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1. Full Text Circulating proteolytic products of carboxypeptidase N for early detection of breast cancer
by Li, Yaojun and Li, Yueguo and Chen, Tao and Kuklina, Anna S and Bernard, Paul and Esteva, Francisco J and Shen, Haifa and Ferrari, Mauro and Hu, Ye
Clinical Chemistry, ISSN 0009-9147, 01/2014, Volume 60, Issue 1, pp. 233 - 242
BACKGROUND: Carboxypeptidase N(CPN) is important in regulating vasoactive peptide hormones, growth factors, and cytokines by specifically cleaving their... 
BIOMARKERS | PEPTIDOME | PROTEIN | KININASE-I | TISSUE | ENRICHMENT | MEDICAL LABORATORY TECHNOLOGY | IDENTIFICATION | ANGIOTENSIN-CONVERTING ENZYME | TUMOR MICROENVIRONMENT | BRADYKININ | Peptides - blood | Peptides - antagonists & inhibitors | Early Detection of Cancer | Humans | Tumor Microenvironment | Biomarkers, Tumor - blood | Breast Neoplasms - enzymology | Animals | Peptidomimetics | Lysine Carboxypeptidase - metabolism | Female | Breast Neoplasms - diagnosis | Mice | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Biomarkers, Tumor - antagonists & inhibitors | Disease Models, Animal | Lysine Carboxypeptidase - blood | Protein research | Proteolysis | Proteases | Oncology, Experimental | Breast cancer | Research | Diagnosis | Health aspects | Methods | Cancer | Proteins | Studies | Biomarkers | Enzymes | Peptides | Carboxypeptidase N | Circulating peptides | Nanopore-based assay | Early detection
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2. Full Text Inactivation of C3a and C5a Octapeptides by Carboxypeptidase R and Carboxypeptidase N
by Campbell, William D and Lazoura, Eliada and Okada, Noriko and Okada, Hidechika
Microbiology and Immunology, ISSN 0385-5600, 02/2002, Volume 46, Issue 2, pp. 131 - 134
Pro‐carboxypeptidase R (proCPR), also known as thrombin‐activatable fibrinolysis inhibitor (TAFI), precursor of carboxypeptidase U and plasma carboxypeptidase... 
complement | inflammation | anaphylatoxin | carboxypeptidase | Carboxypeptidase | Complement | Inflammation | Anaphylatoxin | ACTIVATION | PROTEIN | MICROBIOLOGY | IMMUNOLOGY | ALTERNATIVE COMPLEMENT PATHWAY | PLASMA CARBOXYPEPTIDASE | Complement C5a - antagonists & inhibitors | Hydrolysis | Carboxypeptidase B2 - pharmacology | Time Factors | Complement C3a - antagonists & inhibitors | Humans | Carboxypeptidase B2 - blood | Lysine Carboxypeptidase - pharmacology | Lysine Carboxypeptidase - blood
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3. Full Text Major carboxypeptidase N deficiency
by Willemse, Johan L and Chen, David and Hendriks, Dirk F
Clinica Chimica Acta, ISSN 0009-8981, 03/2008, Volume 389, Issue 1-2, pp. 181 - 182
Carboxypeptidase N | Angio-oedema | Inflammation | ACE inhibitors | Deficiency | TAFI | carboxypeptidase N | PLASMA | ASSAY | deficiency | inflammation | SERUM | MEDICAL LABORATORY TECHNOLOGY | angio-oedema | PROCARBOXYPEPTIDASE-U TAFI | Reference Values | Reference Standards | Humans | Lysine Carboxypeptidase - deficiency | Lysine Carboxypeptidase - blood
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4. Full Text Metallopeptidase activities in hereditary angioedema: Effect of androgen prophylaxis on plasma aminopeptidase P
by Drouet, Christian, PhD and Désormeaux, Anik and Robillard, Josée, MSc and Ponard, Denise and Bouillet, Laurence, MD, PhD and Martin, Ludovic, MD, PhD and Kanny, Gisèle, MD, PhD and Moneret-Vautrin, Denise-Anne, MD and Bosson, Jean-Luc, MD, PhD and Quesada, Jean-Louis, MSc and López-Trascasa, Margarita, PhD and Adam, Albert, PhD
Journal of Allergy and Clinical Immunology, The, ISSN 0091-6749, 2008, Volume 121, Issue 2, pp. 429 - 433
Background Aminopeptidase P (APP) plays an important role in the catabolism of kinins in human plasma, mostly for des-Arg9 -bradykinin. Impaired degradation of... 
