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Enzymatic Degradation of Bradykinin
Published in Sami I. Said, Proinflammatory and Antiinflammatory Peptides, 2020
Randal A. Skidgel, Ervin G. Erdös
The potential physiological and pathophysiological functions of carboxypeptidase M are many. For example, carboxypeptidase M could be involved in inflammatory and pathological processes by regulating the activity of kinins and anaphylatoxins that mediate many responses to inflammation. In the kidney, carboxypeptidase M may control the activity of kinins which are released by kallikrein liberated from the distal tubules (Scicli et al., 1978). In one study, hypertensive patients excreted significantly more kininases than normal individuals, and the major kininase was a kininase I-type enzyme (Iimura et al., 1987). (As a basic carboxypeptidase, it was probably carboxypeptidase M.) Thus, increased release of carboxypeptidase M into the urine could be an early sign of renal damage due to hypertension or other diseases.
Revision of potential prognostic markers of cholangiocarcinoma for clinical practice
Published in Expert Review of Anticancer Therapy, 2023
Charupong Saengboonmee, Sumalee Obchoei, Kanlayanee Sawanyawisuth, Sopit Wongkham
A study in bile samples found that squamous cell carcinoma antigen 1 (SCCA1) protein can be detected in bile by specific antibodies but rarely detected in the serum. Patients with positive SCCA1 were tended to have portal invasion and recurrence tumors. Possibly due to the limited number of samples, the results from this study were not statistically significant [68]. In a case-control and single-center study, bile samples from patients with benign biliary conditions (n = 36) and CCA (n = 36) were used for metabolomic and proteomic analyses [103]. These omics data with the aid of a machine-learning pipeline, the authors could identify biomarkers with predictive capacity. A panel of five proteins, namely, lactotransferrin (LTF), 5′-nucleotidase (NT5E), carboxypeptidase M (CPM), alpha-2-macroglobulin (A2M), and alpha-4-actinin (ACTN4), could distinguish between benign cholangiopathy and CCA with 100% sensitivity and specificity and AUC of 1. In addition, a combination of 10 lipid species, including seven phosphatidylcholines (PCs), two ceramides (Cers), and total triacylglycerols (TG), performed a similar task as does a protein panel, with an AUC of 0.98, 94.1% sensitivity and 92.3% specificity [103]. However, the prognostic capacity of these biomarkers was not discussed. The study of metabolites in urine samples reported some potential biomarkers for CCA diagnosis and for the differential diagnosis with hepatocellular carcinoma. However, the changes in urine metabolites and prognosis of CCA are underway investigation and have not been well established [104,105].
Recent advances in proteolytic stability for peptide, protein, and antibody drug discovery
Published in Expert Opinion on Drug Discovery, 2021
Xianyin Lai, Jason Tang, Mohamed E.H. ElSayed
Carboxypeptidases (EC 3.4.16–3.4.18) are peptidases that cleave a peptide bond at the carboxy-terminal (C-terminal) end of a peptide or protein. Carboxypeptidases are named with a combination of one letter and one number following the word carboxypeptidase at the beginning. There are at least 17 carboxypeptidases, belonging to two major groups. One uses serine as an active site residue named as serine carboxypeptidases, and the other uses zinc at the active site, known as metallocarboxypeptidases, which are further separated into two subgroups based on amino acid sequence similarities [66]. Among the carboxypeptidases, some of them have low tissue specificity with expression in many tissues and are secreted into bodily fluids with a low concentration, such as carboxypeptidases D and X2. Some are in specific tissues without leaking into bodily fluids or with a low concentration in bodily fluids, such as carboxypeptidase A4 in the esophagus and skin, carboxypeptidase A6 in the intestine, prostate, and retina, carboxypeptidase E in the brain, carboxypeptidase M in the adipose, carboxypeptidase O in the intestine, X1 in the placenta, and carboxypeptidase Z in the ovary. And others are produced in specific tissues and then secreted into either small intestinal fluid or blood. Carboxypeptidases A1, A2, and B1 are produced in the pancreas and activated in the duodenum. All three proteins are zinc-containing metallopeptidases [67]. Compared to the high abundance of trypsin, chymotrypsin and elastase in the small intestine, carboxypeptidases such as A1, A2, and B1, have a much lower concentration.
Is individual genetic susceptibility a link between silica exposure and development or severity of silicosis? A systematic review
Published in Inhalation Toxicology, 2020
Kaio Cezar Rodrigues Salum, Marcos Cesar Santos Castro, Ângela Santos Ferreira Nani, Fabiana Barzotto Kohlrausch
Carboxypeptidase M (CPM) belongs to the family of the carboxypeptidases, which function is removing C-terminal amino acids from peptides and proteins and exert roles in physiological processes like inflammation. CPM has been suggested to play critical roles in inflammatory diseases (Deiteren et al. 2009), and a higher expression level of CPM may promote the progression of lung fibrosis (Chu et al. 2019). In fact, the relative expression of the CPM gene was significantly higher in subjects with silicosis compared with healthy controls (Chu et al. 2019). Based on the hypothesis that the rs12812500 polymorphism is located on the promoter of the CPM gene and was associated with higher CPM expression, Chu et al. (2019) evaluated this polymorphism and observed the G allele was associated with an increased risk of silicosis in an additive genetic model controlled for confounders.