The thiol enzyme from rat spleen that produces bradykinin potentiating peptide from rat plasma

Yamafuji, Kaoru; Taniguchi, Yoriko; Sakamoto, Eri

doi:10.1016/0162-3109(95)00080-1

Cited by 9 publications

(13 citation statements)

References 6 publications

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“…Later, other BPPs were isolated from the venom of other snakes (Kato and Suzuki, 1971;Cintra et al, 1990;Ferreira et al, 1992), spiders (Akchumov et al, 1992) and scorpions (Ferreira et al, 1993). Peptides with bradykinin potentiating activity can also be formed by hydrolysis of proteins taken from serum (Yamafuji et al, 1996), hemoglobin (Piot et al, 1992;Ivanov et al, 1997), and milk (Henriques et al, 1987;Lebrun et al, 1995). The main effects of natural ACE inhibition are not restricted to the reduction of angiotensin II production, but also include a decrease in bradykinin degradation, synergistically leading to several outcomes in the progression of the cell cycle.…”

Section: Discussionmentioning

confidence: 99%

Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII

Farias

Sabatini

Sampaio

et al. 2006

Biological Chemistry

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Extracellular matrix and soluble plasma proteins generate peptides that regulate biological activities such as cell growth, differentiation and migration. Bradykinin, a peptide released from kininogen by kallikreins, stimulates vasodilatation and endothelial cell proliferation. Various classes of substances can potentiate these biological actions of bradykinin. Among them, the best studied are bradykinin potentiating peptides (BPPs) derived from snake venom, which can also strongly inhibit angiotensin I-converting enzyme (ACE) activity. We identified and synthesized sequences resembling BPPs in the vicinity of potential proteolytic cleavage sites in the collagen XVIII molecule, close to endostatin. These peptides were screened as inhibitors of human recombinant wild-type ACE containing two intact functional domains; two full-length ACE mutants containing only a functional C- or N-domain catalytic site; and human testicular ACE, a natural form of the enzyme that only contains the C-domain. The BPP-like peptides inhibited ACE in the micromolar range and interacted preferentially with the C-domain. The proteolytic activity involved in the release of BPP-like peptides was studied in human serum and human umbilical-vein endothelial cells. The presence of enzymes able to release these peptides in blood led us to speculate on a physiological mechanism for the control of ACE activities.

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Section: Discussionmentioning

confidence: 99%

Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII

Farias

Sabatini

Sampaio

et al. 2006

Biological Chemistry

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“…Very recently new potentiating peptides have been isolated from the venom of B. jararaca [36]. Surprisingly peptides with potentiating activity have also been formed by the partial hydrolysis of proteins taken from serum [80], hemoglobin [38,66,81], milk [34,46], or wheat germ [51]. Also degradation fragments of angiotensin such as the heptapeptide 1-7 were found to potentiate the BK action [64].…”

Section: Introductionmentioning

confidence: 99%

Potentiation of bradykinin actions by analogues of the bradykinin potentiating nonapeptide BPP9α

Mueller

Gothe

Siems³

et al. 2005

Peptides

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Synthetic analogues of the bradykinin potentiating nonapeptide BPP9alpha indicate significantly different structural requirements for potentiation of the bradykinin (BK)-induced smooth muscle contraction (GPI) and the inhibition of isolated somatic angiotensin I-converting enzyme (ACE). The results disprove the ACE inhibition as the only single mechanism and also the direct interaction of potentiating peptides with the bradykinin receptors in transfected COS-7 cells as molecular mechanism of potentiation. Our results indicate a stimulation of inositol phosphates (IPn) formation independently from the B2 receptor. Furthermore, the results with La3+ support the role of extracellular Ca2+ and its influx through corresponding channels. The missing effect of calyculin on the GPI disproves the role of phosphatases in the potentiating action. These experimental studies should not only contribute to a better understanding of the potentiating mechanisms but also incorporate a shift in the research towards the immune system, in particular towards the immunocompetent polymorphonuclear leukocytes. The chemotaxis of these cells can be potentiated most likely by exclusive inhibition of the enzymatic degradation of bradykinin. Thus the obtained results give evidence that the potentiation of the bradykinin action can occur by different mechanisms, depending on the system and on the applied potentiating factor.

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“…Although a relatively small number of putative endogenous BPPs are genomically encoded, the snake venom gland of Bothrops jararaca [17–19], and from other species such as spider [20] and scorpion [21], produces a large variety of BPP molecules. Surprisingly, peptides with Bk‐potentiating activity can also be generated by limited proteolysis of seric proteins [22], hemoglobin [19,23,24], milk [25,26] or wheatgerm [27]. However, the most important characteristic of classical BPPs is that they are not Bk analogs or agonists; they function by a different, uncharacterized mechanism other than synergistic action and/or prevention of Bk proteolysis [6,7].…”

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confidence: 99%

A novel bradykinin potentiating peptide isolated from Bothrops jararacussu venom using catallytically inactive oligopeptidase EP24.15

et al. 2008

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Characterization of the peptide content of venoms has a number of potential benefits for basic research, clinical diagnosis, development of new therapeutic agents, and production of antiserum. Here, we use a substrate‐capture assay that employs a catalytically inactive mutant of thimet oligopeptidase (EC 3.4.24.15; EP24.15) to identify novel bioactive peptides in Bothrops jararacussu venom. Of the peptides captured with inactive EP24.15 and identified by mass spectrometry, three were previously identified bradykinin‐potentiating peptides (BPP),

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The thiol enzyme from rat spleen that produces bradykinin potentiating peptide from rat plasma

Cited by 9 publications

References 6 publications

Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII

Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII

Potentiation of bradykinin actions by analogues of the bradykinin potentiating nonapeptide BPP9α

A novel bradykinin potentiating peptide isolated from Bothrops jararacussu venom using catallytically inactive oligopeptidase EP24.15

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