Endoplasmic Reticulum Abnormality in Alzheimer's Disease: Selective Alteration in Platelet NADH-Cytochrome C Reductase Activity

We have obtained and studied a 105,000-g pellet from T-3-Cl-2 cells, a cloned line of Friend virus-induced erythroleukemia cells. By difference spectrophotometry, the pellet was shown to contain cytochrome b5 and cytochrome P-450, hemeproteins that have been shown to participate in electron-transport reactions of endoplasmic reticulum and other membranous fractions of various tissues. The pellet also possesses NADH-cytochrome c reductase activity which is inhibited by anti-cytochrome b5 gamma-globulin, indicating the presence of cytochrome b5 reductase. This is the first demonstration of membrane-bound forms of these redox proteins in erythroid cells. Dimethyl sulfoxide-treated T-3-Cl-2 cells were also shown to possess membrane-bound cytochrome b5 and NADH-cytochrome c reductase activity. We failed to detect soluble cytochrome b5 in the 105,000-g supernatant fraction from homogenates of untreated or dimethyl sulfoxide-treated T-3-Cl-2 cells. In contrast, erythrocytes obtained from mouse blood were shown to possess soluble cytochrome b5 but no membrane-bound form of this protein. These findings are supportive of our hypothesis that soluble cytochrome b5 of erythrocytes is derived from endoplasmic reticulum or some other membrane structure of immature erythroid cells during cell maturation.

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Endoplasmic reticulum membrane isolated from small-intestinal epithelial cells: enzyme and protein components

Journal of Cell Science ◽

10.1242/jcs.52.1.215 ◽

1981 ◽

Vol 52 (1) ◽

pp. 215-222

Author(s):

M. Fujita ◽

H. Ohta ◽

T. Uezato

Keyword(s):

Endoplasmic Reticulum ◽

Epithelial Cells ◽

Cytochrome C ◽

Endoplasmic Reticulum Membrane ◽

Dependent Manner ◽

Cytochrome C Reductase ◽

Basolateral Membranes ◽

Nadh Cytochrome ◽

Protein Components ◽

A Minor

Endoplasmic reticulum membrane-rich fraction was obtained by subfractionation of the light microsomes from mouse jejunal mucosal epithelial cells. It was marked by high glucose-6-phosphatase, NADPH-cytochrome c reductase, and NADH-cytochrome c reductase activities and low Na+,K+-ATPase activity. The enrichment of Na+,K+-ATPase was 180-fold higher in the basolateral membranes than in the endoplasmic reticulum membrane-rich fraction relative to glucose-6-phosphatase. The protein peak that was phosphorylated in a Na-dependent manner was prominent in the basolateral membranes while it was a minor peak in the endoplasmic reticulum membrane-rich fraction. Under the electron microscope the fraction was seen to be composed of homogeneous small vesicles with thin smooth membranes.

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Brain Regional Analysis of NADH-Cytochrome C Reductase Activity in Alzheimerʼs Disease

Journal of Neuropathology & Experimental Neurology ◽

10.1097/00005072-199005000-00002 ◽

1990 ◽

Vol 49 (3) ◽

pp. 206-214 ◽

Cited By ~ 9

Author(s):

GEORGE S. ZUBENKO ◽

JOHN MOOSSY ◽

DIANA CLAASSEN ◽

A. Julio Martinez ◽

GUTTI R. RAO

Keyword(s):

Cytochrome C ◽

Reductase Activity ◽

Regional Analysis ◽

Cytochrome C Reductase ◽

Nadh Cytochrome

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Studies on the Function of Cell Membrane 6th Report: Influence of Sex Hormones on the Elevation of Nadh-Cytochrome c Reductase Activity in Liver Plasma Membrane of CCl4-Administered Rats

The Japanese Journal of Pharmacology ◽

10.1016/s0021-5198(19)31521-5 ◽

1973 ◽

Vol 23 (6) ◽

pp. 753-756

Author(s):

Yasusuke MASUDA ◽

Masato KUCHII ◽

Hiroyuki YAMAMOTO ◽

Tadashi MURANO

Keyword(s):

