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1. Full Text Functional variant of the carboxypeptidase M (CPM) gene may affect silica-related pneumoconiosis susceptibility by its expression: a multistage case–control study
by Chu, Minjie and Wu, Shuangshuang and Wang, Wei and Yu, Yuhui and Zhang, Mingjiong and Sang, Lingli and Tian, Tian and Lu, Yihua and Yuan, Weiwei and Huang, Qiqing and Yi, Min and Gao, Yuexia and Xiao, Jing and Lian, Yulong and Zhuang, Xun and Zhang, Zuo-Feng and Wu, Jianqing
Occupational and Environmental Medicine, ISSN 1351-0711, 03/2019, Volume 76, Issue 3, pp. 169 - 174
ObjectivesIn a genome-wide association study, we discovered chromosome 12q15 (defined as rs73329476) as a silica-related pneumoconiosis susceptibility region.... 
silicosis | cpm | expression | FIBROSIS | PUBLIC, ENVIRONMENTAL & OCCUPATIONAL HEALTH | ASSOCIATION | INFLAMMATION | DELETION | Health care | Genes | Occupational diseases | Genomes | mRNA | Single-nucleotide polymorphism | Leukocytes | Gene polymorphism | Silica | Blood | Silicon dioxide | Reporter gene | Peripheral blood | Chromosome 12 | Dust control | Silicosis | Public health | Carboxypeptidase M | Pneumoconiosis | Inflammation | Exposure | Gene expression | Dust | X rays | Workers | Polyadenylation | Alleles | Silicas | Health risk assessment | Polymorphism | Geriatrics | Workplace | 1506
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2. Full Text Interactions between carboxypeptidase M and kinin B1 receptor in endothelial cells
by Guimarães, Paola Bianchi and da Silva, Rafael Filippelli and Hoff, Carolina Caldas and Fernandes, Liliam and Nakaie, Clovis Ryuichi and Chagas, Jair Ribeiro and Carmona, Adriana Karaoglanovic and Bader, Michael and Pesquero, João Bosco
Inflammation Research, ISSN 1023-3830, 10/2019, Volume 68, Issue 10, pp. 845 - 855
Carboxypeptidase M (CPM) is a glycosylphosphatidylinositol anchored enzyme that plays an important role in the kallikrein–kinin system (KKS). CPM catalytic... 
Allergology | Neurology | Carboxypeptidase M | Biomedicine | Immunology | Enzymatic activity | Dermatology | Rheumatology | B 1 receptor | Kinins | Pharmacology/Toxicology | Microdomains | receptor | MEMBRANE-BOUND CARBOXYPEPTIDASE | SIGNAL | ACTIVATION | ACE | MECHANISMS | IMMUNOLOGY | CELL BIOLOGY | PHARMACOLOGY | BRADYKININ B-2 RECEPTORS | PROTEINS | B-1 receptor | EXPRESSION | Enzymes | Evaluation | Bradykinin | Physiological aspects | Kallikrein | Genetic engineering | Endothelium | Cell culture | Enzyme activity | Peptides | Incubation | Transgenic mice | mRNA | Endothelial cells | Signaling | Receptors | Transfection | Carboxypeptidase A | Mice | Glycosylphosphatidylinositol | Microvasculature | Catalysis | Culture
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3. Full Text Carboxypeptidase M Expressed by Human Bone Marrow Cells Cleaves the C‐Terminal Lysine of Stromal Cell‐Derived Factor‐1α: Another Player in Hematopoietic Stem/Progenitor Cell Mobilization?
by Marquez‐Curtis, Leah and Jalili, Ali and Deiteren, Kathleen and Shirvaikar, Neeta and Lambeir, Anne‐Marie and Janowska‐Wieczorek, Anna
STEM CELLS, ISSN 1066-5099, 05/2008, Volume 26, Issue 5, pp. 1211 - 1220
Carboxypeptidase M (CPM) is a membrane‐bound zinc‐dependent protease that cleaves C‐terminal basic residues, such as arginine or lysine, from... 
