Localization of Leucine Aminopeptidase in Serum and Body Fluids by Starch Gel Electrophoresis*

Kowlessar, O. Dhodanand; Haeffner, Lorraine J.; Sleisenger, Marvin H.

doi:10.1172/jci104082

Cited by 49 publications

(7 citation statements)

References 5 publications

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“…The elevation of the LDH activity peak in the ft-globulin and the appearance of a large activity peak in the y-globulin in plasma from a patient with hepatitis are in harmony with the observation that the majority of LDH activity in liver homogenate resides in peaks with similar mobilities. Analagous to the appearance of a large LDH activity peak in serum during hepatitis is the appearance of additional peaks of leucine aminopeptidase activity in serum during liver disease (16). Both observations provide further support for the hypothesis that elevations in serum enzyme activity during several disease states are attributable in part to the liberation of enzymes from damaged organs.…”

Section: Discussionmentioning

confidence: 53%

Isozymes of Lactic Dehydrogenase in Human Tissues*

Vesell¹,

Bearn²

1961

J. Clin. Invest.

143

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Section: Discussionmentioning

confidence: 53%

Isozymes of Lactic Dehydrogenase in Human Tissues*

Vesell¹,

Bearn²

1961

J. Clin. Invest.

143

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“…In the kidneys, the enzymes ALP, LAP, and γGTP are localized at the brush border membrane (BBM) of the proximal tubules (Koseki et al, 1980) and LDH are widely localized through the renal tubules (Endo, 1978). Although these enzymes are also expressed in other organs, including the liver, and can also be detected in the blood (Yong, 1967;Kowlessar et al, 1960;Naftalin et al, 1969), they do not appear in the urine because their molecular weights are too large to allow their filtration through the glomeruli. Therefore, the ALP, LAP, and γGTP detected in the urine originate from the kidneys, especially the proximal tubules.…”

Section: Discussionmentioning

confidence: 99%

Sex differences in the excretion levels of traditional and novel urinary biomarkers of nephrotoxicity in rats

et al. 2017

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-Urinary biomarkers have been used widely in preclinical toxicity studies to detect dysfunctions and injuries of the kidney caused by drugs under development. While they have been well studied for evaluating nephrotoxicity, knowledge of sex differences in excretion levels of urinary biomarkers remains inadequate. We conducted experiments focused on effects of endogenous sex hormones on urinary biomarkers using intact and castrated male and female rats. Comparisons of the urinary biomarker excretion levels between intact male and female rats at 5, 7, 9 and 12 weeks of age revealed higher excretion levels of leucine aminopeptidase (LAP), γ-glutamyl transpeptidase (γGTP), total protein, liver-type fatty acid-binding protein (L-FABP), cystatin C (Cys-C) and β2-microglobulin (β2-MG), and lower excretion level of kidney injury molecule 1 (Kim-1), in male rats as compared to female rats. Orchidectomized male rats showed lower urinary excretion levels of alkaline phosphatase (ALP), LAP, γGTP, N-acetyl-β-D-glucosaminidase (NAG), glucose, total protein, L-FABP, Cys-C, β2-MG and neutrophil gelatinaseassociated lipocalin (NGAL), and higher urinary excretion levels of clusterin (CLU) and Kim-1, than sham-operated male rats. On the other hand, no significant differences in the urinary biomarker excretion levels excluding ALP were observed between ovariectomized and sham-operated female rats. In the present study, we demonstrated the existence of sex differences in excretion levels of urinary biomarkers that are universally used in preclinical toxicity studies, and also that these differences, especially in relation to the urinary excretions of ALP, LAP, γGTP, total protein, L-FABP, Cys-C, and β2-MG, may closely relate to the endogenous testosterone.

