Distribution of Enzymes Between Subcellular Fractions in Animal Tissues

Duve, Christian de; Wattiaux, Robert; Baudhuin, Pierre

doi:10.1002/9780470124888.ch6

Cited by 118 publications

(5 citation statements)

References 375 publications

(58 reference statements)

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“…LDH is one of the glycolytic enzymes and is associated mainly with the cytoplasm (De Duve et al 1962). Lawson and Wilson (1980) added that LDH is not a regulatory factor for glycolysis but its activity is normally re- lated to the maximum rate of glycolysis.…”

Section: Discussionmentioning

confidence: 99%

Efficacy of Citrus reticulata and Mirazid in treatment of Schistosoma mansoni

Hamed¹,

Hetta

2005

Mem. Inst. Oswaldo Cruz

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This work has been carried out to investigate the effect ofCurrent control of the disease by chemotherapeutic agents is impractical because of the common occurrence of re-infection after treatment due to the relative resistance of the larval stages of Schistosoma mansoni to schistosomicide drugs (Silva et al. 2003). Praziquantel, the currently used drug for chemotherapeutic control, was reported to induce hemorrhage in the lung tissue of the host (Flisser & McLaren 1989) The present study is a trial to clarify the antischistosomal effect of C. reticulata root extract compared to commiphora extract (Mirazid). Enzyme markers for different cell organelles were measured in liver of S. mansoni infected mice; succinate dehydrogenase (SDH) for mitochondria; lactate dehydrogenase (LDH), and its isoenzymes for cytoplasm; glucose-6-phosphatase (G-6-Pase) for microsomes; acid phosphatase (AP) for lysosomes and 5'-nucleotidase for plasma membrane. Liver function enzymes; aspartate aminotransferase (AST); alanine aminotransferase (ALT) and alkaline phosphatase (ALP) were also measured. Parasitological studies through ova count and worm burden will take into consideration. MATERIALS AND METHODSChemicals -All chemicals used in the present study were of high analytical grade, products of Sigma (US), Merck (Germany), BDH (England).Mirazid (the oleo-resin extract from Myrrh of C. molmol tree, family: Burseraceae) is a product of Pharco Pharmaceutical Company, Egypt.Animals -The animals used were intact male Swiss albino mice of CDI strain of similar age (8 weeks) and weight (18-20 g). They were obtained from Theodor Bilharz Research Institute, Cairo, Egypt. Animals were kept in a controlled environment and were maintained on water and stock commercial pellet diet ad libitum.Plant material -C. reticulata (Family: Rutaceae) roots were collected from Modereyet El Tahrir, Behera, Egypt. It was authenticated by Dr Mohamed Abdel Ghaffar, Faculty of Agriculture, Al-Azhar University, Egypt. A voucher specimen is deposited at Chemistry of Natural Compounds Dept., National Research Center, Dokki, Cairo, Egypt.Extraction and isolation -Air dried powered roots of C. reticulata (0.85 kg) were extracted with 80% ethyl alcohol. The ethanolic extract was evaporated and the aqueous residue extracted sequentially thrice with equal volumes of n-hexane, ether, ethyl acetate, and n-butanol. The ethyl acetate extract was evaporated to dryness. The residue monitored by TLC using precoated silica gel 60 F254 aluminium sheets (0.2 mm thickness, Merk), was found to + Corresponding

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Section: Discussionmentioning

confidence: 99%

Efficacy of Citrus reticulata and Mirazid in treatment of Schistosoma mansoni

Hamed¹,

Hetta

2005

Mem. Inst. Oswaldo Cruz

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“…It possesses many complex properties, being allosterically regulated by numerous effectors and exhibiting concentration-dependent polymerization from a basic hexameric unit to massive polymers (Fisher, 1985). Immunohistochemical data showed two distinct mitochondrial matrix locations for GDH, one soluble and one membrane-associated (de Duve et al, 1962;Knecht et al, 1986). Scatchard analysis and surface plasmon resonance techniques have shown that only a subset of GDH is able to bind RNA, and this subset was shown to be phosphorylated (Preiss et al, 1995).…”

Section: Glutamate Dehydrogenase (Gdh)mentioning

confidence: 99%

Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?