Bone marrow | Carboxypeptidase M | Mobilization | CXCR4 | Stromal cell‐derived factor‐1 | Granulocyte‐colony‐stimulating factor | Stromal cell-derived factor-1 | Granulocyte-colony- stimulating factor | MEMBRANE-BOUND CARBOXYPEPTIDASE | PROGENITOR CELLS | carboxypeptidase M | mobilization | COLONY-STIMULATING FACTOR | SDF-1 | FACTOR-I | bone marrow | MESENCHYMAL STEM-CELLS | granulocyte-colony-stimulating factor | CELL BIOLOGY | CD34(+) CELLS | ONCOLOGY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | GROWTH-FACTORS | CXCR4 ACTIVATION | stromal cell-derived factor-1 | HEMATOLOGY | BINDING
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4. Full Text MicroRNA-146a promote cell migration and invasion in human colorectal cancer via carboxypeptidase M/src-FAK pathway
by Lu, Di and Yao, Qunyan and Zhan, Cheng and Le-meng, Zhang and Liu, Hongchun and Cai, Yu and Tu, Chuantao and Li, Xi and Zou, Yanting and Zhang, Shuncai
Oncotarget, ISSN 1949-2553, 2017, Volume 8, Issue 14, pp. 22674 - 22684
Colorectal cancer (CRC) is one of the most common cancers worldwide, and microRNAs play important roles in CRC progression. This study aimed to investigate the... 
Carboxypeptidase M | Migration | Invasion | Colorectal cancer | MiR-146a-5p | miR-146a-5p | BREAST-CANCER | carboxypeptidase M | colorectal cancer | invasion | DIRECTS | migration | TYROSINE KINASES | FOCAL ADHESION KINASE | C-SRC | CELL BIOLOGY | Metalloendopeptidases - genetics | Focal Adhesion Kinase 1 - genetics | Cell Proliferation | Prognosis | Colorectal Neoplasms - genetics | Humans | Gene Expression Regulation, Neoplastic | Metalloendopeptidases - metabolism | Neoplasm Recurrence, Local - pathology | src-Family Kinases - metabolism | Biomarkers, Tumor - metabolism | Tumor Cells, Cultured | Focal Adhesion Kinase 1 - metabolism | Colorectal Neoplasms - metabolism | Neoplasm Recurrence, Local - metabolism | Signal Transduction | Neoplasm Invasiveness | Survival Rate | GPI-Linked Proteins - metabolism | Neoplasm Recurrence, Local - genetics | Biomarkers, Tumor - genetics | MicroRNAs - genetics | Colorectal Neoplasms - pathology | Neoplasm Staging | src-Family Kinases - genetics | Apoptosis | Cell Movement | GPI-Linked Proteins - genetics
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5. Full Text Carboxypeptidase M: Multiple alliances and unknown partners
by Deiteren, Kathleen and Hendriks, Dirk and Scharpé, Simon and Lambeir, Anne Marie
Clinica Chimica Acta, ISSN 0009-8981, 2009, Volume 399, Issue 1, pp. 24 - 39
Carboxypeptidase M (EC 3.4.17.12) belongs to the family of the carboxypeptidases. These enzymes remove C-terminal amino acids from peptides and proteins and... 
Mesenchymal cells | Membrane protein | Carboxypeptidase | Inflammation | Peptides | Cancer | MEMBRANE-BOUND CARBOXYPEPTIDASE | PEPTIDE-HORMONE ACTIVITY | ACTIVATABLE FIBRINOLYSIS INHIBITOR | DIFFERENTIATED U937 CELLS | C-TERMINAL LYSINE | NITRIC-OXIDE PRODUCTION | METALLOCARBOXYPEPTIDASE GENE FAMILY | EPIDERMAL-GROWTH-FACTOR | MONOCYTE-DERIVED MACROPHAGES | MEDICAL LABORATORY TECHNOLOGY | NEUTRAL ENDOPEPTIDASE ENKEPHALINASE | Metalloendopeptidases - antagonists & inhibitors | Metalloendopeptidases - genetics | Amino Acid Sequence | Humans | GPI-Linked Proteins | Molecular Sequence Data | Protease Inhibitors - chemistry | Substrate Specificity | Metalloendopeptidases - metabolism | Cell Membrane - genetics | Cell Membrane - chemistry | Protease Inhibitors - pharmacology | Animals | Metalloendopeptidases - chemistry | Protein Binding | Cell Membrane - metabolism | Physiological aspects | Proteases | Stem cells
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6. Full Text Carboxypeptidase M in apoptosis, adipogenesis and cancer
by Denis, Catherine J and Deiteren, Kathleen and Hendriks, Dirk and Proost, Paul and Lambeir, Anne-Marie
Clinica Chimica Acta, ISSN 0009-8981, 01/2013, Volume 415, pp. 306 - 316
This review covers carboxypeptidase M (CPM) research that appeared in the literature since 2009. The focus is on aspects that are new or interesting from a... 
