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At least 973 records · Page 54Linked to original sources
PubMed1975

Procollagen peptidase: its mode of action on the native substrate.

Procollagen peptidase was recovered from the medium of human and mouse fibroblast cultures by precipitation with ammonium sulfate. The test substrate for the in vitro enzymatic reaction was radioactively-labeled, disulfide-linked procollagen prepared from the medium of human fibroblast cultures. The enzymatic digests were analyzed by electrophoresis in polyacrylamide gets containing sodium dodecyl sulfate and urea. The human and mouse enzymes reacted with the substrate to generate the same intermediates and final products. Procollagen peptidase acts as an endopeptidase which cleaves each of the three procollagen chains in turn. The final products of the reaction are collagen and a three-chain, disulfide-linked fragment derived from the nonhelical aminoterminal residues of procollagen.

Animals↗
PubMed1981

Membrane assembly from purified components. II. Assembly of M13 procoat into liposomes reconstituted with purified leader peptidase.

The major coat protein of coliphage M13 is an integral protein of the E. coli plasma membrane prior to its assembly into new virus particles. It is generated from its precursor, procoat, by a membrane-bound leader peptidase. We now describe the reconstitution of a highly purified preparation of this enzyme into vesicles of E. coli phospholipids. These vesicles bind procoat made in vitro and procoat isolated from in vitro synthesis. Both the crude and the purified substrates were converted post-translationally to coat protein. A significant proportion of the coat protein becomes inserted into the vesicle bilayer, with the N terminus facing the vesicle interior and the C terminus exposed to the external medium. These results strongly suggest that highly purified leader peptidase from E. coli and phospholipids are the only components necessary to mediate the binding, processing and insertion of this integral membrane protein.

Coliphages↗
PubMed1989

Protection of endogenous enkephalin degradation from peptidases in human serum by actinonin.

This paper describes a new method for detecting the endogenous enkephalin level in human serum without interference from serum peptidases and contaminating proteins. The method consists of a combination of addition of a peptidase inhibitor, actinonin to serum and dialysis. The activity of enkephalin degrading enzymes was completely abolished by actinonin. Furthermore, contaminating proteins which interfered with RIA assay of enkephalins were removed by the dialysis process. This combination process enabled precise detection of the concentration of enkephalin-like substances in human serum. The mean normal serum level of leucine-enkephalin assayed by this method in 12 healthy volunteers was 93.4 pg/ml.

Adult↗
PubMed1991

Receptor-selective, peptidase-resistant agonists at neurokinin NK-1 and NK-2 receptors: new tools for investigating neurokinin function.

The pharmacological profiles of two novel neurokinin agonists have been investigated. delta Ava[L-Pro9,N-MeLeu10]SP(7-11) (GR73632) and [Lys3,Gly8-R-gamma-lactam-Leu9] NKA(3-10) (GR64349) are potent and selective agonists at NK-1 and NK-2 receptors respectively. In the guinea-pig isolated trachea preparation, contractions induced by these agonists were largely unaffected by inclusion of peptidase inhibitors in the bathing medium, indicating that these agonists are resistant to metabolism by peptidases. In the anaesthetised guinea-pig, both agonists were more potent bronchoconstrictor agents than either NKA or the SP analogue, SP methylester. In the anaesthetised rat, the NK-1 agonist, GR73632 was more potent than SP, NKA or NKB at causing the histamine-independent extravasation of plasma proteins into the skin after intradermal administration. The NK-2 agonist, GR64349 and the NK-3 agonist, senktide were without significant effect in this model. These agonists are useful tools for characterizing neurokinin receptor-mediated actions both in vitro and in vivo.

Administration, Cutaneous↗
PubMed1995

Characterization of a serine peptidase responsible for the inactivation of endogenous cholecystokinin in human brain.

Depolarization of slices of human cerebral cortex releases cholecystokinin-8 immunoreactivity, only a fraction of which is recovered in intact immunoreactive form in the medium. This suggests that extensive hydrolysis takes place during short incubations. In the presence of diisopropylfluorophosphate, a serine reagent, the recovery is nearly doubled, however, consistent with the involvement of a serine peptidase activity. The latter was characterized by assessing the protective effects of a series of serine protease inhibitors belonging to the families of peptide chloromethylketones or boronic acids. The relative potency of these inhibitors was similar to corresponding values previously found with rat brain slices indicating that a similar serine peptidase activity is responsible for endogenous cholecystokinin inactivation in the two species.