Cieśla

2006

Acta Biochim Pol

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Several enzymes that were originally characterized to have one defined function in intermediatory metabolism are now shown to participate in a number of other cellular processes. Multifunctional proteins may be crucial for building of the highly complex networks that maintain the function and structure in the eukaryotic cell possessing a relatively low number of protein-encoding genes. One facet of this phenomenon, on which I will focus in this review, is the interaction of metabolic enzymes with RNA. The list of such enzymes known to be associated with RNA is constantly expanding, but the most intriguing question remains unanswered: are the metabolic enzyme-RNA interactions relevant in the regulation of cell metabolism? It has been proposed that metabolic RNA-binding enzymes participate in general regulatory circuits linking a metabolic function to a regulatory mechanism, similar to the situation of the metabolic enzyme aconitase, which also functions as iron-responsive RNA-binding regulatory element. However, some authors have cautioned that some of such enzymes may merely represent "molecular fossils" of the transition from an RNA to a protein world and that the RNA-binding properties may not have a functional significance. Here I will describe enzymes that have been shown to interact with RNA (in several cases a newly discovered RNA-binding protein has been identified as a well-known metabolic enzyme) and particularly point out those whose ability to interact with RNA seems to have a proven physiological significance. I will also try to depict the molecular switch between an enzyme's metabolic and regulatory functions in cases where such a mechanism has been elucidated. For most of these enzymes relations between their enzymatic functions and RNA metabolism are unclear or seem not to exist. All these enzymes are ancient, as judged by their wide distribution, and participate in fundamental biochemical pathways.

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“…The increase in acid phosphatase activities, 'marker' enzyme of the lysosomal membrane (de Duve et al, 1962;Collins and Lewis, 1971) might be attributed to increase in functional activity of the tissues leading to de novo synthesis of the enzyme molecule in situ (Umezawa and Hooper, 1982;Yakubu et al, 2001) or loss of other proteins (Akanji et al, 1993;Akanji and Yakubu, 2000). This could result in indiscriminate hydrolysis of phosphate esters, which are potential energy source for the cell (Butterworth and Moss, 1966).…”

Section: Plate 3bmentioning

confidence: 99%

Enzyme activities and histopathology of selected tissues in rats treated with potassium bromate.

Akanji¹,

Nafiu²,

Yakubu³

2010

African Journal of Biomedical Research

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The effect of chronic administration of potassium bromate (KBrO 3 ), a flour improver, on some 'marker' enzymes of rat cellular system was investigated. The levels of these enzymes were measured progressively in the kidney, liver and small intestine, 24h after days 1, 3, 5, 10, 15 and 20 following the administration of 10mg/kg body weight of potassium bromate and when left for 10days without administration after their 20 daily doses. The alkaline phosphatase (ALP), lactate dehydrogenase (LDH) and glutamate dehydrogenase (GDH) activities of all the tissues were significantly (P<0.05) decreased in KBrO 3 treated groups with corresponding significant (P<0.05) increase in the serum enzymes. Acid phosphatase (ACP) activities of all the tissues as well as the serum enzyme activities were significantly (P<0.05) decreased. There was only recovery in the ACP activities of all the tissues. Histological examination revealed congestion of the central vein with blood cells in the hepatocytes, infiltration of the interstitial cells accompanied with acute nephritis in the nephrons and mild mucosal dysfunction in the small intestine. The alterations in the 'marker' enzymes as well as in the tissue histology are indications of adverse effect of potassium bromate on the cells which might be due to the presence of oxygen in the molecule leading to oxidation of polyunsaturated fatty acids on the ordered lipid bilayer of cell membranes. All these might be responsible for the various adverse effects associated with the chemical compound.

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Distribution of Enzymes Between Subcellular Fractions in Animal Tissues

Cited by 118 publications

References 375 publications

Efficacy of Citrus reticulata and Mirazid in treatment of Schistosoma mansoni

Efficacy of Citrus reticulata and Mirazid in treatment of Schistosoma mansoni

Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?

Enzyme activities and histopathology of selected tissues in rats treated with potassium bromate.

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