Carboxypeptidase H
Carboxypeptidases
Chromaffin Granules
Carboxypeptidase B
Carboxypeptidases A
Lysine Carboxypeptidase
Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. (1/106)
Several recently discovered members of the carboxypeptidase E (CPE) gene family lack critical active site residues that are conserved in other family members. For example, three CPE-like proteins contain a Tyr in place of Glu300 (equivalent to Glu270 of carboxypeptidase A and B). To investigate the importance of this position, Glu300 of rat CPE was converted into Gln, Lys, or Tyr, and the proteins expressed in Sf9 cells using the baculovirus system. All three mutants were secreted from the cells, but the media showed no enzyme activity above background levels. Wild-type CPE and the Gln300 point mutant bound to a p-aminobenzoyl-Arg-Sepharose affinity resin, and this binding was competed by an active site-directed inhibitor, guanidinoethylmercaptosuccinic acid. The affinity purified mutant CPE protein showed no detectable enzyme activity (<0.004% of wild-type CPE) toward dansyl-Phe-Ala-Arg. Expression of the Gln300 and Lys300 mutant CPE proteins in the NIT3 mouse pancreatic beta-cell line showed that these mutants are routed into secretory vesicles and secreted via the regulated pathway. Taken together, these results indicate that Glu300 of CPE is essential for enzyme activity, but not required for substrate binding or for routing into the regulated secretory pathway. (+info)Biosynthesis and packaging of carboxypeptidase D into nascent secretory vesicles in pituitary cell lines. (2/106)
Metallocarboxypeptidase D (CPD) is a membrane-bound trans-Golgi network (TGN) protein. In AtT-20 cells, CPD is initially produced as a 170-kDa endoglycosidase H-sensitive glycoprotein. Within 30 min of chase, the CPD increases to 180 kDa and is resistant to endoglycosidase H as a result of carbohydrate maturation. CPD also undergoes an activation step required for binding to a substrate affinity resin. Blocking the protein exit from the endoplasmic reticulum inhibits the increase in molecular mass but not the step required for affinity column binding, suggesting that enzyme activation precedes carbohydrate maturation and that these reactions occur in distinct intracellular compartments. Only the higher molecular weight mature CPD enters nascent secretory vesicles, which bud from the TGN of permeabilized AtT-20 and GH3 cells. The budding efficiency of CPD into vesicles is 2-3-fold lower than that of endogenous proopiomelanocortin in AtT-20 cells or prolactin in GH3 cells. In contrast, the packaging of a truncated form of CPD, which lacks the cytoplasmic tail and transmembrane domain, was similar to that of proopiomelanocortin. Taken together, the results support the proposal that CPD functions in the TGN in the processing of proteins that transit the secretory pathway and that the C-terminal region plays a major role in TGN retention. (+info)Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing. (3/106)
Five novel peptides were identified in the brains of mice lacking active carboxypeptidase E, a neuropeptide-processing enzyme. These peptides are produced from a single precursor, termed proSAAS, which is present in human, mouse, and rat. ProSAAS mRNA is expressed primarily in brain and other neuroendocrine tissues (pituitary, adrenal, pancreas); within brain, the mRNA is broadly distributed among neurons. When expressed in AtT-20 cells, proSAAS is secreted via the regulated pathway and is also processed at paired-basic cleavage sites into smaller peptides. Overexpression of proSAAS in the AtT-20 cells substantially reduces the rate of processing of the endogenous prohormone proopiomelanocortin. Purified proSAAS inhibits prohormone convertase 1 activity with an IC(50) of 590 nM but does not inhibit prohormone convertase 2. Taken together, proSAAS may represent an endogenous inhibitor of prohormone convertase 1. (+info)Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor. (4/106)
Membrane carboxypeptidase E (CPE) is a sorting receptor for targeting prohormones, such as pro-opiomelanocortin, to the regulated secretory pathway in endocrine cells. Its membrane association is necessary for it to bind a prohormone sorting signal at the trans-Golgi network (TGN) to facilitate targeting. In this study, we examined the lipid interaction of CPE in bovine pituitary secretory granule membranes, which are derived from the TGN. We show that CPE is associated with detergent-resistant lipid domains, or rafts, within secretory granule membranes. Lipid analysis revealed that these rafts are enriched in glycosphingolipids and cholesterol. Pulse-chase and subcellular fractionation experiments in AtT-20 