carboxypeptidase e การใช้
- At the C-terminus Carboxypeptidase E then removes the terminal lysine and arginine residues.
- Carboxypeptidase E is a glycoprotein that exists in both membrane-associated and soluble forms.
- Mice with mutant carboxypeptidase E, Cpe fat, display endocrine disorders like obesity and infertility.
- Within cells, carboxypeptidase E is present in the secretory granules along with its peptide substrates and products.
- Carboxypeptidase E is found in brain and throughout the neuroendocrine system, including the endocrine pancreas, pituitary, and adrenal gland chromaffin cells.
- However, this role for carboxypeptidase E remains controversial, and evidence shows that this enzyme is not necessary for the sorting of regulated secretory proteins.
- Carboxypeptidase E is not found in the fruit fly ( Drosophila ), and another enzyme ( presumably carboxypeptidase D ) fills in for carboxypeptidase E in this organism.
- Carboxypeptidase E is not found in the fruit fly ( Drosophila ), and another enzyme ( presumably carboxypeptidase D ) fills in for carboxypeptidase E in this organism.
- It binds carboxypeptidase E ( CPE ), and the disruption of this binding has been proposed to cause the loss of sorting of BDNF into dense-core vesicles.
- Carboxypeptidase E is found in all species of vertebrates that have been examined, and is also present in many other organisms that have been studied ( nematode, sea slug ).
- It has been proposed that membrane-associated carboxypeptidase E acts as a trans-Golgi network of the pituitary and in secretory granules; regulated secretory proteins are mostly hormones and neuropeptides.
- In obesity, high levels of circulating free fatty acids have been reported to cause a decrease in the amount of carboxypeptidase E protein in pancreatic beta-cells, leading to beta-cell dysfunction ( hyperproinsulinemia ) and increased beta-cell apoptosis ( via an increase in ER-stress ).
- Metallocarboxypeptidase D is located in the trans Golgi network where it contributes to the biosynthesis of neuropeptides and peptide hormones ( such as insulin ) along with carboxypeptidase E . In addition to this role, metallocarboxypeptidase D contributes to the processing of proteins, following the action of furin ( an endoprotease located in the trans Golgi network ).