A Clinical Evaluation of Serum Monoamine Oxidase, with Special Reference to Hepatic Fibrosis

Ito, Kenichi; Nakagawa, Jun; Minakuchi, Chisato; Fukase, M

doi:10.1159/000197095

Cited by 33 publications

(14 citation statements)

References 14 publications

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“…As a further criterion we showed that the serum enzyme is insensitive to Cu 24 ", whereas the liver mitochondrial enzyme was reported to be strongly inactivated (29). Previous studies have demonstrated elevated enzyme activities under several pathological conditions, especially iri progressive hepatic fibrosis (12)(13)(14)(15)(16)(30)(31)(32). The latter observation established the diagnostic significance of the enzyme and suggested that it might catalyze the initial step of collagen cross-linking in the liver (12,31,32).…”

Section: Discussionmentioning

confidence: 73%

“…In its substrate specifity it resembles the type B (23-25) mitochondria! outer membrane monoamine oxidase, but the inhibition by lathyrogens (26,27), such as j3-aminopropionitrile, and electrophoretic mobility clearly indicate marked differences between these two enzymes (12,28). As a further criterion we showed that the serum enzyme is insensitive to Cu 24 ", whereas the liver mitochondrial enzyme was reported to be strongly inactivated (29).…”

Section: Discussionmentioning

confidence: 99%

“…Despite its great clinical significance, the early diagnosis and therapeutic monitoring of hepatic fibroproliferation by biochemical means is presently hindered by a limited supply of reliable and practicable clinical-chemical parameters (9)(10)(11). Of these, the determination of the activity of monoamine oxidase (monoamine: 0 2 oxidoreductase, EC 1.4.3.4) in serum has been proposed as a useful, supplementary diagnostic procedure for organ fibrosis, in particular for active hepatic fibrosis (12)(13)(14).…”

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confidence: 99%

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Evaluation of the Assay for Serum Monoamine Oxidase – an Index of Hepatic Fibrosis

Gressner¹

1980

CCLM

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At present, neither the diagnostic efficiency, the analytic reliability, nor the practicability of clinical chemical tests for estimation of the degree and/or activity of the fibrotic transformation of the chronically injured liver are satisfactory. Among the various parameters proposed, the determination of the activity of monoamine oxidase (monoaniine: O 2 oxidoreductase, EC 1.4.3.4) in serum seems to be advantageous. To facilitate its routine use we studied some important practical aspects of the new colorimetric assay for the activity of monoamine oxidase in serum. The reaction procedes linearly with time for at least two hours and with enzyme concentrations up to 6 kU/1. Gressner: Monoamine oxidase determination in serum Unter den 26 getesteten Kontrollseren enthalten nur wenige Monoaminoxidase-Aktivität, die quantitativ (d.h. vergleichbare katalytische Konzentration) und qualitativ (d. h. vergleichbare Sensitivität gegenüber /3-Aminopropionitril und ähnliches Aktivitätsverhältnis in Tris-/Phosphat-Puffer) der in menschlichen Seren vorhandenen entspricht. Mithin sind nur wenige der kommerziell erhältlichen Kontrollseren für die Präzisionskpntrolle dieser Bestimmung geeignet.

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Section: Discussionmentioning

confidence: 73%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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Evaluation of the Assay for Serum Monoamine Oxidase – an Index of Hepatic Fibrosis

Gressner¹

1980

CCLM

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“…Previous work demonstrated that plasma amine oxidase measured with benzylamine as substrate increases during hepatic fibrosis and suggested that this enzyme might catalyze collagen croslinking in the liver (32)(33)(34). It is unlikely that the assay with collagen substrates used here detected amine oxidase rather than lysyl oxidase activity because purified amine oxidase preparations do not utilize collagen substrates (2) and 10 mM L-lysine was added to each assay as a competitive substrate for amine oxidase.…”

Section: Discussionmentioning

confidence: 99%

Biochemical and immunochemical study of lysyl oxidase in experimental hepatic fibrosis in the rat.