cells show that the association of CPE with membrane rafts occurred only after it reached the Golgi. Cholesterol depletion resulted in dissociation of CPE from secretory granule membranes and decreased the binding of prohormones to membranes. In vivo cholesterol depletion using lovastatin resulted in the lack of sorting of CPE and its cargo to the regulated secretory pathway. We propose that the sorting receptor function of CPE necessitates its interaction with glycosphingolipid-cholesterol rafts at the TGN, thereby anchoring it in position to bind to its prohormone cargo. (+info)Oligomerization of pro-opiomelanocortin is independent of pH, calcium and the sorting signal for the regulated secretory pathway. (5/106)
Studies indicate that pro-opiomelanocortin (POMC) is sorted to the regulated secretory pathway by binding to a sorting receptor identified as membrane-bound carboxypeptidase E (CPE) [Cool et al. (1997) Cell 88, 73-83]. The efficiency of this sorting mechanism could be enhanced if POMC molecules were to self-associate to form oligomers, prior or subsequent to binding to CPE. Using cross-linking and gel filtration techniques, we demonstrated that POMC forms oligomers at both neutral and acidic pHs and calcium was not necessary. delta N-POMC, which lacks the N-terminal sorting signal for the regulated secretory pathway, also formed similar oligomers, indicating that the sorting and oligomerization domains are different. (+info)Impaired prohormone convertases in Cpe(fat)/Cpe(fat) mice. (6/106)
A spontaneous point mutation in the coding region of the carboxypeptidase E (CPE) gene results in a loss of CPE activity that correlates with the development of late onset obesity (Nagert, J. K., Fricker, L. D., Varlamov, O., Nishina, P. M., Rouille, Y., Steiner, D. F., Carroll, R. J., Paigen, B. J., and Leiter, E. H. (1995) Nat. Genet. 10, 135-142). Examination of the level of neuropeptides in these mice showed a decrease in mature bioactive peptides as a result of a decrease in both carboxypeptidase and prohormone convertase activities. A defect in CPE is not expected to affect endoproteolytic processing. In this report we have addressed the mechanism of this unexpected finding by directly examining the expression of the major precursor processing endoproteases, prohormone convertases PC1 and PC2 in Cpe(fat) mice. We found that the levels of PC1 and PC2 are differentially altered in a number of brain regions and in the pituitary. Since these enzymes have been implicated in the generation of neuroendocrine peptides (dynorphin A-17, beta-endorphin, and alpha- melanocyte-stimulating hormone) involved in the control of feeding behavior and body weight, we compared the levels of these peptides in Cpe(fat) and wild type animals. We found a marked increase in the level of dynorphin A-17, a decrease in the level of alpha-melanocyte-stimulating hormone, and an alteration in the level of C-terminally processed beta-endorphin. These results suggest that the impairment in the level of these and other peptides involved in body weight regulation is mainly due to an alteration in carboxypeptidase and prohormone convertase activities and that this may lead to the development of obesity in these animals. (+info)ProSAAS processing in mouse brain and pituitary. (7/106)
ProSAAS is a newly discovered protein with a neuroendocrine distribution generally similar to that of prohormone convertase 1 (PC1), a peptide-processing endopeptidase. Several proSAAS-derived peptides were previously identified in the brain and pituitary of the Cpe(fat)/Cpe(fat) mouse based on the accumulation of C-terminally extended peptides due to the absence of enzymatically active carboxypeptidase E, a peptide-processing exopeptidase. In the present study, antisera against different regions of proSAAS were used to develop radioimmunoassays and examine the processing profile of proSAAS in wild type and Cpe(fat)/Cpe(fat) mouse tissues following gel filtration and reverse phase high performance liquid chromatography. In wild type mouse brain and pituitary, the majority of proSAAS is processed into smaller peptides. These proSAAS-derived peptides elute from the reverse-phase column in the same positions as synthetic peptides that correspond to little SAAS, PEN, and big LEN. Mass spectrometry revealed the presence of peptides with the expected molecular masses of little SAAS and big LEN in the fractions containing immunoreactive peptides. The processing of proSAAS is slightly impaired in Cpe(fat)/Cpe(fat) mice, relative to wild-type mice, leading to the accumulation of partially processed peptides. One of these peptides, the C-terminally extended form of PEN, is known to inhibit PC1 activity and this could account for the reduction in enzymatically active PC1 seen in Cpe(fat)/Cpe(fat) mice. The observation that little SAAS and big LEN are the major forms of these peptides produced in mouse brain and pituitary raises the possibility that these peptides function as neurotransmitters or hormones. (+info)Cholesterol, a cell size-dependent signal that regulates glucose metabolism and gene expression in adipocytes. (8/106)
