The Submitochondrial Localization of Monoamine Oxidase

Schnaitman, Carl A.; Erwin, V. Gene; Greenawalt, John W.

doi:10.1083/jcb.32.3.719

Cited by 814 publications

(230 citation statements)

References 23 publications

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“…The outer membrane in particular has been reported to contain substantial thyroid hormone binding sites [7,29] some of which may be related to plasma thyroxine binding 282 pre-albumin [29]. Hence we sought, by removing the outher membrane with digitonin [23] and leaving intact inner membrane vesicles, to reduce the endogenous pool of hormone. Table 1 presents the findings with mitoplasts prepared thus from euthyroid animals.…”

Section: Resultsmentioning

confidence: 99%

“…Mitoplasts -intact mitochondrial inner membrane vesicles with the outer membrane and intermembrane space enzymes removed -were prepared by the controlled digitonin method of Schnaitman et al [23] using 0.2 mg digitonin per mg mitochondrial protein followed by differential centrifugation as described by Schnaitman and Greenawalt [24]. The mitoplasts were finally resuspended in 0.25 M sucrose.…”

Section: Mitoplast Preparationmentioning

confidence: 99%

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Evidence for ADP‐ribosylation in the mechanism of rapid thyroid hormone control of mitochondria

Thomas

Mowbray

1987

FEBS Letters

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Triiodothyronine in vitro at concentrations between lo-r3 and lo-"M very rapidly activates oxidative phosphorylation in hypothyroid rat liver mitochondria. Comparing the concentrations of hormone with estimates of the amounts of respiratory chain components present suggests that this activation may involve an amplification mechanism. Here we present evidence that while no changes in phosphorylation were detected following hormone administration, nicotinamidc, an inhibitor of mono ADP-ribosylation reported to occur rapidly and reversibly in mitochondria, prevented activation by hormone. Moreover incubation with nicotinamide of euthyroid mitochondria and derived intact inner membrane vesicles revealed lowered ADPjO ratios under the same conditions as shown by hypothyroid preparations. While this lesion could be reversed simply by washing the intact mitochondria, the membrane vesicles required triiodothyronine addition.

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Section: Resultsmentioning

confidence: 99%

Section: Mitoplast Preparationmentioning

confidence: 99%

Evidence for ADP‐ribosylation in the mechanism of rapid thyroid hormone control of mitochondria

Thomas

Mowbray

1987

FEBS Letters

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“…Succinate dehydrogenase activity (EC 1.3.99.1) was assayed by the procedure of Earl & Korner (1965). Monoamine oxidase activity (EC 1.4.3.4) was determined spectrophotometrically as described by Schnaitman et al (1967).…”

Section: Experimental Methodsmentioning

confidence: 99%

Functional polarity of the rat hepatocyte surface membrane. Isolation and characterization of plasma-membrane subfractions from the blood-sinusoidal, bile-Canalicular and contiguous surfaces of the hepatocyte

Wisher¹,

Evans²

1975

Biochemical Journal

305

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1. Six rat liver plasma-membrane subfractions of different density and morphological, enzymric and chemical properties were prepared from homogenates by a combination of differential, rate-zonal and density-gradient centrifugation. They consisted of three vesicular 'light' subfractions of density 1.12-1.13 and three 'heavy' subfractions of density 1.16-1.18 containing membrane strips and intercellular junctions. 2. All six subfractions contained a basal adenylate cyclase activity. One of the 'light' subfractions that showed the highest glucagon-stimulated adenylate cyclase activity was identified as deriving from the blood-sinusoidal face of the hepatocyte. This subfraction, unlike the others, was contaminated by Golgi components, as indicated by its morphological properties and the presence of galactosyl-and sialyl-transferase activities. 3. All the six subfractions showed high activities of the following plasma-membrane marker enzymes: 5'-nucleotidase, alkaline phosphodiesterase (nucleotide pyrophosphatase), alkaline phosphatase, leucine naphthylamidase and Mg2+-activated adenosine triphosphatase. A 'light' subfraction that showed the highest specific activities of all the above marker enzymes, but lacked a glucagon-stimulated adenylate cyclase activity, was identified as deriving from the bilecanalicular face of the hepatocyte. 4. The 'heavy' subfractions, which showed generally the lowest activities of the above plasma-membrane enzyme markers, and were characterized by the presence of desmosomes and gap junctions, were taken to originate from the contiguous faces of the hepatocyte. 5. The protein composition of the six subfractions was generally similar, as shown by polyacrylamide-gel electrophoresis. Differences in the amounts of various protein and glycoprotein bands among the subfractions correlated with their morphology, enzymic composition and sialic acid content. 6. Hormonal and histochemical evidence supporting the identification of a bile-canalicular subfraction, a blood-sinusoidal subfraction and contiguous-face subfractions is discussed.

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“…The techniques for separating the two membrane systems include densitygradient centrifugation following mitochondrial swelling and contraction (1,2), gradient centrifugation following controlled osmotic lysis (3,4), and treatment with digitonin in isotonic media followed by differential centrifugation (3,5). Of these techniques the digitonin fractionation, described first by Levy et al (5) and subsequently by Schnaitman et al (3), is often the most advantageous.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Properties of the Inner and Outer Membranes of Rat Liver Mitochondria

Schnaitman¹,

Greenawalt²

1968

The Journal of Cell Biology

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1,382

478

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Treatment of rat liver mitochondria with digitonin followed by differential centrifugation was used to resolve the intramitochondrial localization of both soluble and particulate enzymes. Rat liver mitochondria were separated into three fractions: inner membrane plus matrix, outer membrane, and a soluble fraction containing enzymes localized between the membranes plus some solublized outer membrane. Monoamine oxidase, kynurenine hydroxylase, and rotenone-insensitive NADH-cytochrome c reductase were found primarily in the outer membrane fraction. Succinate-cytochrome c reductase, succinate dehydrogenase, cytochrome oxidase, j-hydroxybutyrate dehydrogenase, a-ketoglutarate dehydrogenase, lipoamide dehydrogenase, NAD-and NADH-isocitrate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase, and ornithine transcarbamoylase were found in the inner membrane-matrix fraction. Nucleoside diphosphokinase was found in both the outer membrane and soluble fractions; this suggests a dual localization. Adenylate kinase was found entirely in the soluble fraction and was released at a lower digitonin concentration than was the outer membrane; this suggests that this enzyme is localized between the two membranes. The inner membrane-matrix fraction was separated into inner membrane and matrix by treatment with the nonionic detergent Lubrol, and this separation was used as a basis for calculating the relative protein content of the mitochondrial components. The inner membrane-matrix fraction retained a high degree of morphological and biochemical integrity and exhibited a high respiratory rate and respiratory control when assayed in a sucrose-mannitol medium containing EDTA.

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The Submitochondrial Localization of Monoamine Oxidase

Cited by 814 publications

References 23 publications

Evidence for ADP‐ribosylation in the mechanism of rapid thyroid hormone control of mitochondria

Evidence for ADP‐ribosylation in the mechanism of rapid thyroid hormone control of mitochondria

Functional polarity of the rat hepatocyte surface membrane. Isolation and characterization of plasma-membrane subfractions from the blood-sinusoidal, bile-Canalicular and contiguous surfaces of the hepatocyte

Enzymatic Properties of the Inner and Outer Membranes of Rat Liver Mitochondria

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