Dipeptidyl peptidase-II activity in cultured astroglial cells from neonatal rat brain

Stevens, Bruce R.; Raizada, Mohan K.; Sumners, Colin; Fernandez, Alarico

doi:10.1016/0006-8993(87)90775-x

Cited by 13 publications

(2 citation statements)

References 8 publications

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“…In an immunohistochemical study of rat brain slices, Ito et al (1986) detected DPP I1 in lysosomes and parts of the Golgi apparatus. Gorenstein et al (1 98 1) localized hydrolyzing activity for Lys-Ala-Cmethoxy-NNap only in neurons, but probably DPP I1 also exists in growing glial elements (Koshiya et al, 1984;Stevens et al, 1987). Whether differences in the localization of the membrane-associated and soluble DPP I1 exist or not remains to be established.…”

Section: Peptide Specificity and Possible Functionmentioning

confidence: 99%

Purification of Two Dipeptidyl Aminopeptidases II from Rat Brain and Their Action on Proline‐Containing Neuropeptides

Mentlein

Struckhoff

1989

Journal of Neurochemistry

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From the soluble and membrane fractions of rat brain homogenate, two enzymes that liberate dipeptides of the type Xaa-Pro from chromogenic substrates were purified to homogeneity. The two isolated dipeptidyl peptidases had similar molecular and catalytic properties: For the native proteins, molecular weights of 110,000 were estimated; for the denatured proteins, the estimate was 52,500. Whereas the soluble peptidase yielded one band of pI 4.2 after analytical isoelectric focusing, two additional enzymatic active bands were detected between pI 4.2 and 4.3 for the membrane-associated form. As judged from identical patterns after neuraminidase treatment, both peptidases contained no sialic acid. A pH optimum of 5.5 was estimated for the hydrolysis of Gly-Pro- and Arg-Pro-nitroanilide. Substrates with alanine instead of proline in the penultimate position were hydrolyzed at comparable rates. Acidic amino acids in the ultimate N-terminal position of the substrates reduced the activities of the peptidases 100-fold as compared with corresponding substrates with unblocked neutral or, especially, basic termini. The action of the dipeptidyl peptidase on several peptides with N-terminal Xaa-Pro sequences was investigated. Tripeptides were rapidly hydrolyzed, but the activities considerably decreased with increasing chain length of the peptides. Although the tetrapeptide substance P 1-4 was still a good substrate, the activities detected for the sequential liberation of Xaa-Pro dipeptides from substance P itself or casomorphin were considerably lower. Longer peptides were not cleaved. The peptidases hydrolyzed Pro-Pro bonds, e.g., in bradykinin 1-3 or 1-5 fragments, but bradykinin itself was resistant. The enzymes were inhibited by serine protease inhibitors, like diisopropyl fluorophosphate or phenylmethylsulfonyl fluoride, and by high salt concentrations but not by the aminopeptidase inhibitors bacitracin and bestatin. Based on the molecular and catalytic properties, both enzymes can be classified as species of dipeptidyl peptidase II (EC 3.4.14.2) rather than IV (EC 3.4.14.5). However, some catalytic properties differentiate the brain enzyme from forms of dipeptidyl peptidase II of other sources.

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Section: Peptide Specificity and Possible Functionmentioning

confidence: 99%

Purification of Two Dipeptidyl Aminopeptidases II from Rat Brain and Their Action on Proline‐Containing Neuropeptides

Mentlein

Struckhoff

1989

Journal of Neurochemistry

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“…Enzymatic activity attributed to DP-II was detected in brain homogenates [186,187] and histochemically in specific neuronal populations in rat brain by Gorenstein et al [188]. Later studies demonstrated its presence in glial cells [189] and speculated its association with astrocyte differentiation [190].…”

Section: Expression Of Dpp-iv and Related Proteases In Normal Brain Amentioning

confidence: 98%

Dipeptidyl Peptidase-IV and Related Proteases in Brain Tumors

Bušek¹,

Šedo²

2013

Evolution of the Molecular Biology of Brain Tumors and the Therapeutic Implications

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Marmoset Fine B Cell and T Cell Epitope Specificities Mapped onto a Homology Model of the Extracellular Domain of Human Myelin Oligodendrocyte Glycoprotein

Mesleh

Belmar

et al. 2002

Neurobiology of Disease

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Dipeptidyl peptidase-II activity in cultured astroglial cells from neonatal rat brain

Cited by 13 publications

References 8 publications

Purification of Two Dipeptidyl Aminopeptidases II from Rat Brain and Their Action on Proline‐Containing Neuropeptides

Purification of Two Dipeptidyl Aminopeptidases II from Rat Brain and Their Action on Proline‐Containing Neuropeptides

Dipeptidyl Peptidase-IV and Related Proteases in Brain Tumors

Marmoset Fine B Cell and T Cell Epitope Specificities Mapped onto a Homology Model of the Extracellular Domain of Human Myelin Oligodendrocyte Glycoprotein

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