Enlarged fat cells exhibit modified metabolic capacities, which could be involved in the metabolic complications of obesity at the whole body level. We show here that sterol regulatory element-binding protein 2 (SREBP-2) and its target genes are induced in the adipose tissue of several models of rodent obesity, suggesting cholesterol imbalance in enlarged adipocytes. Within a particular fat pad, larger adipocytes have reduced membrane cholesterol concentrations compared with smaller fat cells, demonstrating that altered cholesterol distribution is characteristic of adipocyte hypertrophy per se. We show that treatment with methyl-beta-cyclodextrin, which mimics the membrane cholesterol reduction of hypertrophied adipocytes, induces insulin resistance. We also produced cholesterol depletion by mevastatin treatment, which activates SREBP-2 and its target genes. The analysis of 40 adipocyte genes showed that the response to cholesterol depletion implicated genes involved in cholesterol traffic (caveolin 2, scavenger receptor BI, and ATP binding cassette 1 genes) but also adipocyte-derived secretion products (tumor necrosis factor alpha, angiotensinogen, and interleukin-6) and proteins involved in energy metabolism (fatty acid synthase, GLUT 4, and UCP3). These data demonstrate that altering cholesterol balance profoundly modifies adipocyte metabolism in a way resembling that seen in hypertrophied fat cells from obese rodents or humans. This is the first evidence that intracellular cholesterol might serve as a link between fat cell size and adipocyte metabolic activity. (+info)Carboxypeptidase H is also known as carboxypeptidase E or CPE. It is an enzyme that plays a role in the processing and activation of neuropeptides, which are small protein-like molecules that function as chemical messengers within the nervous system. Carboxypeptidase H/E is responsible for removing certain amino acids from the end of newly synthesized neuropeptides, allowing them to become biologically active. It is widely expressed in the brain and other tissues throughout the body.
Carboxypeptidases are a group of enzymes that catalyze the cleavage of peptide bonds at the carboxyl-terminal end of polypeptides or proteins. They specifically remove the last amino acid residue from the protein chain, provided that it has a free carboxyl group and is not blocked by another chemical group. Carboxypeptidases are classified into two main types based on their catalytic mechanism: serine carboxypeptidases and metallo-carboxypeptidases.
Serine carboxypeptidases, also known as chymotrypsin C or carboxypeptidase C, use a serine residue in their active site to catalyze the hydrolysis of peptide bonds. They are found in various organisms, including animals and bacteria.
Metallo-carboxypeptidases, on the other hand, require a metal ion (usually zinc) for their catalytic activity. They can be further divided into several subtypes based on their structure and substrate specificity. For example, carboxypeptidase A prefers to cleave hydrophobic amino acids from the carboxyl-terminal end of proteins, while carboxypeptidase B specifically removes basic residues (lysine or arginine).
Carboxypeptidases have important roles in various biological processes, such as protein maturation, digestion, and regulation of blood pressure. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.
Mannoheptulose is a type of sugar that occurs naturally in some plants, including avocados and a few other fruits. Its chemical formula is C7H14O7, and it's a heptose (a monosaccharide or simple sugar with seven carbon atoms) with a mannose configuration.
In the context of medical definitions, mannoheptulose might be mentioned in relation to certain metabolic disorders or dietary considerations. For instance, some research has suggested that mannoheptulose may have an impact on insulin secretion and glucose metabolism, although its effects are not fully understood and it is not widely used in clinical practice.
It's worth noting that while mannoheptulose does occur naturally in some foods, it's not a common or well-known sugar, and it's not typically included as an added ingredient in processed foods. As with any sugar or sweetener, it's generally a good idea to consume it in moderation as part of a balanced diet.