Siegel¹,

Chen²,

Greenspan³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

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Lysyl oxidase catalyzes the crosslinking of collagen and elastin. Lysyl oxidase activity was measured and localized in rat liver during the evolution of hepatic fibrosis induced by CCL4. Enzyme activity measured with DL[6-3HJ-lysine-labeled collagen substrates in liver and plasma increased sharply after approximately 3 wk of injection, reached a maximum at 6 wk, and then decreased. The increase in activity correlated histologically with early connective tissue septa formation, and the magnitude of increase was significantly greater than that found for the intracellular collagen biosynthetic enzymes protocollagen prolyl hydroxylase and lysyl hydroxylase. Indirect immunofluorescence studies showed that lysyl oxidase was present in association with collagen in the extracellular space. However, it was not possible to correlate the distribution pattern with a particular liver cell type. These observations suggest that serial measurements of lysyl oxidase activity in liver or plasma may be useful for correlating changes in connective tissue formation with histologic connective tissue deposition. Lysyl oxidase catalyzes the enzymatic reaction that initiates collagen and elastin crosslinking (1, 2). In this reaction, the e-amino groups of certain lysyl and hydroxylysyl residues are oxidatively deaminated to form the corresponding 6-semialdehydes (3). These then condense either with e-amino groups of other lysyl or hydroxylysyl residues or with other semialdehydes to form Schiff base or aldol crosslinks (4). To date, studies of lysyl oxidase activity in experimental fibrosis have been limited to wounds and granulation tissue forming in implanted sponges (5-7). Investigations comparing the alterations in lysyl oxidase activity during experimental fibrosis to activity of other post-translational collagen biosynthetic enzymes are limited to a single study dealing with the effect of cholesterol on collagen metabolism in the chicken aorta (8). The purposes of the present study are: (i) to describe the changes in lysyl oxidase activity that occur during hepatic fibrosis induced by CC14 in the rat; (ii) to compare these changes with the alterations in activity of other enzymes required for collagen biosynthesis, such as protocollagen prolyl hydroxylase (proline,2-oxoglutarate dioxygenase, EC 1.14.11.2) and lysyl hydroxylase (lysine,2-oxoglutarate dioxygenase, EC 1.14.11.4); and (iii) to identify the tissue localization of lysyl oxidase by indirect immunofluorescence. Experimental hepatic fibrosis is a useful model for this type of comparative study because the initial collagen content of liver is quite low and large amounts relative to that initially present may be synthesized during the fibrosis caused by chronic CC14 intoxication (9). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. Biochemical Studies. Weighed portions of liver were homogenized ...

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“…Fatty change was graded in three according to the extent of fatty change occupying the parenchyma: +1, less than 20 %; +2, 20-40 %; +3, more than 40 %. 'Active' hepatitis and 'active' liver cirrhosis were defined ac cording to the description by the Japanese Association of Hepatologists (7,8).…”

Section: Introductionmentioning

confidence: 99%

Tyramine Oxidase Activity in Needle Biopsy of Normal Livers and Diseased Livers

Arima¹,

Okada²,

Kubota³

et al. 1977

Enzyme

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Tyramine oxidase and UDP-glucuronyl transferase activities were determined in 52 diseased livers obtained by needle biopsy. 14 liver specimens were also subjected to acetyl CoA carboxylase determination. Tyramine oxidase level was elevated in livers with nonalcoholic fatty change or toxic hepatitis, and reduced in livers with fibrosis or chronic alcoholic injury. UDP-glucuronyl transferase activity was reduced in livers with severe parenchymal damage or hyperbilirubinemia. Acetyl CoA carboxylase activity decreased markedly in an active alcoholic cirrhotic liver, and was elevated in alcoholic fatty livers as well as in a liver with acute venous stasis.

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A Clinical Evaluation of Serum Monoamine Oxidase, with Special Reference to Hepatic Fibrosis

Cited by 33 publications

References 14 publications

Evaluation of the Assay for Serum Monoamine Oxidase – an Index of Hepatic Fibrosis

Evaluation of the Assay for Serum Monoamine Oxidase – an Index of Hepatic Fibrosis

Biochemical and immunochemical study of lysyl oxidase in experimental hepatic fibrosis in the rat.

Tyramine Oxidase Activity in Needle Biopsy of Normal Livers and Diseased Livers

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