Carboxypeptidase N: a pleiotropic regulator of inflammation

KW Matthews, SL Mueller-Ortiz, RA Wetsel - Molecular immunology, 2004 - Elsevier
Carboxypeptidase N (CPN) is a plasma zinc metalloprotease, which consists of two
enzymatically active small subunits (CPN1) and two large subunits (CPN2) that protect the …

The kinin–kallikrein system: physiological roles, pathophysiology and its relationship to cancer biomarkers

E Kashuba, J Bailey, D Allsup, L Cawkwell - Biomarkers, 2013 - Taylor & Francis
The kinin–kallikrein system (KKS) is an endogenous multiprotein cascade, the activation of
which leads to triggering of the intrinsic coagulation pathway and enzymatic hydrolysis of …

Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1α in the circulation

DA Davis, KE Singer, M De La Luz Sierra, M Narazaki… - Blood, 2005 - ashpublications.org
The chemokine stromal-derived factor-1α (SDF-1α) is an essential regulator of
hematopoiesis, lymphocyte homing, pre-B-cell growth, and angiogenesis. As SDF-1α is …

Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator

RA Skidgel, EG Erdös - International immunopharmacology, 2007 - Elsevier
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 “anaphylatoxin …

Targeted disruption of the gene encoding the murine small subunit of carboxypeptidase N (CPN1) causes susceptibility to C5a anaphylatoxin-mediated shock

SL Mueller-Ortiz, D Wang, JE Morales, L Li… - The Journal of …, 2009 - journals.aai.org
Carboxypeptidase N (CPN) is a plasma zinc metalloprotease, which consists of two
enzymatically active small subunits (CPN1) and two large subunits (CPN2) that protect the …

Whole-genome sequencing study of serum peptide levels: the Atherosclerosis Risk in Communities study

PS de Vries, B Yu, EV Feofanova… - Human molecular …, 2017 - academic.oup.com
Oligopeptides are important markers of protein metabolism, as they are cleaved from larger
polypeptides and proteins. Genetic association studies may help elucidate their origin and …

Two carboxypeptidase counterparts from rock bream (Oplegnathus fasciatus): molecular characterization, genomic arrangement and immune responses upon …

GI Godahewa, WDN Wickramaarachchi… - Veterinary Immunology …, 2014 - Elsevier
Carboxypeptidases (CPs) are proteases that hydrolyze C-terminal peptide bonds. They are
involved in regulating the complement system of the immune system. Here, we report the …

Structural characterization of the human carboxypeptidase D gene and its promoter

B Timblin, M Rehli, RA Skidgel - International immunopharmacology, 2002 - Elsevier
Human carboxypeptidase D (CPD) is a 180-kDa type I membrane protein with three tandem
active site domains. CPD is a B-type (or kininase I-type) carboxypeptidase that cleaves C …

Structure of the human carboxypeptidase M gene. Identification of a proximal GC-rich promoter and a unique distal promoter that consists of repetitive elements

J Li, M Rehli, B Timblin, F Tan, SW Krause, RA Skidgel - Gene, 2002 - Elsevier
The human carboxypeptidase M (CPM) gene was found to encompass∼ 112.6 kb of
genomic sequence, containing 11 exons of which eight (exons 2–9) are common to all …

Expression of the third complement component (C3) and carboxypeptidase N small subunit (CPN1) during mouse embryonic development

KW Matthews, SM Drouin, C Liu, JF Martin… - Developmental & …, 2004 - Elsevier
Complement regulatory proteins prevent excessive complement system activation and
deposition, which can lead to host tissue damage, including fetal loss during pregnancy. To …