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Carboxypeptidase N, polypeptide 1

Lysine Carboxypeptidase, kininase I
Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer comprised of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Angiotensin II, carboxypeptidase, ACID, Kallikrein, CAN
Papers on Lysine Carboxypeptidase
The role of kinin B1 receptor and the effect of angiotensin I-converting enzyme inhibition on acute gout attacks in rodents.
Ferreira et al., Santa Maria, Brazil. In Ann Rheum Dis, Jan 2016
Additionally, B1R immunoreactivity in ankle tissue and sensory neurons, kininase I activity and des-Arg(9)-bradykinin synovial levels were also measured.
Further pharmacological evaluation of a novel synthetic peptide bradykinin B2 receptor agonist.
Gobeil et al., Sherbrooke, Canada. In Biol Chem, 2013
Contraction assays using isolated mouse stomachs (containing kinin B1R, B2R, and kininase I- and II-like activities) showed that NG291 is a more potent contractant than BK and is inhibited by HOE-140 (B2R antagonist) but unaffected by R954 (B1R antagonist), whereas both decreased the potency of BK.
Both B1R and B2R act as intermediate signaling molecules in high glucose-induced stimulation of glutamate uptake in ARPE cells.
Park et al., Kwangju, South Korea. In J Cell Physiol, 2009
High glucose increased B1R and B2R mRNA and protein expression in a time-dependent manner, increased B1R and B2R translocation from the cytosol to the nucleus, and stimulated kininogen, kallikrein, and kininase I mRNA expression.
Targeted disruption of the gene encoding the murine small subunit of carboxypeptidase N (CPN1) causes susceptibility to C5a anaphylatoxin-mediated shock.
Wetsel et al., Houston, United States. In J Immunol, 2009
we report the generation of a mouse with complete CPN deficiency by targeted disruption of the CPN1 gene
Regulation of chemerin bioactivity by plasma carboxypeptidase N, carboxypeptidase B (activated thrombin-activable fibrinolysis inhibitor), and platelets.
Leung et al., Stanford, United States. In J Biol Chem, 2009
circulating CPN/CPB and platelets may potentially contribute to regulating the bioactivity of leukocyte chemoattractant chemerin
Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator.
Erdös et al., Chicago, United States. In Int Immunopharmacol, 2008
This review summarizes the structure, enzymatic properties and function of this enzyme, including insights gained by the recent elucidation of the crystal structure of the CPN catalytic subunit and structural modeling of the non-catalytic 83 kDa subunit.
Potentiation of bradykinin effect by angiotensin-converting enzyme inhibition does not correlate with angiotensin-converting enzyme activity in the rat mesenteric arteries.
Salgado et al., Ribeirão Preto, Brazil. In Hypertension, 2007
Recovery of BK was increased in both groups in the presence of a kininase I inhibitor and in the hypertensive group by neutral endopeptidase 24.11 inhibitor; however, ACE inhibition did not affect BK metabolism in both groups.
Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain.
Bode et al., Martinsried, Germany. In J Mol Biol, 2007
Normally, CPN circulates in blood plasma as a hetero-tetramer consisting of two 83 kDa (CPN2) domains each flanked by a 48 to 55 kDa catalytic (CPN1) domain.
Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation.
Tosato et al., Bethesda, United States. In Blood, 2005
carboxypeptidase N regulates the biologic activity of SDF-1alpha by reducing the chemokine-specific activity
Lead-induced hypertension: role of oxidative stress.
Sica et al., Orange, United States. In Curr Hypertens Rep, 2004
The pathogenesis of lead-induced hypertension is multifactorial, including such diverse mechanisms as: inactivation of endogenous nitric oxide and downregulation of soluble guanylate cyclase by reactive oxygen species (ROS), leading to a functional deficiency in nitric oxide; heightened sympathetic activity and plasma norepinephrine together with depressed vascular and elevated renal beta-adrenergic receptor density; elevated plasma angiotensin-converting enzyme (ACE) activity, plasma renin activity (PRA), angiotensin II (Ang-II), and aldosterone levels; increased kininase I and kininase II activities; lead-induced inhibition of vascular smooth muscle Na(+)-K+ ATPase, leading to a rise in cellular Na+ and, hence, Ca2+; and a possible rise in endothelin and thromboxane generation.