Chromaffin granules are membrane-bound organelles found in the cytoplasm of chromaffin cells, which are a type of neuroendocrine cell. These cells are located in the adrenal medulla and some sympathetic ganglia and play a crucial role in the body's stress response.
Chromaffin granules contain a variety of substances, including catecholamines such as epinephrine (adrenaline) and norepinephrine (noradrenaline), as well as proteins and other molecules. When the chromaffin cell is stimulated, the granules fuse with the cell membrane and release their contents into the extracellular space, where they can bind to receptors on nearby cells and trigger a variety of physiological responses.
The name "chromaffin" comes from the fact that these granules contain enzymes that can react with chromium salts to produce a brown color, which is why they are also sometimes referred to as "black-brown granules."
Carboxypeptidase B is a type of enzyme that belongs to the peptidase family. It is also known as carboxypeptidase B1 or CpB. This enzyme plays a crucial role in the digestion of proteins by cleaving specific amino acids from the carboxyl-terminal end of polypeptides.
Carboxypeptidase B preferentially removes basic arginine and lysine residues from protein substrates, making it an essential enzyme in various physiological processes, including blood clotting, hormone processing, and neuropeptide metabolism. It is synthesized as an inactive zymogen, procarboxypeptidase B, which is converted to its active form upon proteolytic activation.
In addition to its physiological functions, carboxypeptidase B has applications in research and industry, such as protein sequencing, peptide synthesis, and food processing.
Carboxypeptidases A are a group of enzymes that play a role in the digestion of proteins. They are found in various organisms, including humans, and function to cleave specific amino acids from the carboxyl-terminal end of protein substrates. In humans, Carboxypeptidase A is primarily produced in the pancreas and secreted into the small intestine as an inactive zymogen called procarboxypeptidase A.
Procarboxypeptidase A is activated by trypsin, another proteolytic enzyme, to form Carboxypeptidase A1 and Carboxypeptidase A2. These enzymes have different substrate specificities, with Carboxypeptidase A1 preferentially cleaving aromatic amino acids such as phenylalanine and tyrosine, while Carboxypeptidase A2 cleaves basic amino acids such as arginine and lysine.
Carboxypeptidases A play a crucial role in the final stages of protein digestion by breaking down large peptides into smaller di- and tripeptides, which can then be absorbed by the intestinal epithelium and transported to other parts of the body for use as building blocks or energy sources.
Lysine carboxypeptidase is not a widely recognized or used medical term. However, in biochemistry, carboxypeptidases are enzymes that cleave peptide bonds at the carboxyl-terminal end of a protein or peptide. If there is a specific enzyme named "lysine carboxypeptidase," it would be an enzyme that selectively removes lysine residues from the carboxyl terminus of a protein or peptide.
There are several enzymes that can act as carboxypeptidases, and some of them have specificities for certain amino acids, such as arginine or lysine. These enzymes play important roles in various biological processes, including protein degradation, processing, and regulation.
It's worth noting that the term "lysine carboxypeptidase" may refer to different enzymes depending on the context, such as bacterial or mammalian enzymes, and they may have different properties and functions.
Cathepsin A is a lysosomal protein that belongs to the peptidase family. It plays a role in various biological processes, including protein degradation and activation, cell signaling, and inflammation. Cathepsin A has both endopeptidase and exopeptidase activities, which allow it to cleave and process a wide range of substrates.
In addition to its enzymatic functions, cathepsin A also plays a structural role in the formation and stability of the protective protein complex called the "serglycin-cathepsin A proteoglycan complex." This complex protects certain proteases from degradation and helps regulate their activity within the lysosome.
Deficiencies or mutations in cathepsin A have been linked to several diseases, including a rare genetic disorder called galactosialidosis, which is characterized by developmental delays, coarse facial features, and progressive neurological deterioration.