Amino Acid Sequence↗
PubMed1996

A secreted peptidase involved in T cell beta-endorphin metabolism.

Beta-endorphin metabolism by CD4+ and CD8+ T cells, and the thymoma cell line, EL4, was investigated. In all three cell types, extracellular beta-endorphin was metabolized exclusively by a secreted, metal-dependent, thiol peptidase. The enzyme activity is expressed constitutively in EL4 cells and following activation of CD4+ and CD8+ T cells with anti-CD3 antibody. The enzyme is not one of the proteinases associated with cytolytic T cells and does not appear to be identical with any previously described beta-endorphin metabolizing enzyme. The enzyme cleaves beta-endorphin at approximately equal rates at either of two sites to yield beta-endorphin(1-17) (which is gamma-endorphin), beta-endorphin(1-18), beta-endorphin(18-31) and beta-endorphin(19-31). Evidence in the literature indicates that these N- and C-terminal peptides which contain, respectively, the opioid and non-opioid receptor binding domains of beta-endorphin, are biologically active. Thus, it is likely that this new T cell peptidase has important immunoregulatory activity.

Amino Acid Sequence↗
PubMed1982

Peptidases from Plasmodium falciparum cultured in vitro.

An acid peptidase that degrades hemoglobin optimally at pH 3.5, a neutral aminopeptidase and an alkaline endopeptidase that acts on an alpha-N-blocked synthetic substrate have been demonstrated in Plasmodium falciparum in culture. The enzymes were shown to be distinct by anion exchange chromatography, gel filtration on Sephadex G-200 and isoelectric focusing. The activities of the acid peptidase and the aminopeptidase were inhibited by antimalarial compounds.

Animals↗
PubMed1982

Mechanism of neurotensin degradation by rat brain peptidases.

Neurotensin is degraded by peptidases present in soluble and particulate (25000 x g) fractions of rat hypothalamus, thalamus, cortex and pituitary, the soluble fraction of the hypothalamus having the highest activity. High performance liquid chromatography and amino acid analysis were used to identify the degradation pathway. The main product in both fractions was [1-8]neurotensin and the corresponding C-terminal fragment [9-13]neurotensin was identified. [1-10]Neurotensin was also identified, proportionately more of this peptide being produced by the particulate rather than the soluble fraction. In the presence of dithiothreitol, [1-7]neurotensin and [1-10]neurotensin were major products particularly in the soluble fraction. These results suggest that the main sites of cleavage of neurotensin by rat brain peptidases are the Arg8-Arg9, Pro10-Tyr11 and Pro7-Arg8 bonds.

Amino Acid Sequence↗
PubMed1986

Axonal transport of substance P-hydrolyzing peptidase in rat sciatic nerves.

The axonal transport of substance P-hydrolyzing peptidase was studied both 2 and 10 days after the ligation of rat sciatic nerves. A peptidase(s) hydrolyzing substance P at the bonds of Phe7-Phe8 and Phe8-Gly9 was found to have accumulated to about 2 times the normal amount in the proximal segment 10 days after ligation. This enzyme activity was inhibited by ethylenediamine tetraacetate or dithiothreitol. These results suggest that this is a metalloendopeptidase which is slowly transported to inactivate neuropeptides in the nerve terminals.

Animals↗
PubMed1989

Peptidases and proteases of Escherichia coli and Salmonella typhimurium.

A number of peptidases and proteases have been identified in Escherichia coli. Although their specific physiological roles are often not known, some of them have been shown to be involved in: the maturation of nascent polypeptide chains; the maturation of protein precursors; the signal peptide processing of exported proteins; the degradation of abnormal proteins; the use of small peptides as nutrients; the degradation of colicins; viral morphogenesis; the inactivation of some regulatory proteins for which a limited lifetime is a physiological necessity. Some of these enzymes act in concert to carry out specific functions. At present, twelve peptidases and seventeen proteases have been characterized. The specificity for only a few of them is known. The possible roles and the properties of these enzymes are discussed in this review.

Escherichia coli↗
PubMedDate not supplied

Degradation of alpha and beta neo-endorphin by rat brain membrane peptidases.