Role of aminopeptidases in the blood pressure regulation.
Mizutani et al., Nagoya, Japan. In Biol Pharm Bull, 2004
This review describes the roles of aminopeptidase A, placental leucine aminopeptidase and kininase I, which are enzymes responsible for hydrolyzing angiotensin II (AngII), vasopressin (AVP) and bradykinin (BK), respectively, in BP regulation.
Angiotensin converting enzyme (ACE) and neprilysin hydrolyze neuropeptides: a brief history, the beginning and follow-ups to early studies.
Erdös et al., Chicago, United States. In Peptides, 2004
Our investigations started when synthetic bradykinin became available and we could characterize two enzymes that cleaved it: kininase I or plasma carboxypeptidase N and kininase II, a peptidyl dipeptide hydrolase that we later found to be identical with the angiotensin I converting enzyme (ACE).
Umbilical plasma kininase I activity in fetal hypoxia.
Mizutani et al., Nagoya, Japan. In Horm Metab Res, 2003
To shed light on the role of bradykinin in preeclampsia in addition to acute hypoxia, we measured the activity of kininase I, the enzyme responsible for its degradation, in umbilical plasma.
Kininase I-type carboxypeptidases enhance nitric oxide production in endothelial cells by generating bradykinin B1 receptor agonists.
Skidgel et al., Chicago, United States. In Am J Physiol Heart Circ Physiol, 2003
Kininase I-type carboxypeptidases convert native kinin agonists for B(2) receptors into B(1) receptor agonists by specifically removing the COOH-terminal Arg residue.
Trypanosoma cruzi induces edematogenic responses in mice and invades cardiomyocytes and endothelial cells in vitro by activating distinct kinin receptor (B1/B2) subtypes.
Scharfstein et al., Rio de Janeiro, Brazil. In Faseb J, 2003
Our results indicate that captopril potentiates parasite invasion regardless of the kinin (B2/B1) activation pathways, whereas DL-2-mercaptomethyl-3-guanidino-ethylthiopropanoic acid (MGTA), an inhibitor of kininase I (carboxypeptidase M/N), selectively decreases parasite infectivity for B1R-expressing cells.
Structural characterization of the human carboxypeptidase D gene and its promoter.
Skidgel et al., Chicago, United States. In Int Immunopharmacol, 2002
CPD is a B-type (or kininase I-type) carboxypeptidase that cleaves C-terminal basic residues from proteins and peptides, such as Arg9 from bradykinin.
Pathogenesis of lead-induced hypertension: role of oxidative stress.
Vaziri, Irvine, United States. In J Hypertens Suppl, 2002
Several mechanisms have been shown to contribute to the pathogenesis of lead-induced hypertension: (1) avid oxidation and inactivation of endogenous nitric oxide (NO) by reactive oxygen species leading to functional NO deficiency; (2) increased sympathetic activity and circulating noradrenaline coupled with decreased vascular and elevated renal beta-adrenergic receptor density; (3) increased angiotensin-converting enzyme (ACE) activity and elevated plasma renin, angiotensin II and aldosterone levels; (4) heightened kininase I and kininase II activities; (5) possible increase in endothelin and thromboxane production; and (6) lead-mediated inhibition of vascular smooth muscle Na(+)-K+ ATPase leading to a rise in cellular Na+ and hence Ca2+ stores.
Involvement of the kallikrein-kinin system in the antihypertensive effect of the angiotensin converting enzyme inhibitors.
Brunner et al., Lausanne, Switzerland. In Br J Clin Pharmacol, 1988
4. The plasma activity of carboxypeptidase N (= kininase I), another pathway of bradykinin degradation, remained intact during a 1 week course of treatment with an ACE inhibitor in normal subjects.
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