Plasma Membrane ◽

Cytochrome C ◽

Cell Membrane ◽

Sex Hormones ◽

Reductase Activity ◽

Cytochrome C Reductase ◽

Liver Plasma Membrane ◽

Nadh Cytochrome

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Structural and functional relationships of enzyme activities induced by nitrate in barley

Biochemical Journal ◽

10.1042/bj1190715 ◽

1970 ◽

Vol 119 (4) ◽

pp. 715-725 ◽

Cited By ~ 158

Author(s):

John L. Wray ◽

Philip Filner

Keyword(s):

Cytochrome C ◽

Nitrate Reductase ◽

Nitrate Reductase Activity ◽

Reductase Activity ◽

Bottom Layer ◽

Sucrose Density Gradient ◽

Enzyme Complex ◽

Cytochrome C Reductase ◽

Functional Relationships ◽

Nadh Cytochrome

1. Nitrate induces the development of NADH-nitrate reductase (EC 1.6.6.1), FMNH2–nitrate reductase and NADH–cytochrome c reductase activities in barley shoots. 2. Sucrose-density-gradient analysis shows one band of NADH–nitrate reductase (8S), one band of FMNH2–nitrate reductase activity (8S) and three bands of NADH–cytochrome c reductase activity (bottom layer, 8S and 3.7S). Both 8S and 3.7S NADH–cytochrome c reductase activities are inducible by nitrate, but the induction of the 8S band is much more marked. 3. The 8S NADH–cytochrome c reductase band co-sediments with both NADH–nitrate reductase activity and FMNH2–nitrate reductase activity. Nitrite reductase activity (4.6S) did not coincide with the activity of either the 8S or the 3.7S NADH–cytochrome c reductase. 4. FMNH2–nitrate reductase activity is more stable (t½ 12.5min) than either NADH–nitrate reductase activity (t½ 0.5min) or total NADH–cytochrome c reductase activity (t½ 1.5min) at 45°C. 5. NADH–cytochrome c reductase and NADH–nitrate reductase activities are more sensitive to p-chloromercuribenzoate than is FMNH2–nitrate reductase activity. 6. Tungstate prevents the formation of NADH–nitrate reductase and FMNH2–nitrate reductase activities, but it causes superinduction of NADH–cytochrome c reductase activity. Molybdate overcomes the effects of tungstate. 7. The same three bands (bottom layer, 8S and 3.7S) of NADH–cytochrome c reductase activity are observed irrespective of whether induction is carried out in the presence or absence of tungstate, but only the activities in the 8S and 3.7S bands are increased. 8. The results support the idea that NADH–nitrate reductase, FMNH2–nitrate reductase and NADH–cytochrome c reductase are activities of the same enzyme complex, and that in the presence of tungstate the 8S enzyme complex is formed but is functional only with respect to NADH–cytochrome c reductase activity.

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Cytochrome b5-like Hemoprotein of Outer Mitochondrial Membrane; OM Cytochrome b II. Contribution of OM Cytochrome b to Rotenone-Insensitive NADH-cytochrome c Reductase Activity

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a132754 ◽

1980 ◽

Vol 87 (1) ◽

pp. 73-80 ◽

Cited By ~ 20

Author(s):

Akio ITO

Keyword(s):

Cytochrome C ◽

Cytochrome B ◽

Mitochondrial Membrane ◽

Reductase Activity ◽

Cytochrome B5 ◽

Outer Mitochondrial Membrane ◽

Cytochrome C Reductase ◽

Nadh Cytochrome

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Inhibition and inactivation of NADH-cytochrome c reductase activity of bovine heart submitochondrial particles by the iron(III)-adriamycin complex

Biochemical Journal ◽

10.1042/bj2650865 ◽

1990 ◽

Vol 265 (3) ◽

pp. 865-870 ◽

Cited By ~ 24

Author(s):

B B Hasinoff

Keyword(s):