Carboxypeptidase
Carboxypeptidase P
Muramoyltetrapeptide carboxypeptidase
Carboxypeptidase D
Glutamate carboxypeptidase
Carboxypeptidase B2
Carboxypeptidase E
Dipeptidyl carboxypeptidase
Carboxypeptidase G
Carboxypeptidase B
Muramoylpentapeptide carboxypeptidase
Carboxypeptidase U
Carboxypeptidase C
Carboxypeptidase A
Lysine carboxypeptidase
Carboxypeptidase A6
Arginine carboxypeptidase
Carboxypeptidase M
DD-carboxypeptidase
Carboxypeptidase A2
Carboxypeptidase T
Carboxypeptidase A1
Alanine carboxypeptidase
Zinc carboxypeptidase
Carboxypeptidase Taq
Carboxypeptidase D (disambiguation)
Gly-X carboxypeptidase
Glutamate carboxypeptidase II
Carboxypeptidase A inhibitor
Potato carboxypeptidase inhibitor
Carboxypeptidase - Wikipedia
Scpep1 serine carboxypeptidase 1 [Mus musculus (house mouse)] - Gene - NCBI
Cpa2 MGI Mouse Gene Detail - MGI:3617840 - carboxypeptidase A2, pancreatic
Glutamate carboxypeptidase II - wikidoc
Carboxypeptidase E/CPE Antibody (NBP2-15699): Novus Biologicals
SCOP 1.55: Fold e.3: beta-Lactamase/D-ala carboxypeptidase
JCI - An N-terminal truncated carboxypeptidase E splice isoform induces tumor growth and is a biomarker for predicting future...
Carboxypeptidase E is a Sorting Receptor for the Regulated Secretory Pathway - Y. Peng Loh Lab | NICHD - Eunice Kennedy Shriver...
Submit a review for Human Carboxypeptidase A1/CPA1 Antibody (MAB2856): R&D Systems: R&D Systems
Drug Repurposing Against Angiotensin-Converting Enzyme-Related Carboxypeptidase (ACE2) Through Computational Approach - PubMed
ENZYME - 3.4.16.6 carboxypeptidase D
carboxypeptidases | NAL Agricultural Thesaurus
Novel interaction between neurotrophic factor-α1/carboxypeptidase E and serotonin receptor, 5-HTR1E, protects human neurons...
Carboxypeptidase E/Neurotrophic factor-α1 is a novel neuroprotective protein functioning independently of its prohormone...
Reactome | Carboxypeptidase [extracellular region]
Effects of rituximab and infliximab on carboxypeptidase B and its substrates in RA synovium
Carboxypeptidase | DC Chemicals
RCSB PDB Group Summary: 550 30
Glutamate Carboxypeptidase II | Profiles RNS
GO:0004180: carboxypeptidase activity details
Anti-Carboxypeptidase A1 Rabbit Polyclonal Antibody | VWR
Carboxypeptidase U - Institutional Repository University of Antwerp
Carboxypeptidases. Medical search. Definitions
Human CPA4(Carboxypeptidase A4) ELISA Kit - Lotuskring Poeldijk
Single-cell dynamics of the chromosome replication and cell division cycles in mycobacteria | Nature Communications
Publication: Identification of prolyl carboxypeptidase as an alternative enzyme for processing …
Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints....
Carboxypeptidase D is a potential candidate to carry out redundant processing functions of carboxypeptidase E based on...
