the subcellular localization was not changed by α-tocopherol. The results suggest that the physiological role of TAP in mast cells is not regulation of tocopherol function but an as-yet-unidentified activity.

scholarly journals Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme

Antioxidants ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 357 ◽  
Author(s):  
Lucia A. Seale
Keyword(s):  
Amino Acid ◽  
Energy Metabolism ◽  
Subcellular Localization ◽  
Hepatic Steatosis ◽  
Glucose Intolerance ◽  
Physiological Role ◽  
Dependent Manner ◽  
Technical Approach ◽  
Expression And Activity

The enzyme selenocysteine β-lyase (SCLY) was first isolated in 1982 from pig livers, followed by its identification in bacteria. SCLY works as a homodimer, utilizing pyridoxal 5’-phosphate as a cofactor, and catalyzing the specific decomposition of the amino acid selenocysteine into alanine and selenide. The enzyme is thought to deliver its selenide as a substrate for selenophosphate synthetases, which will ultimately be reutilized in selenoprotein synthesis. SCLY subcellular localization is unresolved, as it has been observed both in the cytosol and in the nucleus depending on the technical approach used. The highest SCLY expression and activity in mammals is found in the liver and kidneys. Disruption of the Scly gene in mice led to obesity, hyperinsulinemia, glucose intolerance, and hepatic steatosis, with SCLY being suggested as a participant in the regulation of energy metabolism in a sex-dependent manner. With the physiological role of SCLY still not fully understood, this review attempts to discuss the available literature regarding SCLY in animals and provides avenues for possible future investigation.

Subcellular Localization of Quinate: Oxidoreductase from Phaseolus mungo L. Sprouts

1994 ◽  
Vol 49 (7-8) ◽  
pp. 415-420 ◽  
Author(s):  
Xiangbo Kang ◽  
H. Ekkehard Neuhaus ◽  
Renate Scheibe
Keyword(s):  
Subcellular Localization ◽  
Western Blotting ◽  
Mung Bean ◽  
Plant Material ◽  
Physiological Role ◽  
Single Band ◽  
Phaseolus Mungo ◽  
Monospecific Antiserum

Quinate:oxidoreductase (QORase, EC 1.1.1.24) was isolated and purified from etiolated mung bean (Phaseolus mungo L.) sprouts and a monospecific antiserum was raised in rabbit to the homogeneous protein. Highly intact etioplasts were isolated from the same plant material. The stroma of the purified etioplasts was enzymatically characterized. Contamination by cytosol, mitochondria and vacuole was estimated from activities of marker en­zymes. QORase activity was localized in the stroma (about 91% for both NAD+ and NADP+ as a cofactor). Western blotting and immunoprinting of the stroma proteins revealed a single band that migrated identically with the purified QORase. The results suggest that the QOR-ase is localized predominantly, if not exclusively, in the etioplast stroma. The physiological role of the enzyme is discussed

scholarly journals An Overview of the Physiological and Pathological Role of Mast Cells in the Central Nervous System

2020 ◽  
Vol 3 (1) ◽  
pp. 56-64
Author(s):  
Serghei Covantev ◽  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Mast Cells ◽  
Cerebrovascular Disorders ◽  
Physiological Role ◽  
Pharmaceutical Treatment ◽  
Central Nervous System Trauma ◽  
The Central Nervous System ◽  
Lateral Sclerosis

Neurological disorders present a major group of diseases with the global prevalence of 6.3%. They are responsible for 12% global mortality. Mast cells are one of the most abundantly present cell of the immune system in the connective tissue and the central nervous system is not an exception. In this article is presented a review of studies on mast cells regarding their physiological role in cental nervous system. We also disscuss their role in several conditions like: multiple sclerosis, amyotrophic lateral sclerosis, Alzheimer’s disease, neuropsychiatric disorders, cerebrovascular disorders and central nervous system trauma, epilepsy, seizures and tumors. Finally, we evaluate whether they can be used as a targed for pharmaceutical treatment.

scholarly journals Subcellular localization and physiological role of α-methylacyl-CoA racemase

2000 ◽  
Vol 41 (11) ◽  
pp. 1890-1896 ◽  
Author(s):  
Sacha Ferdinandusse ◽  
Simone Denis ◽  
Lodewijk IJlst ◽  
Georges Dacremont ◽  
Hans R. Waterham ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Physiological Role

Author response for "The role of galanin in the differentiation of mucosal mast cells in mice"

2019 ◽  
Author(s):  
Tomoko Yamaguchi ◽  
Yumi Ikeda ◽  
Katsuhisa Tashiro ◽  
Yasuyuki Ohkawa ◽  
Kenji Kawabata
Keyword(s):  
Mast Cells ◽  
Author Response ◽  
Mucosal Mast Cells

Thrombin Augments Vascular Cell-dependent Migration of Human Mast Cells: Role of MGF

1997 ◽  
Vol 77 (03) ◽  
pp. 577-584 ◽  
Author(s):  
Mehrdad Baghestanian ◽  
Roland Hofbauer ◽  
Hans G Kress ◽  
Johann Wojta ◽  
Astrid Fabry ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Mast Cells ◽  
Umbilical Vein ◽  
Vascular Cells ◽  
Migratory Response ◽  
Thrombin Activation ◽  
Umbilical Vein Endothelial Cells ◽  
Primary Tissue ◽  
Local Expression

SummaryRecent data suggest that auricular thrombosis is associated with accumulation of mast cells (MC) in the upper endocardium (where usually no MC reside) and local expression of MGF (mast cell growth factor) (25). In this study, the role of vascular cells, thrombin-activation and MGF, in MC-migration was analyzed. For this purpose, cultured human auricular endocardial cells (HAUEC), umbilical vein endothelial cells (HUVEC) and uterine-(HUTMEC) and skin-derived (HSMEC) microvascular endothelial cells were exposed to thrombin or control medium, and the migration of primary tissue MC (lung, n = 6) and HMC-1 cells (human MC-line) against vascular cells (supernatants) measured. Supernatants (24 h) of unstimulated vascular cells (monolayers of endocardium or endothelium) as well as recombinant (rh) MGF induced a significant migratory response in HMC-1 (control: 3025 ± 344 cells [100 ± 11.4%] vs. MGF, 100 ng/ml: 8806 ± 1019 [291 ± 34%] vs. HAUEC: 9703 ± 1506 [320.8 ± 49.8%] vs. HUTMEC: 8950 ± 1857 [295.9 ± 61.4%] vs. HSMEC: 9965 ± 2018 [329.4 ± 66.7%] vs. HUVEC: 9487 ± 1402 [313.6 ± 46.4%], p <0.05) as well as in primary lung MC. Thrombin-activation (5 U/ml, 12 h) of vascular cells led to an augmentation of the directed migration of MC as well as to a hirudin-sensitive increase in MGF synthesis and release. Moreover, a blocking anti-MGF antibody was found to inhibit MC-migration induced by unstimulated or thrombin-activated vascular cells. Together, these data show that endocardial and other vascular cells can induce migration of human MC. This MC-chemotactic signal of the vasculature is associated with expression and release of MGF, augmentable by thrombin, and may play a role in the pathophysiology of (auricular) thrombosis.

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