Cytochrome C ◽

Reductase Activity ◽

Inner Mitochondrial Membrane ◽

Submitochondrial Particles ◽

Cytochrome C Reductase ◽

Fast Phase ◽

Bovine Heart ◽

Direct Binding ◽

Nadh Cytochrome

The NADH-cytochrome c reductase activity of bovine heart submitochondrial particles was found to be slowly (half-time of 16 min) and progressively lost upon incubation with the Fe2(+)-adriamycin complex. In addition to this slow progressive inactivation seen on incubation, a reversible fast phase of inhibition was also seen. However, if EDTA was added to the incubation mixture within 15 s, the slow progressive loss in activity was largely preventable. Separate experiments indicated that EDTA removed about one-half of the iron from the Fe2(+)-adriamycin complex in about 40 s. These results indicated the requirement for iron for the inactivation process. Since the Vmax. for the fast phase of inhibition was decreased by the inhibitor, the inhibition pattern was similar to that seen for uncompetitive or mixed-type inhibition. The direct binding of both Fe3(+)-adriamycin and adriamycin to submitochondrial particles was also demonstrated, with the Fe3(+)-adriamycin complex binding 8 times more strongly than adriamycin. Thus binding of Fe3(+)-adriamycin to the enzyme or to the inner mitochondrial membrane with subsequent generation of oxy radicals in situ is a possible mechanism for the Fe3(+)-adriamycin-induced inactivation of respiratory enzyme activity.

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NADH-cytochrome c reductase activity in cultured human lymphocytes

Archives of Biochemistry and Biophysics ◽

10.1016/0003-9861(76)90147-8 ◽

1976 ◽

Vol 176 (1) ◽

pp. 119-126 ◽

Cited By ~ 11

Author(s):

Russell A. Prough ◽

Richard L. Imblum ◽

Richard A. Kouri

Keyword(s):

Cytochrome C ◽

Reductase Activity ◽

Human Lymphocytes ◽

Cytochrome C Reductase ◽

Nadh Cytochrome

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Increased peak oxygen consumption of trained muscle requires increased electron flux capacity

Journal of Applied Physiology ◽

10.1152/jappl.1994.77.4.1941 ◽

1994 ◽

Vol 77 (4) ◽

pp. 1941-1952 ◽

Cited By ~ 44

Author(s):

D. M. Robinson ◽

R. W. Ogilvie ◽

P. C. Tullson ◽

R. L. Terjung

Keyword(s):

Electron Transport ◽

Cytochrome C ◽

Reductase Activity ◽

Tight Binding ◽

Treadmill Running ◽

Complex Iii ◽

Peak Oxygen Consumption ◽

Transport Capacity ◽

Cytochrome C Reductase ◽

Nadh Cytochrome

The importance of the training-induced increase in mitochondrial capacity in realizing the increase in maximal O2 consumption (VO2max) of trained muscle was evaluated using an isolated perfused rat hindlimb preparation at a high blood flow (approximately 80 ml.min-1.100 g-1) during tetanic contractions. Rats trained for 8-–12 wk by treadmill running exhibited an approximately 25% increase in muscle VO2max (5.62 +/- 0.31 to 7.06 +/- 0.64 mumol.min-1.g-1), an increase in mitochondrial enzyme activity (approximately 70% for cytochrome oxidase and approximately 55% for NADH cytochrome-c reductase), and an increase in tissue capillarity (14%) that is expected to increase the O2 exchange capacity of the tissue. Muscle VO2max of sedentary (n = 34) and trained (n = 30) animals was determined, and electron transport capacity was acutely managed with myxothiazol, a tight-binding inhibitor of complex III. Inhibition of complex III was similar among 1) the low- and high-oxidative fibers and 2) the superficial and deep mitochondrial populations within muscle. Inhibition of NADH cytochrome-c reductase activity resulted in reductions in muscle VO2max with similar dose responses (mean effective dose of approximately 0.2 microM) of myxothiazol added to the perfusion medium. The extraction of O2 by the contracting muscle decreased as VO2max declined. The increase in muscle VO2max observed in the muscle of trained animals was eliminated when its electron transport capacity was reduced to that observed in normal sedentary rat muscle. Thus, the exercise-induced adaptation of an increased muscle mitochondrial content appears to be essential for trained muscle to exhibit its increased O2 flux capacity. The results of the present experiment illustrate the importance of mitochondrial adaptations in muscle remodeled by exercise training.

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