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Enzymatic Degradation of Bradykinin
Published in Sami I. Said, Proinflammatory and Antiinflammatory Peptides, 2020
Randal A. Skidgel, Ervin G. Erdös
At present, other potential functions of carboxypeptidase D are still unknown, but hypothetically it could be involved in peptide and protein processing in the constitutive secretory pathway, analogous to the participation of carboxypeptidase E in prohormone processing in the regulated secretory pathway. Whether mammalian carboxypeptidase D can also act as a hepatitis B virus-binding protein is unknown, but this might be a fruitful area for further investigation.
Noninsulin-Dependent Animal Models of Diabetes Mellitus
Published in John H. McNeill, Experimental Models of Diabetes, 2018
Christopher H. S. McIntosh, Raymond A. Pederson
Examples of the use of transgenic animals in studying the physiology of leptin and the agouti protein have been discussed earlier. Identification of the genes involved in the rare, probably monogenic, obesity syndromes, such as Prader–Willi, Bardet–Biedl, Alström, and Cohen, is likely to provide interesting information regarding specific pathways involved in body weight control, and the introduction of equivalent mutations into animals should provide important information regarding their function. Apart from leptin, carboxypeptidase E, and agouti plus ART, a plethora of candidate obesity genes have been identified. For example, DNA polymorphism studies have provided evidence for linkage with uncoupling proteins, the β3-adrenergic receptor, and TNF.406 Evidence supporting or refuting a role for some of these genes has come from transgenic mouse models.
PEPTIDES
Published in Stephen W. Carmichael, Susan L. Stoddard, The Adrenal Medulla 1986 - 1988, 2017
Stephen W. Carmichael, Susan L. Stoddard
Fricker, Evans, Esch et al. (1986) cloned and determined the sequence of cDNA for bovine carboxypeptidase E. This peptidase, formerly called enkephalin convertase, was first identified in bovine adrenal chromaffin vesicles. The predicted amino acid sequence of the cDNA clone contains the partially determined sequences of carboxypeptidase E and several pairs of basic amino acids and displays some homology with carboxypeptidases A and B. Restriction analysis suggests that there is only one gene for carboxypeptidase E. This is consistent with a broad role for the enzyme in the biosynthesis of many neuropeptides.
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.
Exploring neuropeptide signalling through proteomics and peptidomics
Published in Expert Review of Proteomics, 2019
Samantha Louise Edwards, Lucas Mergan, Bhavesh Parmar, Bram Cockx, Wouter De Haes, Liesbet Temmerman, Liliane Schoofs
One of the earliest applications of proteomics in the context of neuropeptides was to study the first steps of neuropeptide signaling: neuropeptide synthesis and processing. In a first study, dense core vesicles (DCV) from bovine chromaffin cells were lysed, soluble and membrane fractions were subjected to one-dimensional SDS-PAGE, and tryptic digests of gel slices were analyzed by LC-MS/MS. Proteins were identified from a variety of categories, including propeptides, proteases, and their regulators. As well as known components of these processing pathways, such as prohormone convertases 1 (PC1/3) and 2 (PC2) and carboxypeptidase E (CPE), novel elements were also discovered, such as cathepsins B and D, which at the time were known primarily as lysosomal proteins [44,45]. A similar approach was later used upon DCV of human pheochromocytoma, a tumor of the adrenal medulla. Normalized spectral abundance factor analysis was applied for relative quantification of over 300 of the identified proteins. PC1/3, PC2 and CPE were the most abundant propeptide-cleaving proteases, and their regulators proSAAS and 7B2 were also present [46,47]. Studies such as these contribute to a more complete picture of neuropeptide production in DCV, the primary stage of neuropeptide signaling.