Allergy and Immunology | des-Arg 9-bradykinin | androgen | Hereditary angioedema | danazol | stanozolol | C1 inhibitor | bradykinin | aminopeptidase P | des-Arg | SYSTEM | ACE | ENDOGENOUS KININS | IMMUNOLOGY | PATHOPHYSIOLOGY | hereditary angioedema | ALLERGY | EDEMA | INFLAMMATION | des-Arg-bradykinin | INHIBITORS | RECEPTORS | Severity of Illness Index | Kinins - metabolism | Prospective Studies | Humans | Middle Aged | Aminopeptidases - blood | Angioedemas, Hereditary - prevention & control | Metabolism | Peptidyl-Dipeptidase A - blood | Metalloproteases - blood | Aged, 80 and over | Adult | Androgens - therapeutic use | Aged | Complement C1 Inhibitor Protein - metabolism | Angioedemas, Hereditary - blood | Angioedemas, Hereditary - physiopathology | Lysine Carboxypeptidase - blood | Drug therapy | Angioneurotic edema | Studies | Plasma | Ligands | Androgens | Patients | Rodents | Metalloproteases | Angioedema, Hereditary | Health | Aminopeptidases | Kinins | Peptidyl-Dipeptidase A | Complement C1 Inhibitor Protein | Life Sciences | Ecology, environment | Lysine Carboxypeptidase | des-Arg9-bradykinin
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5. Full Text The intrinsic enzymatic activity of plasma procarboxypeptidase U (TAFI) can interfere with plasma carboxypeptidase N assays
by Willemse, Johan L and Polla, Magnus and Hendriks, Dirk F
Analytical Biochemistry, ISSN 0003-2697, 2006, Volume 356, Issue 1, pp. 157 - 159
CHEMISTRY, ANALYTICAL | ACTIVATION | SERUM | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | Blood Chemical Analysis - methods | Humans | Carboxypeptidase B2 - blood | Substrate Specificity | Kinetics | Dipeptides - chemistry | In Vitro Techniques | Lysine Carboxypeptidase - blood | Enzymes
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6. Full Text Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator
by Skidgel, Randal A and Erdös, Ervin G
International Immunopharmacology, ISSN 1567-5769, 2007, Volume 7, Issue 14, pp. 1888 - 1899
Human carboxypeptidase N (CPN) was discovered in the early 1960s as a plasma enzyme that inactivates bradykinin and was identified 8 years later as the major... 
Anaphylatoxins | Human carboxypeptidase N | Proteolysis | Protein structure | Bradykinin | Plasmin | PROTEIN | KININASE-I | I-CONVERTING-ENZYME | CRYSTAL-STRUCTURE | bradykinin | IMMUNOLOGY | PROTAMINE REVERSAL | human carboxypeptidase N | protein structure | ACTIVE SUBUNIT | NITRIC-OXIDE PRODUCTION | plasmin | anaphylatoxins | ENDOTHELIAL-CELLS | PHARMACOLOGY & PHARMACY | B-1 RECEPTORS | proteolysis | CREATINE-KINASE | Protein Structure, Tertiary | Sequence Homology, Amino Acid | Amino Acid Sequence | Lysine Carboxypeptidase - chemistry | Lysine Carboxypeptidase - genetics | Humans | Models, Molecular | Crystallography, X-Ray | Structure-Activity Relationship | Amino Acid Motifs | Lysine Carboxypeptidase - blood | Physiological aspects
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7. Full Text Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen
by W Wang and D F Hendriks and S S ScharpÃ
Journal of Biological Chemistry, ISSN 0021-9258, 06/1994, Volume 269, Issue 22, pp. 15937 - 15944
A novel basic carboxypeptidase clearly different from carboxypeptidase N has been isolated from human plasma. It circulates as an enzymatically inactive... 