Chemokine | Adipocyte | Biomarker | Inflammation | Protease | Peptide | MEMBRANE-BOUND CARBOXYPEPTIDASE | GENE-EXPRESSION SIGNATURE | DIFFERENTIAL EXPRESSION | DEXAMETHASONE-INDUCED APOPTOSIS | MACROPHAGE MATURATION | GROWTH-FACTOR RECEPTOR | IN-VIVO | CHEMOKINE RECEPTOR | MESENCHYMAL-STEM-CELLS | MEDICAL LABORATORY TECHNOLOGY | CHROMOSOMAL-ABERRATIONS | Metalloendopeptidases - genetics | Proto-Oncogene Proteins c-mdm2 - genetics | Prognosis | Adenocarcinoma of Lung | Soft Tissue Neoplasms - diagnosis | Humans | Liposarcoma - blood supply | ErbB Receptors - genetics | Neovascularization, Pathologic | Liposarcoma - diagnosis | Substrate Specificity | Apoptosis - genetics | Metalloendopeptidases - metabolism | Biomarkers, Tumor - metabolism | Adenocarcinoma - genetics | Soft Tissue Neoplasms - enzymology | Adipogenesis - genetics | Proto-Oncogene Proteins c-mdm2 - metabolism | Soft Tissue Neoplasms - genetics | Lung Neoplasms - blood supply | Lung Neoplasms - genetics | Gene Expression | ErbB Receptors - metabolism | Lung Neoplasms - enzymology | Signal Transduction | Adenocarcinoma - enzymology | Liposarcoma - genetics | GPI-Linked Proteins - metabolism | Liposarcoma - enzymology | Adenocarcinoma - blood supply | Adenocarcinoma - diagnosis | Soft Tissue Neoplasms - blood supply | Biomarkers, Tumor - genetics | Lung Neoplasms - diagnosis | GPI-Linked Proteins - genetics | Peptides | Proteases | Cancer | Apoptosis
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7. Full Text Carboxypeptidase M is a positive allosteric modulator of the kinin B1 receptor
by Zhang, Xianming and Tan, Fulong and Skidgel, Randal A
Journal of Biological Chemistry, ISSN 0021-9258, 11/2013, Volume 288, Issue 46, pp. 33226 - 33240
Ligand binding to extracellular domains of G protein-coupled receptors can result in novel and nuanced allosteric effects on receptor signaling. We previously... 
Metalloendopeptidases - genetics | Protein Structure, Tertiary | MAP Kinase Signaling System - physiology | Mitogen-Activated Protein Kinase 3 - genetics | Protein Structure, Secondary | Humans | Metalloendopeptidases - metabolism | GPI-Linked Proteins - metabolism | Receptor, Bradykinin B1 - genetics | Allosteric Regulation - physiology | Mitogen-Activated Protein Kinase 3 - metabolism | Mitogen-Activated Protein Kinase 1 - genetics | HEK293 Cells | Receptor, Bradykinin B1 - metabolism | GPI-Linked Proteins - genetics | Mitogen-Activated Protein Kinase 1 - metabolism | Peptidases | G Protein-coupled Receptors (GPCR) | Peptide Hormones | Signal Transduction | Glycosyl Phosphatidylinositol Anchors | Kallidin | Allosteric Regulation | Bradykinin | Carboxypeptidase
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8. Full Text Genome-wide association study of migraine implicates a common susceptibility variant on 8q22.1
by Anttila, Verneri and Stefansson, Hreinn and Kallela, Mikko and Todt, Unda and Terwindt, Gisela M and Calafato, M Stella and Nyholt, Dale R and Dimas, Antigone S and Freilinger, Tobias and Müller-Myhsok, Bertram and Artto, Ville and Inouye, Michael and Alakurtti, Kirsi and Kaunisto, Mari A and Hämäläinen, Eija and De Vries, Boukje and Stam, Anine H and Weller, Claudia M and Heinze, Axel and Heinze-Kuhn, Katja and Goebel, Ingrid and Borck, Guntram and Göbel, Hartmut and Steinberg, Stacy and Wolf, Christiane and Björnsson, Asgeir and Gudmundsson, Gretar and Kirchmann, Malene and Hauge, Anne and Werge, Thomas and Schoenen, Jean and Eriksson, Johan G and Hagen, Knut and Stovner, Lars and Wichmann, H-Erich and Meitinger, Thomas and Alexander, Michael and Moebus, Susanne and Schreiber, Stefan and Aulchenko, Yurii S and Breteler, Monique M. B and Uitterlinden, Andre G and Hofman, Albert and Van Duijn, Cornelia M and Tikka-Kleemola, Päivi and Vepsäläinen, Salli and Lucae, Susanne and Tozzi, Federica and Muglia, Pierandrea and Barrett, Jeffrey and Kaprio, Jaakko and Färkkilä, Markus and Peltonen, Leena and Stefansson, Kari and Zwart, John-Anker and Ferrari, Michel D and Olesen, Jes and Daly, Mark and Wessman, Maija and Van Den Maagdenberg, Arn M.J.M and Dichgans, Martin and Kubisch, Christian and Dermitzakis, Emmanouil T and Frants, Rune R and Palotie, Aarno and Int Headache Genetics Consortium and International Headache Genetics Consortium and the International Headache Genetics Consortium
Nature Genetics, ISSN 1061-4036, 10/2010, Volume 42, Issue 10, pp. 869 - 873
Migraine is a common episodic neurological disorder, typically presenting with recurrent attacks of severe headache and autonomic dysfunction. Apart from rare... 
