Comparison of soluble and membrane-bound pyroglutamyl peptidase I activities in rat brain tissues in the presence of detergents

doi:10.1016/0143-4179(95)90092-6

Neuropeptides

Volume 29, Issue 2, August 1995, Pages 103-107

https://doi.org/10.1016/0143-4179(95)90092-6 Get rights and content

Abstract

Pyroglutamyl peptidase I activity from soluble and membrane-bound fractions of rat brain homogenates is inhibited by the presence of sodium deoxycholate but not by triton X-100. Biobeads SM2, a polystyrene adsorbent reported to be useful in removing detergents from aqueous solutions, inhibits enzymatic activity in both fractions regardless of the presence of these detergents, probably because of partial adsorption of the enzyme by the polymeric microspheres. These effects seem to be enzyme-specific since other aminopeptidase activities are not affected by detergents or biobeads. The results suggest that soluble and membranebound forms of the enzyme represent the same protein in two different cell compartments.

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Cited by (12)

Ontogeny of prolyl endopeptidase and pyroglutamyl peptidase I in rat tissues
2007, Regulatory Peptides
Prolyl endopeptidase and pyroglutamyl peptidase I are enzymes which participate in the degradation of thyrotropin-releasing hormone (TRH), a hormone which is thought to play an important role in the development of organs and tissues. Here, we have characterized the ontogeny of TRH degrading enzyme activity in the brain cortex, lung, heart, kidney and liver. Overall, prolyl endopeptidase activity was found to be 2 to 5 fold higher in newborn vs. adult rat tissues, with the exception of the soluble form in the liver and the particulate form in the lung. In contrast, the developmental profile of pyroglutamyl peptidase I activity was found to be more variable and tissue dependent. These results corroborate the idea that both enzymes play important, tissue-specific roles during the development and maturation of rat organs.
Subcellular distribution of membrane-bound aminopeptidases in the human and rat brain
2005, Neuroscience Letters
We evaluated the subcellular distribution of four membrane-bound aminopeptidases in the human and rat brain cortex. The particulate enzymes under study—puromycin-sensitive aminopeptidase (PSA), aminopeptidase N (APN), pyroglutamyl-peptidase I (PG I) and aspartyl-aminopeptidase (Asp-AP)—were fluorometrically measured using β-naphthylamide derivatives. Membrane-bound aminopeptidase activity was found in all the studied subcellular fractions (myelinic, synaptosomal, mitochondrial, microsomal and nuclear fractions), although not homogenously. Human PSA showed highest activity in the microsomal fraction. APN was significantly higher in the nuclear fraction of both species, while PG I showed highest activity in the synaptosomal and myelinic fractions of the human and rat brain. The present results suggest that in addition to inactivating neuropeptides at the synaptic cleft, these enzymes may participate in other physiological processes. Moreover, these peptidases may play specific roles depending on their activity levels at the different subcellular structures where they are localized.
Pyroglutamyl peptidase I and prolyl endopeptidase in human semen: Increased activity in necrozoospermia
2004, Regulatory Peptides
Thyrotropin-releasing hormone (TRH) and its analogues have been reported to have important functions in human semen. In the present paper, we have characterized the activity of the TRH-degrading enzymes pyroglutamyl peptidase I and prolyl endopeptidase in the fluid and prostasomes of human semen and in subcellular fractions of the corresponding sperm. Enzymatic activities were measured fluorimetrically using β-naphthylamine derivatives as substrate. Activity associated with both enzymes was detected in seminal fluid and in the prostasome fraction, as well as in soluble and particulate sperm subcellular fractions. Pyroglutamyl-peptidase I activity presented highest levels in the particulate sperm fraction, whereas the activity of prolyl endopeptidase was maximal in the soluble sperm fraction. In addition, we compared the activity of both enzymes in different seminal fractions in normozoospermic, fertile men and in subfertile patients with different abnormalities revealed by spermiogram analysis (astenozoospermia, necrozoospermia and teratozoospermia). The activities of pyroglutamyl peptidase I and prolyl endopeptidase in necrozoospermia were found to be higher in the corresponding soluble and particulate sperm fractions, respectively, with respect to those measured in normozoospermic semen. The results of the present study indicate that these enzymes may participate in regulating the levels of seminal TRH analogues and in mediating sperm death associated with necrozoospermia.
Effect of the disruption of body fluid balance on pyroglutamyl aminopeptidase (Type-1) in rat brain structures
2002, Neuropeptides
The activity of soluble and membrane-bound pyroglutamyl aminopeptidase Type-1 (PAP I) was evaluated in the hypothalamus, hippocampus, thalamus, brain cortex, and pituitary gland of rats after applying certain hydromineral challenges. Compared to euhydrated rats, decreased enzyme activity was found in the hypophysis of rats deprived of water for 48 h, or rats drinking ad libitum hypertonic sodium chloride solution (2%) for 6 days or distilled water for 6 days and then submitted to acute water overload. PAP I cleaves the pGlu-amino acid bond of neuropeptides such as thyroliberin, luliberin, neurotensin, and bombesin. The decay of particulate PAP I activity may cause an increase of these pyroglutamate peptides in the whole pituitary. Although the deleterious or pro-homeostatic influence of this decay remains to be elucidated, the present data provide evidence for the involvement of this enzyme activity at this anatomical location in the water–electrolyte imbalance.
Subcellular ontogeny of brain pyroglutamyl peptidase I
2000, Peptides
The present work studies pyroglutamyl-peptidase I activity in several subcellular fractions of the developing brain. In the synaptosomal fraction, soluble pGlu-peptidase I activity is low until postnatal Day 9 (with a peak at postnatal Day 2) and the activity increases at postnatal Day 15. In later stages there are not significant changes of synaptosomal pGlu-peptidase I activity. However, in the cytosolic fraction the activity is high from ED22 until postnatal Day 9, and afterwards decreases. The changes in the particulate fractions are generally less drastic.
Role of central and peripheral aminopeptidase activities in the control of blood pressure: A working hypothesis
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Comparison of soluble and membrane-bound pyroglutamyl peptidase I activities in rat brain tissues in the presence of detergents

Abstract

J. Pharmac. Sci.

Neuropeptides

Neuropeptides

Biochim. Biophys. Acta

Biochim. Biophys. Acta

Anal. Biochem.

Biochem. Pharmacol.

Trends Biochem. Sci.

Bovine pituitary pyrrolidonecarboxylyl peptidase

Endocrinology

Specificity of a serum peptidase hydrolyzing thyroliberin at the pyroglutamyl-histidine bond

Eur. J. Biochem.