HUMAN-SERUM | CATALYZED HYDROLYSIS | ACTIVATOR | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | PURIFICATION | ANAPHYLATOXIN | TERMINAL LYSINE | BINDING-SITES | CREATINE-KINASE | FIBRIN | Amino Acid Sequence | Chromatography, Ion Exchange | Lysine Carboxypeptidase - isolation & purification | Molecular Weight | Humans | Enzyme Stability | Molecular Sequence Data | Substrate Specificity | Plasminogen - metabolism | Macromolecular Substances | Peptide Fragments - chemistry | Chromatography, Affinity | Carboxypeptidases - blood | Carboxypeptidase B2 | Carboxypeptidases - chemistry | Kinetics | Chromatography, Gel | Binding Sites | Carboxypeptidases - isolation & purification
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8. Full Text Pro-Carboxypeptidase R is an Acute Phase Protein in the Mouse, Whereas Carboxypeptidase N Is Not
by Sato, Tomoo and Miwa, Takashi and Akatsu, Hiroyasu and Matsukawa, Noriyuki and Obata, Kyoko and Okada, Noriko and Campbell, William and Okada, Hidechika
The Journal of Immunology, ISSN 0022-1767, 07/2000, Volume 165, Issue 2, pp. 1053 - 1058
Carboxypeptidase R (EC 3.4.17.20; CPR) and carboxypeptidase N (EC 3.4.17.3; CPN) cleave carboxyl-terminal arginine and lysine residues from biologically active... 
HUMAN-SERUM | FIBRINOLYSIS | THROMBOMODULIN | PLASMA PROCARBOXYPEPTIDASE-B | ARGININE CARBOXYPEPTIDASE | TAFI | PURIFICATION | COAGULATION | SUBUNITS | ANAPHYLATOXIN | IMMUNOLOGY | Liver - enzymology | Humans | Lipopolysaccharides - administration & dosage | Enzyme Precursors - genetics | Molecular Sequence Data | Male | Acute-Phase Proteins - genetics | Organ Specificity - genetics | RNA, Messenger - biosynthesis | Lysine Carboxypeptidase - genetics | Carboxypeptidases - blood | Base Sequence | Cloning, Molecular | Carboxypeptidase B2 | Lysine Carboxypeptidase - biosynthesis | Amino Acid Sequence | Acute-Phase Proteins - metabolism | Gene Expression Regulation - immunology | Enzyme Precursors - biosynthesis | Injections, Intraperitoneal | Carboxypeptidases - genetics | DNA, Complementary - isolation & purification | Enzyme Precursors - metabolism | Animals | Lysine Carboxypeptidase - metabolism | Carboxypeptidases - biosynthesis | Carboxypeptidases - metabolism | Mice | Mice, Inbred BALB C | Kinetics | Acute-Phase Proteins - biosynthesis
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9. Full Text Plasma carboxypeptidases as regulators of the plasminogen system
by Redlitz, Alexander and Tan, Anthony K and Eaton, Dan L and Plow, Edward F
Journal of Clinical Investigation, ISSN 0021-9738, 1995, Volume 96, Issue 5, pp. 2534 - 2538
Carboxy-terminal lysine residues on the surface of cells and fibrin bind plasminogen and control its activation. Since plasma contains basic carboxypeptidases,... 
fibrinolysis | thrombolysis | plasminogen activation | plasminogen receptors | MEDICINE, RESEARCH & EXPERIMENTAL | CELLS | RECEPTOR | PLASMINOGEN ACTIVATION | FIBRINOLYSIS | ACTIVATOR | LYSINES | THROMBOLYSIS | BINDING | FIBRINOGEN | PLASMINOGEN RECEPTORS | UROKINASE | SURFACES
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10. Full Text Aminopeptidase P in individuals with a history of angio-oedema on ACE inhibitors
by Adam, Albert and Cugno, Massimo and Molinaro, Giuseppe and Perez, Melissa and Lepage, Yves and Agostoni, Angelo
The Lancet, ISSN 0140-6736, 06/2002, Volume 359, Issue 9323, pp. 2088 - 2089
Angio-oedema is a rare but potentially life threatening side-effect of angiotensin-converting-enzyme (ACE) inhibitor treatment. Identification of individuals... 