GLUTAMATE | MUTATION | INVOLVEMENT | GENETICS & HEREDITY | GENE-EXPRESSION | LYMPHOBLASTOID CELL-LINES | MECHANISMS | FAMILIAL HEMIPLEGIC MIGRAINE | EPISODIC ATAXIA | SPREADING DEPRESSION | CONFERS RISK | Lymphocytes - metabolism | Chromosomes, Human, Pair 8 - genetics | Cell Adhesion Molecules - genetics | Genetic Predisposition to Disease | Genome-Wide Association Study | Humans | Antigens, Surface - genetics | Cells, Cultured | Genotype | Male | Case-Control Studies | Microsatellite Repeats - genetics | Glutamate Carboxypeptidase II - genetics | Migraine Disorders - genetics | Female | Genome, Human | Quantitative Trait Loci | Calcium-Binding Proteins - genetics | Quantitative trait loci | Genetic aspects | Research | Genetic susceptibility | Migraine | Risk factors | Haplotypes | Medical research | Health sciences | Biomedical research | Education | Quality control | Mutation
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9. Full Text Loss of tubulin deglutamylase CCP1 causes infantile-onset neurodegeneration
by Shashi, V and Magiera, M.M and Klein, D and Zaki, M and Schoch, K and Rudnik-Schoneborn, S and Norman, A and Neto, O. Abath and Dusl, M and Yuan, X and Bartesaghi, L and Marco, P. De and Alfares, A.A and Marom, R and Arold, Stefan T and Guzman-Vega, F.J and Pena, L.D and Smith, E.C and Steinlin, M and Babiker, M.O and Mohassel, P and Foley, A.R and Donkervoort, S and Kaur, R and Ghosh, P.S and Stanley, V and Musaev, D and Nava, C and Mignot, C and Keren, B and Scala, M and Tassano, E and Picco, P and Doneda, P and Fiorillo, C and Issa, M.Y and Alassiri, A and Alahmad, A and Gerard, A and Liu, P and Yang, Y and Ertl-Wagner, B and Kranz, P.G and Wentzensen, I.M and Stucka, R and Stong, N and Allen, A.S and Goldstein, D.B and Schoser, B and Rosler, K.M and Alfadhel, M and Capra, V and Chrast, R and Strom, T.M and Kamsteeg, E.J and Bonnemann, C.G and Gleeson, J.G and Martini, R and Janke, C and Senderek, J and Undiagnosed Dis Network and Undiagnosed Diseases Network
EMBO Journal, ISSN 0261-4189, 2018, Volume 37, Issue 23, p. n/a
A set of glutamylases and deglutamylases controls levels of tubulin polyglutamylation, a prominent post-translational modification of neuronal microtubules.... 
tubulin polyglutamylation | neurodegeneration | cytosolic carboxypeptidase 1 (CCP1/AGTPBP1/NNA1) | motor neuron | cerebellum | CYTOSOLIC CARBOXYPEPTIDASE | VARIANTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE | DEGENERATION | CELL BIOLOGY | TRANSPORT | SERVER | DISEASE | NEURONS | MUTATIONS | PROTEINS | Cerebellum | Motor neurons | Translation | Enzyme activity | Neurodegenerative diseases | Neurons | Peripheral nerves | Motors | Neuropathy | Drug development | Atrophy | Tubulin | Enzymatic activity | Neurodegeneration | Microtubules | Nerves | Mice | Degeneration | Mutation | Neuroscience | AGTPBP1 | NNA1 | cytosolic carboxypeptidase 1 (CCP1 | Molecular Biology of Disease
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10. Full Text Cross-talk between carboxypeptidase M and the kinin B1 receptor mediates a new mode of G protein-coupled receptor signaling
by Zhang, Xianming and Tan, Fulong and Brovkovych, Viktor and Zhang, Yongkang and Skidgel, Randal A
Journal of Biological Chemistry, ISSN 0021-9258, 05/2011, Volume 286, Issue 21, pp. 18547 - 18561
G protein-coupled receptor (GPCR) signaling is affected by formation of GPCR homo-or heterodimers, but GPCR regulation by other cell surface proteins is not... 
MEMBRANE-BOUND CARBOXYPEPTIDASE | CONVERTING-ENZYME INHIBITORS |