About Suchandrima Bhowmik - Page 20
Enzymes2
- Enzymes that use a metal in the active site are called "metallo-carboxypeptidases" (EC number 3.4.17). (wikipedia.org)
- carboxypeptidases Two enzymes (A and B) found in pancreatic juice. (fao.org)
Pancreatic2
- Initial studies on carboxypeptidases focused on pancreatic carboxypeptidases A1, A2, and B in the digestion of food. (wikipedia.org)
- In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active form - carboxypeptidase A - by the enzyme trypsin. (wikipedia.org)
Lysine1
- Carboxypeptidases that cleave positively charged amino acids (arginine, lysine) are called carboxypeptidase B (B for basic). (wikipedia.org)
Inhibitor6
- 2-PMPA is a potent and selective inhibitor of glutamate carboxypeptidase II (GCPII) with an IC50 of 300 pM. (dcchemicals.com)
- Carboxypeptidase G2 (CPG2) Inhibitor is a novel Carboxypeptidase G2 (CPG2) Inhibitor, Antitumor agents. (dcchemicals.com)
- CPA inhibitor is a potent inhibitor for carboxypeptidase A (CPA). (dcchemicals.com)
- 2-Benzylsuccinic acid (DL-Benzylsuccinic acid) is an potent inhibitor of carboxypeptidase A (CPA). (dcchemicals.com)
- GCPII-IN-1 is a glutamate carboxypeptidase II (GCPII, or PSMA) inhibitor scaffold with a Ki of 44.3 nM. (dcchemicals.com)
- Furthermore, the dual prolyl carboxypeptidase (PCP)-prolyl endopeptidase (PEP) inhibitor Z-prolyl-prolinal reduced ANG-(1-7) formation in ACE2 KO mice, while the ACE2 inhibitor MLN-4760 had no effect. (nih.gov)
Gene6
- Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1. (nih.gov)
- Glutamate carboxypeptidase II ( GCPII ), also known as N-acetyl-L-aspartyl-L-glutamate peptidase I (NAALADase I), NAAG peptidase , or prostate-specific membrane antigen ( PSMA ) is an enzyme that in humans is encoded by the FOLH1 ( folate hydrolase 1 ) gene . (wikidoc.org)
- This gene encodes a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters, including insulin. (novusbio.com)
- We report here that the carboxypeptidase E gene (CPE) is alternatively spliced in human tumors to yield an N-terminal truncated protein (CPE-ΔN) that drives metastasis. (jci.org)
- The technology from the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD), describes that direct administration of an adenovirus carrying the Carboxypeptidase E (CPE) gene to the hippocampus results in overexpression of the CPE protein in an experimental mouse model of AD. (nih.gov)
- 2023) Hippocampal delivery of neurotrophic factor-α1/carboxypeptidase E gene prevents neurodegeneration, amyloidosis, memory loss in Alzheimer's Disease male mice. (nih.gov)
Enzyme4
- A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. (wikipedia.org)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Carboxypeptidase A4 (CPA4) in serum, plasma, tissue homogenates and other biological fluids. (lotuskringpoeldijk.nl)
- Identification of prolyl carboxypeptidase as an alternative enzyme for processing of renal angiotensin II using mass spectrometry. (nih.gov)
- Carboxypeptidase E was thought to be the only enzyme responsible. (elsevierpure.com)
Prolyl carboxypeptidase1
- Background Prolyl carboxypeptidase (PRCP) is involved in the regulation of body weight, likely by hydrolysing alpha-melanocyte-stimulating hormone and apelin in the hypothalamus and in the periphery. (uantwerpen.be)
Serine carboxypeptidases2
- Other carboxypeptidases that use active site serine residues are called "serine carboxypeptidases" (EC number 3.4.16). (wikipedia.org)
- Mice, double deficient in lysosomal serine carboxypeptidases Scpep1 and Cathepsin A develop the hyperproliferative vesicular corneal dystrophy and hypertrophic skin thickenings. (nih.gov)
Glutamate carboxypeptidase4
- All of which refer to the same protein glutamate carboxypeptidase II. (wikidoc.org)
- Glutamate Carboxypeptidase II" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (wakehealth.edu)
- This graph shows the total number of publications written about "Glutamate Carboxypeptidase II" by people in this website by year, and whether "Glutamate Carboxypeptidase II" was a major or minor topic of these publications. (wakehealth.edu)
- Below are the most recent publications written about "Glutamate Carboxypeptidase II" by people in Profiles. (wakehealth.edu)
Neurotrophic1
- Carboxypeptidase E (CPE) also known as Neurotrophic factor-α1 (NF-α1), was first identified as an exopeptidase and is highly expressed in the nervous and endocrine systems. (nih.gov)
Protein2
- Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. (wikipedia.org)
- Recombinant protein encompassing a sequence within the center region of human Carboxypeptidase E. The exact sequence is proprietary. (novusbio.com)
Peptide2