CONVERTING ENZYME-INHIBITOR | MEDICINE, GENERAL & INTERNAL | PLASMA | BRADYKININ | Humans | Middle Aged | Aminopeptidases - blood | Hypertension - drug therapy | Case-Control Studies | Angioedema - enzymology | Analysis of Variance | Angioedema - blood | Angiotensin-Converting Enzyme Inhibitors - adverse effects | Adult | Angioedema - chemically induced | Aged | Lysine Carboxypeptidase - blood | Adverse and side effects | Angioneurotic edema | ACE inhibitors | Risk factors | Hypertension | Enzymes | Plasma | Side effects | Pharmacology | Drug therapy | Edema | Medical research | Patients | Inhibitors | Peptidyl-dipeptidase A | Bradykinin | Angiotensin | Lysine carboxypeptidase | Aminopeptidase
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11. Full Text Inactivation of bradykinin by angiotensin-converting enzyme and by carboxypeptidase N in human plasma
by Antti Kuoppala and Ken A. Lindstedt and Juhani Saarinen and Petri T. Kovanen and Jorma O. Kokkonen
American Journal of Physiology - Heart and Circulatory Physiology, ISSN 0363-6135, 04/2000, Volume 278, Issue 4, pp. 1069 - 1074
Because bradykinin (BK) appears to have cardioprotective effects ranging from improved hemodynamics to antiproliferative effects, inhibition of BK-degrading... 
Kininase I | Peptides | Kininase II | MYOCARDIUM | CARDIAC & CARDIOVASCULAR SYSTEMS | PHYSIOLOGY | RAT | peptides | KININASE-II | kininase II | HEART | RESPONSES | kininase I | DEGRADATION | PERIPHERAL VASCULAR DISEASE | INHIBITORS | RECEPTORS | BLOOD | Amino Acid Sequence | 3-Mercaptopropionic Acid - analogs & derivatives | Captopril - pharmacology | Bradykinin - chemistry | Humans | Middle Aged | Male | Tritium | Bradykinin - antagonists & inhibitors | Enzyme Activation - drug effects | Blood Proteins - pharmacology | 3-Mercaptopropionic Acid - pharmacology | Protease Inhibitors - pharmacology | Peptidyl-Dipeptidase A - blood | Adult | Female | Angiotensin-Converting Enzyme Inhibitors - pharmacology | Bradykinin - blood | Lysine Carboxypeptidase - blood
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12. Full Text Development of a sensitive and selective assay for the determination of procarboxypeptidase U (thrombin-activatable fibrinolysis inhibitor) in plasma
by Heylen, Evelien and Van Goethem, Sebastiaan and Willemse, Johan and Olsson, Thomas and Augustyns, Koen and Hendriks, Dirk
Analytical Biochemistry, ISSN 0003-2697, 2010, Volume 396, Issue 1, pp. 152 - 154
To date, several assays for procarboxypeptidase U (proCPU) determination exist, all having their own inherent disadvantages and advantages. A drawback of... 
