Evidence map›Paper›PMID 15949642›Full record

ArticlePeptides2005

Potentiation of bradykinin actions by analogues of the bradykinin potentiating nonapeptide BPP9alpha.

Sylvia Mueller, Rita Gothe, Wolf-Dieter Siems, Gabriele Vietinghoff, Inge Paegelow, Siegmund Reissmann

Open access · greenAbstract read
In one paragraph

Article in Peptides, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Human ACE and bradykinin B2 receptors form a complex at the plasma membrane.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2006
    Article
  6. Kallikrein activates bradykinin B2 receptors in absence of kininogen.American journal of physiology. Heart and circulatory physiology · 2006
    Article
  7. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Sylvia MuellerInstitute of Biochemistry and Biophysics, Biological and Pharmaceutical Faculty, Friedrich-Schiller-University, 07743 Jena, Germany.
Rita Gothe
Wolf-Dieter Siems
Gabriele Vietinghoff
Inge Paegelow
Siegmund Reissmann
Friedrich Schiller University Jena · DEUniversity of Rostock · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Amino Acid SequenceAngiotensin-Converting Enzyme InhibitorsAnimalsBradykininCalciumChlorocebus aethiopsCOS CellsDrug SynergismGuinea PigsHumansInositol PhosphatesMolecular Sequence DataMuscle ContractionMuscle, SmoothPeptidesPeptidyl-Dipeptidase AAngiotensin-Converting Enzyme InhibitorsBradykininCalciumInositol PhosphatesPeptidesPeptidyl-Dipeptidase APhosphoprotein PhosphatasesReceptor, Bradykinin B2Teprotide

Identifiers

PMID15949642
PMCPMC7115577
OpenAlexW2030547459

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.