- The extensive distribution of carboxypeptidase D in both glial and neuronal cells indicates the important role of carboxypeptidase D in peptide processing, possibly working together with furin, a ubiquitously expressed proprotein convertase. (elsevierpure.com)
- Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. (abcam.com)
Hydrolysis1
- The carboxypeptidase A hydrolysis reaction has two mechanistic hypotheses, via a nucleophilic water and via an anhydride. (wikipedia.org)
Putative2
- Functional characterization of a putative serine carboxypeptidase in vascular smooth muscle cells. (nih.gov)
- We have generated a molecular model of CPE, and structural alignment with other carboxypeptidases revealed a putative sorting signal binding domain that is independent of the enzymatic site. (nih.gov)
Antibody4
- Western Blot: Carboxypeptidase E/CPE Antibody [NBP2-15699] - Analysis of CPE expression in transfected 293T cell line by CPE polyclonal antibody. (novusbio.com)
- Western Blot: Carboxypeptidase E/CPE Antibody [NBP2-15699] - Sample (20 ug of whole cell lysate) A: mouse brain 10% SDS PAGE gel, diluted at 1:10000. (novusbio.com)
- Immunohistochemistry-Paraffin: Carboxypeptidase E/CPE Antibody [NBP2-15699] - Human breast cancer. (novusbio.com)
- Carboxypeptidase E antibody [N2C2], Internal dilution: 1:500. (novusbio.com)
Catalytic1
- A transmembrane glycoprotein with an extracellular catalytic domain which functions as a carboxypeptidase. (nih.gov)
Amino acid1
- A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. (lookformedical.com)
Serum2
- Description: A sandwich ELISA kit for detection of Carboxypeptidase A4 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (lotuskringpoeldijk.nl)
- Description: A competitive ELISA for quantitative measurement of Rat Carboxypeptidase A4(CPA4) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (lotuskringpoeldijk.nl)
Specificity1
- Carboxypeptidases of broad specificity with optimum pH 4.5-6.0, inhibited by the action of diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents. (expasy.org)
Immunohistochemistry1
- Immunohistochemistry showed the intracellular distribution of carboxypeptidase D with a perinuclear pattern. (elsevierpure.com)
Plasma1
- VORAXAZE is a carboxypeptidase indicated to reduce toxic plasma methotrexate concentration (greater than 1 micromole per liter) in adult and pediatric patients with delayed methotrexate clearance (plasma methotrexate concentrations greater than 2 standard deviations of the mean methotrexate excretion curve specific for the dose of methotrexate administered) due to impaired renal function. (nih.gov)
Mice2
- Recent studies with carboxypeptidase E-deficient mice, Cpe(fat)/Cpe(fat), indicated the existence of carboxypeptidase E-like carboxypeptidases, such as carboxypeptidase D. In order to define potential redundant functions in vivo, we compared the distributions of both carboxypeptidases in the rat central nervous system and selected endocrine tissues. (elsevierpure.com)
- The co-localization of carboxypeptidases D and E suggests that carboxypeptidase D may, at least partially, compensate for carboxypeptidase E processing functions in Cper(fat)/Cpe(fat) mice. (elsevierpure.com)
Peptides2
- They also regulate biological processes, such as the biosynthesis of neuroendocrine peptides such as insulin requires a carboxypeptidase. (wikipedia.org)
- Carboxypeptidases hydrolyze peptides at the first amide or polypeptide bond on the C-terminal end of the chain. (wikipedia.org)
Human1
- Orthologous to human SCPEP1 (serine carboxypeptidase 1). (nih.gov)
Hippocampus1
- Carboxypeptidase D messenger RNA was abundantly expressed in glial cells in the gray and white matter, while neurons in several brain regions, such as the piriform cortex, basolateral amygdala and hippocampus, also expressed high levels of carboxypeptidase D messenger RNA. (elsevierpure.com)
Tissues2
- Co-localization of carboxypeptidases E and D messenger RNAs was observed in many brain regions, the spinal cord and endocrine tissues. (elsevierpure.com)
- Carboxypeptidase Q (CPQ) mRNA expression was higher in glioblastoma (GBM) tissues than in normal tissues. (amegroups.org)
Activity2
Methotrexate2
Family1
- In peptidase family S10 (carboxypeptidase C family). (genome.jp)
Primary1
- A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. (lookformedical.com)
Release1
- Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids . (lookformedical.com)
Form1
- The membrane-bound form of Carboxypeptidase E (CPE) was identified as a sorting receptor for the regulated secretory pathway through studies carried out in our lab. (nih.gov)
Cells1
- This mechanism ensures that the cells wherein pro-carboxypeptidase A is produced are not themselves digested. (wikipedia.org)