Fractionation of Triton-solubilized rat brain membranes on diethylaminoethyl-cellulose resolves two peptidases which hydrolyze beta-neo-endorphin. One of these peptidases was identified as Angiotensin Converting Enzyme by (a) its sensitivity to inhibition by the specific inhibitors MK422 and captopril, (b) by the identification of reaction products, and (c) by comparison to authentic angiotensin converting enzyme. In contrast, alpha-neo-endorphin hydrolysis by angiotensin converting enzyme could not be detected. The second enzyme active on beta-neo-endorphin was identified as an aminopeptidase. This aminopeptidase is identical to the previously described enkephalin-degrading aminopeptidase. The possible involvement of these enzymes in the metabolism of opioid peptides is discussed.

Aminopeptidases↗
PubMedDate not supplied

Peptidases involved in the catabolism of neurotensin: inhibitor studies using superfused rat hypothalamic slices.

In order to identify which peptidases are involved in the catabolism of neurotensin in the CNS, [3H-Tyr3,11]-neurotensin was superfused over rat hypothalamic slices in the presence and absence of peptidase inhibitors. The degree of degradation of the peptide was determined by reverse phase HPLC separation of 3H-labelled neurotensin from 3H-labelled products. Very little degrading activity was released from the slice into the medium during the superfusion. In the absence of inhibitors, 20 to 50% of 3H-neurotensin was degraded giving mainly 3H-Tyr along with other unidentified 3H-labelled products. Inhibitors of endopeptidase 24.11 (phosphoramidon) and proline endopeptidase (antibody) had no effect on the degradation. Captopril, an inhibitor of angiotensin converting enzyme, had a small inhibitory effect. In contrast, dynorphin(1-13), an inhibitor of a soluble, thiol dependent metallopeptidase which hydrolyses neurotensin at Arg8-Arg9, gave greater than 80% inhibition of 3H-neurotensin degradation in the slice preparation. 1,10-Phenanthroline, an inhibitor of metallopeptidases, was also an effective inhibitor. The dynorphin sequence responsible for the inhibition contains the Arg6-Arg7 bond. Other peptides (bradykinin and angiotensin) which are substrates of the soluble metallopeptidase also inhibited neurotensin breakdown by the slice. This evidence suggests that this thiol dependent metalloendopeptidase is the major neurotensin catabolizing enzyme in hypothalamic slices.

Animals↗
PubMed1996

Peptidase inhibitors improve recovery of substance P and calcitonin gene-related peptide release from rat spinal cord slices.

The purpose of present study was to determine whether peptidase activity affects the release of substance P (SP) and calcitonin gene-related peptide (CGRP) from spinal cord slices. When slices were exposed to various inhibitors of endopeptidase 24.11, the resting and capsaicin-stimulated release of SP were less than 0.04% and 0.20% total content per minute, respectively. Resting CGRP release was approximately 0.10% and stimulated release was 0.40%. The combination of 20 microM bacitracin, 100 microM phenylalanylalanine (Phe-Ala), and 50 microM p-chloromercuriphenylsulfonic acid (PCMS) significantly increased both resting and stimulated release of SP and CGRP at least two- or threefold. Doubling the concentration of PCMS and Phe-Ala did not further improve peptide release. These results demonstrate that recovery of peptides released from spinal cord slices is dependent in part on activity of multiple peptidases in the tissues.

4-Chloromercuribenzenesulfonate↗
PubMed1996

Peptidase-1 expression in some organs of the salamander Pleurodeles waltl submitted to a 12-day space flight.

In Pleurodeles, the peptidase-1 is a sex-linked enzyme encoded by two codominant genes (Pep-1A and Pep-1B) located on the Z and W sex chromosomes. The sexual genotype can be determined by the electrophoretic pattern of the peptidase from erythrocytes. ZAWB genotypic females characterized by 3 electrophoretic bands AA, AB and BB were embarked on Cosmos 2229. The pattern in ovary, muscles and gut issued from the embarked or synchrone females displayed the 3 characteristic bands. In heart and kidney, the bands AA and AB [correction of BB] were revealed, while the band BB appeared very faintly. The specific enzymatic activity in the same organs was compared. Except for the kidney, no statistical significant difference was observed between flight and synchrone samples. This enzyme can be efficiently used as sexual genotypic marker of Pleurodeles experimentally submitted to the effects of space environment.

Animals↗
PubMed1986

Stability of [D-Trp11]-neurotensin to rat brain peptidases.