CHEMISTRY, ANALYTICAL | ISCHEMIC-STROKE PATIENTS | THRESHOLD | CARBOXYPEPTIDASE-N | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | RISK | THROMBOLYTIC THERAPY | TAFIA | Reference Standards | Humans | Carboxypeptidase B2 - blood | Enzyme Assays - methods | Substrate Specificity | Calibration | Chromatography, High Pressure Liquid | Lysine Carboxypeptidase - blood | Peptides | Liquid chromatography
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13. Full Text Effects of human soluble thrombomodulin on experimental glomerulonephritis
by Ikeguchi, Hiroshi and Maruyama, Shoichi and Morita, Yoshiki and Fujita, Yutaka and Kato, Tomomi and Natori, Yasuhiro and Akatsu, Hiroyasu and Campbell, William and Okada, Hidechika and Okada, Noriko and Yuzawa, Yukio and Matsuo, Seiichi
Kidney International, ISSN 0085-2538, 02/2002, Volume 61, Issue 2, pp. 490 - 501
Effects of human soluble thrombomodulin on experimental glomerulonephritis. Coagulation and inflammation are both important processes that contribute to... 
kidney | thrombin | glomerular injury | inflammation | anticoagulant | anaphylatoxin | carboxypeptidase | Glomerular injury | Thrombin | Anticoagulant | Carboxypeptidase | Inflammation | Anaphylatoxin | Kidney | CRESCENTIC GLOMERULONEPHRITIS | THROMBIN-CATALYZED ACTIVATION | RHS-TM | PLASMA PROCARBOXYPEPTIDASE-B | GLOMERULAR THROMBOSIS | PULMONARY VASCULAR INJURY | NEPHROTOXIC SERUM | PROTEIN-C ACTIVATION | CARBOXYPEPTIDASE-N | DISSEMINATED INTRAVASCULAR COAGULATION | UROLOGY & NEPHROLOGY | Thrombosis - chemically induced | Rats, Wistar | Thrombosis - complications | Blood Urea Nitrogen | Humans | Prothrombin Time | Carboxypeptidase B2 - blood | Complement C5a - metabolism | Blood Coagulation | Kidney Glomerulus - metabolism | Female | Leukocyte Count | Glomerulonephritis - etiology | Disease Models, Animal | Lysine Carboxypeptidase - blood | Rabbits | Thrombomodulin - administration & dosage | Solubility | Rats | Kidney Glomerulus - pathology | Glomerulonephritis - drug therapy | Thrombosis - pathology | Animals | Platelet Count | Partial Thromboplastin Time | Anaphylatoxins - metabolism | Glomerulonephritis - pathology | Creatinine - blood | Thrombin - metabolism | Fibrin - metabolism
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14. Full Text A rapid and sensitive assay for the quantitation of carboxypeptidase N, an important regulator of inflammation
by Willemse, Johan L and Hendriks, Dirk F
Clinica Chimica Acta, ISSN 0009-8981, 2006, Volume 371, Issue 1, pp. 124 - 129
Carboxypeptidase N is a plasma zinc metallocarboxypeptidase which is constitutively expressed in the liver and was identified as the enzyme responsible for... 
Carboxypeptidase N | Inflammation | Anaphylatoxin inactivator | Kinetic assay | THERMAL-STABILITY | carboxypeptidase N | HUMAN PLASMA | SERUM | PROCARBOXYPEPTIDASE-U TAFI | DEFICIENCY | RESPECT | ENZYME | anaphylatoxin inactivator | inflammation | FIBRINOLYSIS INHIBITOR TAFI | MEDICAL LABORATORY TECHNOLOGY | kinetic assay | Inflammation - pathology | Reproducibility of Results | Anaphylatoxins - antagonists & inhibitors | Humans | Middle Aged | Chromatography, High Pressure Liquid | Inflammation - blood | Anaphylatoxins - metabolism | Sensitivity and Specificity | Adolescent | Adult | Biological Assay | Aged | Dipeptides - metabolism | Kinetics | Lysine Carboxypeptidase - blood | Enzymes | Bradykinin | Immunoproteins
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15. Full Text [40] Human carboxypeptidase N: Lysine carboxypeptidase
by Skidgel, Randal A
1995, ISBN 9780121821494, Volume 248, Issue C
Amino Acid Sequence | Lysine Carboxypeptidase - chemistry | Lysine Carboxypeptidase - isolation & purification | Humans | Lysine Carboxypeptidase - blood
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16. Full Text Assay of Procarboxypeptidase U, a Novel Determinant of the Fibrinolytic Cascade, in Human Plasma
by Schatteman, Katinka A and Goossens, Filip J and Scharpe, Simon S and Neels, Hugo M and Hendriks, Dirk F
Clinical Chemistry, ISSN 0009-9147, 06/1999, Volume 45, Issue 6, pp. 807 - 813
Background: Procarboxypeptidase U (proCPU) is a novel proenzyme found in human plasma. The active form, carboxypeptidase U (CPU; EC 3.4.17.20), retards the... 
