Pathways for bradykinin formation and inflammatory disease

Kaplan, Allen P.; Joseph, Kusumam; Silverberg, Mark

doi:10.1067/mai.2002.121316

Cited by 262 publications

(196 citation statements)

References 145 publications

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“…Two cleavage sites were detected in bradykinin (Figure 4 A) , confi rming the results obtained with the extended bradykinin, which is generated by the proteolytic cleavage of the precursor kininogen-1 by the enzyme kallikrein (Kaplan et al , 2002 ). As a matter of fact, in rat, mouse, bovine, and human, the SPFR motif of kininogen-1 is conserved, but it is followed by a different carboxy terminal amino acid.…”

Section: Identifi Cation Of Substrate Cleavage Sitessupporting

confidence: 60%

Functional characterization of the Mycobacterium tuberculosis zinc metallopeptidase Zmp1 and identification of potential substrates

Petrera¹,

Amstutz²,

Gioia³

et al. 2012

Biological Chemistry

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Zinc metallopeptidases of bacterial pathogens are widely distributed virulence factors and represent promising pharmacological targets. In this work, we have characterized Zmp1, a zinc metallopeptidase identifi ed as a virulence factor of Mycobacterium tuberculosis and belonging to the neprilysin (NEP; M13) family, whose X-ray structure has been recently solved. Interestingly, this enzyme shows an optimum activity toward a fl uorogenic substrate at moderately acidic pH values (i.e., 6.3), which corresponds to those reported for the Mtb phagosome where this enzyme should exert its pathological activity. Substrate specifi city of Zmp1 was investigated by screening a peptide library. Several sequences derived from biologically relevant proteins were identifi ed as possible substrates, including the neuropeptides bradykinin, neurotensin, and neuropeptide FF. Further, subsequences of other small bioactive peptides were found among most frequently cleaved sites, e.g., apelin-13 and substance P. We determined the specifi c cleavage site within neuropeptides by mass spectrometry, observing that hydrophobic amino acids, mainly phenylalanine and isoleucine, are overrepresented at position P1 ′ . In addition, the enzymatic mechanism of Zmp1 toward these neuropeptides has been characterized, displaying some differences with respect to the synthetic fl uorogenic substrate and indicating that the enzyme adapts its enzymatic action to different substrates.

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Section: Identifi Cation Of Substrate Cleavage Sitessupporting

confidence: 60%

Functional characterization of the Mycobacterium tuberculosis zinc metallopeptidase Zmp1 and identification of potential substrates

Petrera¹,

Amstutz²,

Gioia³

et al. 2012

Biological Chemistry

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“…Celui-ci assure le contact du FXIIa et de la prékallicréine avec la surface. En présence de la surface et du KHPM, la kallicréine active d'autres molécules de FXII et libère le nonapeptide bradykinine par deux clivages protéolytiques à l'intérieur du KHPM (schéma inspiré de Kaplan et al [13]). …”

Section: Kerbiriou-nabiasunclassified

Les polyphosphates

Kerbiriou-Nabias

2010

Med Sci (Paris)

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“…In the absence of sufficient C1INH, factor XIIa effectively initiates a cascade leading to the local tissue production of bradykinin[3]. Factor XIIa accomplishes this by converting prekallikrein to kallikrein and also by activating a highly efficient autoactivation cycle, whereby factor XIIa acts on factor XII to produce additional factor XIIa[4]. This cycle efficiently up-regulates kallikrein production.…”

mentioning

confidence: 99%

Hereditary Angioedema Therapy: Kallikrein Inhibition and Bradykinin Receptor Antagonism

Riedl¹

2010

World Allergy Organization Journal

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Current strategies for the treatment of hereditary angioedema (HAE) include targeted inhibition or antagonism of the contact system, which is dysregulated in HAE patients by a C1 esterase inhibitor deficiency. Ecallantide, a plasma kallikrein inhibitor, and icatibant, a selective bradykinin-2 receptor antagonist, have recently been evaluated in clinical studies for the treatment of acute HAE attacks. Both drugs have demonstrated evidence of efficacy and safety in treating acute HAE episodes, with ecallantide approved for use in the United States and icatibant approved for use in Europe. As therapeutic options for HAE expand for both for prophylactic and acute treatment strategies, a number of patient-specific and drug-specific factors have emerged as important considerations when developing individualized HAE management plans. Optimization of HAE therapy will require further integration of new therapies into the current treatment paradigm.

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Pathways for bradykinin formation and inflammatory disease

Cited by 262 publications

References 145 publications

Functional characterization of the Mycobacterium tuberculosis zinc metallopeptidase Zmp1 and identification of potential substrates

Functional characterization of the Mycobacterium tuberculosis zinc metallopeptidase Zmp1 and identification of potential substrates

Les polyphosphates

Hereditary Angioedema Therapy: Kallikrein Inhibition and Bradykinin Receptor Antagonism

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