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 AGIA Tag System for Ultrastructural Protein Localization Analysis in Blood-Stage Plasmodium falciparum

2021 ◽  
Vol 11 ◽  
Author(s):  
Masayuki Morita ◽  
Bernard N. Kanoi ◽  
Naoaki Shinzawa ◽  
Rie Kubota ◽  
Hiroyuki Takeda ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Subcellular Localization ◽  
Western Blotting ◽  
Protein Localization ◽  
Transmembrane Protein ◽  
Physiological Role ◽  
Immunofluorescence Assay ◽  
Blood Stage ◽  
Parasite Development ◽  
High Signal

Precise subcellular localization of proteins is the key to elucidating the physiological role of these molecules in malaria parasite development, understanding of pathogenesis, and protective immunity. In Plasmodium falciparum, however, detection of proteins in the blood-stage parasites is greatly hampered by the lack of versatile protein tags which can intrinsically label such molecules. Thus, in this study, to develop a novel system that can be used to evaluate subcellular localization of known and novel proteins, we assessed the application of AGIA tag, consisting of 9 amino acids (EEAAGIARP), in P. falciparum blood-stage parasites. Specifically, AGIA-tagged ring-infected erythrocyte surface antigen (RESA-AGIA) was episomally expressed in P. falciparum 3D7 strain. The RESA-AGIA protein was detected by Western blotting and immunofluorescence assay (IFA) using recombinant rabbit anti-AGIA tag monoclonal antibody (mAb) with a high signal/noise ratio. Similarly, AGIA-tagged multidrug resistance protein 1 (MDR1-AGIA), as an example of polyptic transmembrane protein, was endogenously expressed and detected by Western blotting and IFA with anti-AGIA tag mAb. Immunoelectron microscopy of the RESA-AGIA transfected merozoites revealed that mouse anti-RESA and the rabbit anti-AGIA mAb signals could definitively co-localize to the dense granules. Put together, this study demonstrates AGIA tag/anti-AGIA rabbit mAb system as a potentially useful tool for elucidating the subcellular localization of new and understudied proteins in blood-stage malaria parasites at the nanometer-level resolution.

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.

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 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

Physiological Role of Cyclic Electron Flow in Higher Plants

2012 ◽  
Vol 30 (1) ◽  
pp. 100
Author(s):  
Wei HUANG ◽  
Shi-Bao ZHANG ◽  
Kun-Fang CAO
Keyword(s):  
Higher Plants ◽  
Electron Flow ◽  
Physiological Role ◽  
Cyclic Electron Flow

The Renal Outer Medullary Potassium Channel (ROMK): An Intriguing Pharmacological Target for an Innovative Class of Diuretic Drugs

2018 ◽  
Vol 25 (23) ◽  
pp. 2627-2636 ◽  
Author(s):  
Vincenzo Calderone ◽  
Alma Martelli ◽  
Eugenia Piragine ◽  
Valentina Citi ◽  
Lara Testai ◽  
...  
Keyword(s):  
Physiological Role ◽  
Clinical Use ◽  
Diuretic Activity ◽  
First Line ◽  
Potassium Homeostasis ◽  
Diuretic Drugs ◽  
Pharmacological Target ◽  
Diuretic Agents ◽  
Effective Drugs

In the last four decades, the several classes of diuretics, currently available for clinical use, have been the first line option for the therapy of widespread cardiovascular and non-cardiovascular diseases. Diuretic drugs generally exhibit an overall favourable risk/benefit balance. However, they are not devoid of side effects. In particular, all the classes of diuretics cause alteration of potassium homeostasis. <p> In recent years, understanding of the physiological role of the renal outer medullary potassium (ROMK) channels, has shown an intriguing pharmacological target for developing an innovative class of diuretic agents: the ROMK inhibitors. This novel class is expected to promote diuretic activity comparable to (or even higher than) that provided by the most effective drugs used in clinics (such as furosemide), with limited effects on potassium homeostasis. <p> In this review, the physio-pharmacological roles of ROMK channels in the renal function are reported, along with the most representative molecules which have been currently developed as ROMK inhibitors.

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