HUMAN-SERUM | CARBOXYPEPTIDASE-N | THROMBIN | ARGININE CARBOXYPEPTIDASE | IN-VIVO | PURIFICATION | TAFI | COAGULATION | CLOT LYSIS | MEDICAL LABORATORY TECHNOLOGY | PLASMINOGEN | Reproducibility of Results | Humans | Middle Aged | Male | Reference Values | Thrombin | Chromatography, High Pressure Liquid | Fibrinolysis | Carboxypeptidases - blood | Sensitivity and Specificity | Carboxypeptidase B2 | Adult | Female | Aged | Enzyme Activation | Thrombomodulin | Enzymes | Fibrin | Lysine
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17. Basic carboxypeptidases of blood: significance for coagulology
by Timofeev, А V
Biomeditsinskaia khimiia, ISSN 2310-6972, 03/2016, Volume 62, Issue 2, p. 141
This review considers the basic metallocarboxypeptidases of human blood and their role in coagulologic disorders. In includes information on the history of the... 
Blood Coagulation Disorders - enzymology | Lysine Carboxypeptidase - chemistry | Carboxypeptidases - blood | Humans | Lysine Carboxypeptidase - metabolism | Carboxypeptidases - metabolism | Blood Coagulation Disorders - diagnosis | Blood Coagulation - physiology | Fibrinolysis - physiology | Fibrin - metabolism | Carboxypeptidase B2 - chemistry | Carboxypeptidase B2 - metabolism
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18. Full Text An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits
by Campbell, William and Okada, Hidechika
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 1989, Volume 162, Issue 3, pp. 933 - 939
An unstable carboxypeptidase N or B like enzyme is generated as a result of coagulation. This enzyme is derived from some plasma component (s) and not from... 
BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOPHYSICS | Arginine | Carboxypeptidases - blood | Enzyme-Linked Immunosorbent Assay | Lysine | Humans | Blood Coagulation | Substrate Specificity | Inflammation - enzymology | Chromatography | Lysine Carboxypeptidase - blood
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19. Thrombin-activatable fibrinolysis inhibitor
by Marx, Pauline F
Current Medicinal Chemistry, ISSN 0929-8673, 09/2004, Volume 11, Issue 17, pp. 2335 - 2348
The coagulation system is a potent mechanism that prevents blood loss after vascular injury. It consists of a number of linked enzymatic reactions resulting in... 
CPB | CPR | Coagulation | TAFI | CPU | Carboxypeptidase | Fibrinolysis | CHEMISTRY, MEDICINAL | PLASMA PROCARBOXYPEPTIDASE-B | BIOCHEMISTRY & MOLECULAR BIOLOGY | JUGULAR-VEIN THROMBOLYSIS | PROTEIN-C | coagulation | carboxypeptidase | fibrinolysis | 3-DIMENSIONAL STRUCTURE | TAFI ANTIGEN LEVELS | TYPE-2 DIABETIC-PATIENTS | TISSUE-PLASMINOGEN-ACTIVATOR | FACTOR-XI | CARBOXYPEPTIDASE-B | PHARMACOLOGY & PHARMACY | CLOT LYSIS | Humans | Carboxypeptidase B2 - blood | Hemorrhagic Disorders - blood | Thrombomodulin - chemistry | Thrombomodulin - metabolism | Animals | Carboxypeptidase B2 - physiology | Thrombin - chemistry | Fibrinogen - metabolism | Blood Coagulation Disorders - blood | Fibrinolysis - physiology | Thrombin - metabolism | Lysine - chemistry | Fibrinolysin - metabolism
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