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“…Riboflavin, TEMED und Triton X-100 lieferte Serva (Heidelberg), Neuraminidase Boehringer (Mannheim) und die übrigen Substanzen Merck (Darmstadt), wobei Acrylamid in Chloroform und BIS in Aceton umkristallisiert wurden (5 (2,9,10,11), Agar (12), Papier (13), Celluloseacetat (14) oder Polyaciylamid (7,15) verwenden und unbefriedigende (9, 12) oder photographisch nicht dokumentierbare (2,10,11,13,14,15) Trennungen liefern, erlaubt das beschriebene Verfahren, ebenso wie die ähnliche Technik von Dingjan et al (16), die Darstellung eindeutiger, gut reproduzierbarer Isoenzymmuster, auch bei Mischung von zwei Organextrakten (Abb. 1).…”

Section: Reagenzien 3 )unclassified

“…Lagerung und mehrfaches Auftauen hatten keinen Einfluß auf die Enzymmuster, die bei 17 000 £-und 100 000>Über-ständen identisch ausfielen, da das Sammelgel alle Partikel am Start zurückhielt. Dieser Befund stimmt mit den Ergebnissen der Literatur (7,9,11,14,17) Serum IV III II Ib la Typl Typ 2 Typ3 Typ 4 2,5-2,6 2,5-2,6 2,5-2,6 3,5-3, nehmender Cholestase und ihr Fehlen bei extrahepatischen und extrabiliären Krankheiten. Sofern neben der Bande I eine oder weitere Banden erschienen, war immer eine Beteiligung der Leber anzunehmen (Lymphogranulomatose, G; biliäre Lobärpneumonie, K), wie sich autoptisch bestätigen ließ.…”

Section: Multiple Formenunclassified

Disk-Elektrophorese multipler Formen von Arylamidasen. Untersuchungen über Arylamidasen menschlicher Gewebe, I. Mitteilung

Lorentz¹,

Marunowski²,

Ritter³

1974

Clinical Chemistry and Laboratory Medicine

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Die disk-elektrophoretische Trennung von Arylamidasen menschlicher Herkunft ergibt organtypische Muster, die von denen der 7-Glutamyltransferase (EC 2.3.2.2) abweichen. Das Serum Gesunder zeigt nur eine anodische Fraktion (Typ 1), zu der bei hepatobiliären Erkrankungen bis zu drei langsamer wandernde Banden in bestimmter Reihenfolge kommen (Typen 2, 3 und 4). Ihr Erscheinen bedeutet ein empfindliches Indiz für den Eintritt einer Cholestase, ist jedoch nicht krankheitsspezifisch. Die Lokalisation der vier Fraktionen korrespondiert nicht mit dem Verteilungstyp in Organextrakten, insbesondere ist die Wanderungsgeschwindigkeit der anodischen Bande höher als die in anderen Geweben. Durch Einwirkung von Neuraminidase werden alle schnellwandernden Arylamidasefraktionen verschiedener Organe so verlangsamt, daß eine einheitliche Beweglichkeit resultiert. Die Mehrzahl der langsamen Banden verschwindet. Ähnliche Beobachtungen bei der 7-Glutämyltransferase führen zu der Hypothese, daß die Freisetzung von Enzymen mikrosomaler Herkunft in das Serum physiologischerweise nach glykosidischer Bindung an Neuraminsäure erfolgt. Disc-electrophoresis ofmultiple forms of arylamidase. Studies on human arylamidases, IThe disc-electrophoresis of arylamidases in human tissues yields typical patterns quite different from those of -Glutamyrtransferase. There is only one fast fraction in normal sera (type 1); three additional slower bands in a certain sequence (types 2, 3, and 4), indicate the onset of biliary stasis, but they are without diagnostic specifity. The patterns do not correspond to the distribution of multiple forms observed in any of the tissue homogenates; in particular, the anodic fraction of the serum is the fastest moving activity of any tissue. Neuraminidase treatment abolishes the majority of the slowly migrating fractions and so retards the different anodic bands that a single band of uniform mobility is produced. Similar effects in the separation of -Glutamyltransferase lead to the conclusion that the release of microsomal activities into the serum is accompanied by the formation of a glycosidic linkage between the enzyme and neuraminic acid.

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Localization of Leucine Aminopeptidase in Serum and Body Fluids by Starch Gel Electrophoresis*

Cited by 49 publications

References 5 publications

Isozymes of Lactic Dehydrogenase in Human Tissues*

Isozymes of Lactic Dehydrogenase in Human Tissues*

Sex differences in the excretion levels of traditional and novel urinary biomarkers of nephrotoxicity in rats

Disk-Elektrophorese multipler Formen von Arylamidasen. Untersuchungen über Arylamidasen menschlicher Gewebe, I. Mitteilung

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