RGD Reference Report - Rat tissue kallikrein releases a kallidin-like peptide from rat low-molecular-weight kininogen. - Rat Genome Database

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Rat tissue kallikrein releases a kallidin-like peptide from rat low-molecular-weight kininogen.

Authors: Hilgenfeldt, U  Stannek, C  Lukasova, M  Schnolzer, M  Lewicka, S 
Citation: Hilgenfeldt U, etal., Br J Pharmacol. 2005 Dec;146(7):958-63.
RGD ID: 1641801
Pubmed: PMID:16231010   (View Abstract at PubMed)
PMCID: PMC1751235   (View Article at PubMed Central)
DOI: DOI:10.1038/sj.bjp.0706409   (Journal Full-text)

The kallikrein-kinin system is subdivided into the plasma and tissue-kallikrein-kinin system, with bradykinin (BK) and kallidin (KAL) (Lys(0)-bradykinin) as functional peptides. This occurs in both humans and other mammals. Both peptides are released by plasma and tissue-kallikrein. BK, but not KAL, has been detected in rats until now. One can explain this observation by the structural differences found in the sequence of rat high- and low-molecular kininogen containing an Arg-residue instead of a Lys-residue in front of the N-terminus of the BK sequence. Nevertheless, we were able to measure a kallidin-like peptide (KLP), in rat plasma and urine, using a specific KAL antiserum.In order to confirm our data, we isolated low-molecular-weight kininogen from rat plasma and incubated it with purified rat glandular kallikrein. The generated peptide was retained on a high-pressure liquid chromatography column and displaced by an excess of angiotensin I. The KLP-containing fraction was identified with the KLP radioimmunoassay. A specific ion signal with a mass to charge ratio (m/z) of 1216.73 was detected with matrix-assisted laser desorption/ionization mass spectrometry.As proposed earlier, the structure of this peptide is Arg(1)-KAL, instead of Lys(1)-KAL. The structural similarity between the Lys- and the Arg-residue explains the high crossreactivity (80%) of KLP with the specific KAL antibody.The incubation of KLP with angiotensin-converting enzyme yields two molecules with masses of 913.4 and 729.3 containing the sequence H-Arg-Arg-Pro-Pro-Gly-Phe-Ser-Pro-OH and H-Arg-Arg-Pro-Pro-Gly-Phe-OH. The enzymatic cleavage could be inhibited by captopril.The data suggest that in rats, as in other mammals, the tissue kallikrein-kinin system mediates its physiological effects via a kallidin-like peptide, which is Arg(1)-kallidin (Arg(0)-bradykinin).



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Klk1Ratendopeptidase activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Klk1  (kallikrein 1)

Objects referenced in this article
Gene Klk1c12 kallikrein 1-related peptidase C12 Rattus norvegicus

Additional Information