Purification and properties of human kidney dipeptidases

Sugiura, Masahiro; Ito, Y.; Hirano, Kazuyuki; Sawaki, Shunji

doi:10.1016/0005-2744(78)90086-4

Cited by 13 publications

(11 citation statements)

References 19 publications

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“…However, carbapenems are rapidly metabolized in vivo, resulting in poor urinary recovery, because they are susceptible to renal dehydropeptidase I (4). Renal dipeptidase has been purified from human (10) and swine (2, 3) kidney.…”

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Purification and characterization of human renal dehydropeptidase I

Mitsuhashi¹,

Fuse²,

Mikami³

et al. 1988

Antimicrob Agents Chemother

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confidence: 99%

Purification and characterization of human renal dehydropeptidase I

Mitsuhashi¹,

Fuse²,

Mikami³

et al. 1988

Antimicrob Agents Chemother

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“…Human tissue was supplied by the Kobe University School of Medicine. The enzymes were either purified or partially purified by the methods of Campbell et al (4,5) and Sugiura et al (20), modified as described below.…”

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confidence: 99%

Stability of meropenem and effect of 1 beta-methyl substitution on its stability in the presence of renal dehydropeptidase I

Fukasawa

Sumita

Harabe

et al. 1992

Antimicrob Agents Chemother

125

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The stability of meropenem in the presence of renal dehydropeptidase I (DHP-I) varied extremely with the animal source of the enzyme. Meropenem, compared with imipenem, was rather easily hydrolyzed by DHP-Is from mice, rabbits, and monkeys, while it showed a higher resistance to guinea pig and beagle dog DHP-Is. In addition, meropenem was four times more resistant than imipenem to human DHP-I. The 1 beta-methyl substituent on carbapenems, i.e., meropenem and 1 beta-methyl imipenem, made them considerably more resistant to mouse and swine DHP-Is than the 1-unsubstituted derivatives are.

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“…Renal dipeptidase (dehydropeptidase-I, EC 3.4.14.1 1) isolated from hog or human kidney is capable of hydrolyzing a variety of dipeptides (Campbell et al, 1966;Sugiura et al, 1978) and inactivating antibiotics containing a p-lactam ring (Kropp et al, 1982;Mikami et al, 1982;Mitsuhashi et al, 1988). These antibiotics may cause direct harmful effects on various kinds of animal or human cells or organs in addition to antimicrobial or anticancer actions.…”

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Differentiation of clara cells and pneumocytes of the rat by means of enzyme‐ and immunohistochemistry

Kudo

1994

Anat. Rec.

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Localization of non-specific esterases, Cu-Zn superoxide dismutase and dehydropeptidase-I, in rat lung was investigated enzyme-cytochemically or immunohistochemically. Esterase was demonstrated in Clara cells, type II pneumocytes, and septal cells (or vitamin A-storing lung cells), to a somewhat lesser extent in type I pneumocytes and ciliated epithelial cells of the bronchioles, and to a minor extent in interstitial fibroblasts of the alveolar septum. Large amounts of esterase reaction product were deposited in the rough endoplasmic reticulum and the nuclear envelope in Clara cells, type II pneumocytes, and septal cells, in addition to smaller amounts in other organelles. No reaction product was found in macrophages (histiocytes) in alveolar septi and alveolar macrophages, except for the primary lysosomes or phagolysosomes and trace amounts in the Golgi vesicles, and none in endothelial cells of alveolar blood capillaries, except for primary lysosomes. Immunolocalization of Cu-Zn superoxide dismutase was generally limited to a particular area of Clara cells. A constriction occurred in the apical cytoplasm of Clara cells between an immunoreactive dome-like protrusion and the non-immunoreactive cytoplasm of the supranuclear area, and the dome-like protrusion appeared to be pinched off in a ball-like or oval form. Immunolocalization of dehydropeptidase-I was demonstrated in a dome-like protrusion or supranuclear area of Clara cells or throughout the cytoplasm and in the surface plasma membrane of mesothelial cells. The presence of these enzymes in Clara cells suggests a contribution to the detoxification system of the lung, together with cytochrome p-450-dependent monooxygenase systems.

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Purification and properties of human kidney dipeptidases

Cited by 13 publications

References 19 publications

Purification and characterization of human renal dehydropeptidase I

Purification and characterization of human renal dehydropeptidase I

Stability of meropenem and effect of 1 beta-methyl substitution on its stability in the presence of renal dehydropeptidase I

Differentiation of clara cells and pneumocytes of the rat by means of enzyme‐ and immunohistochemistry

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