The stability of neurotensin (NT) and a potent, long lasting analogue, [D-Trp11]-NT, to rat brain peptidases was compared by incubating the peptides with subcellular fractions (synaptosomes, synaptic membranes) and a purified endopeptidase from rat brain. Degradation of the peptides with time was followed by high performance liquid chromatography (HPLC). The rates of degradation (pmol/min/mg prot.) in synaptosomes were 890 (NT) and 59 [D-Trp11]-NT), and in synaptic membranes were 1180 (NT) and 12 ([D-Trp11]-NT). The main products of the degradation of [D-Trp11]-NT by synaptic peptidases (isolated by HPLC and characterized by amino acid analysis) were the 1-3, 1-4 and 6-13 fragments implying cleavage of [D-Trp11]-NT at the Tyr3-Glu4, Glu4-Asn5 and Asn5-Lys6 bonds. The rates of degradation of NT and [D-Trp11]-NT by the purified endopeptidase from rat brain were 27.2 and 0.76 pmol/min/microliter of enzyme solution respectively. This endopeptidase, which hydrolyses NT at Arg8-Arg9, may be responsible along with other endopeptidases for NT degradation at nerve terminals.

Animals↗
PubMed1994

The striatonigral dynorphin pathway of the rat studied with in vivo microdialysis--I. Effects of K(+)-depolarization, lesions and peptidase inhibition.

Extracellular levels of dynorphin B were analysed with in vivo microdialysis in the neostriatum and substantia nigra of halothane-anaesthetized rats. Dopamine and its metabolites, 3,4-dihydroxyphenyl-acetic acid and homovanillic acid, as well as GABA were simultaneously monitored. Chromatographic analysis revealed that the dynorphin B-like immunoreactivity measured in perfusates collected under basal and K(+)-depolarizing conditions co-eluted with synthetic dynorphin B. Dynorphin B, GABA and dopamine levels were Ca(2+)-dependently increased by K(+)-depolarization, while 3,4-dihydroxyphenylacetic acid and homovanillic acid levels were decreased. Dopamine and its metabolites, but not dynorphin B or GABA levels, were significantly decreased after a unilateral 6-hydroxydopamine injection into the left medial forebrain bundle. In contrast, following a unilateral injection of ibotenic acid into the striatum, dynorphin B and GABA levels were decreased by > 50% in striatum and substantia nigra on the lesioned side, whereas no significant changes were observed in basal dopamine levels. The inclusion of the peptidase inhibitor captopril (50-500 microM) into the nigral perfusion medium produced a concentration-dependent increase in nigral extracellular levels of dynorphin B. In the striatum, a delayed increase in dynorphin B and GABA levels could be observed following the nigral captopril administration, but this effect was not concentration-dependent. Thus, we demonstrate that extracellular levels of dynorphin B, dopamine and GABA can simultaneously be monitored with in vivo microdialysis. Extracellular dynorphin B appears to originate from neurons, since the levels were (i) increased in a Ca(2+)-dependent manner by K(+)-depolarization, and (ii) decreased by a selective lesion of the striatum, known to contain cell bodies of dynorphin neurons in the striatonigral pathway. Furthermore, (iii) the increase in nigral dynorphin B levels by peptidase inhibition suggests the presence of clearance mechanisms for the released dynorphin peptides.

Animals↗
PubMed1990

Cloning, nucleotide sequence and amplified expression of the gene encoding the extracellular metallo (Zn) DD-peptidase of Streptomyces albus G.

The gene encoding the extracellular metallo (Zn) DD-peptidase of Streptomyces albus G has been cloned in Escherichia coli DH5 alpha MCR via pBR322 or 325, and then transferred into Streptomyces lividans TK24 via pIJ486, with substantial amplification of the expressed DD-peptidase. The gene has the information for the synthesis of a 255 amino acid precursor, the amino terminal region of which has the characteristic features of a signal peptide. The primary structure as deduced from nucleotide sequencing confirms that previously determined by chemical methods except for the occurrence of an Asp instead of Asn at position 1 and an additional Ala immediately downstream of Pro67.

Amino Acid Sequence↗
PubMed1984

A comparative study of neurotensin inactivation by brain peptidases from different vertebrate species.

The products formed from mammalian neurotensin by peptidases in two subcellular fractions from rat, mouse, dove, terrapin and goldfish brain were separated and identified using high-performance liquid chromatography. The main neurotensin metabolites were [1-8]-, [1-10]- and [1-7]-sequences; goldfish and terrapin brain fractions also produced [1-11]- and [1-12]-fragments. Avian neurotensin was cleaved by peptidases in rat and dove brain fractions to [1-8]-, [9-13]-, [1-10]- and [1-12]-fragments. Similar mechanisms of inactivation were found for both mammalian and avian neurotensins .

Animals↗