Studies on the intracellular localization of acetyl-CoA carboxylase.
نویسندگان
چکیده
The present work was performed to identify the subcellular localization of hepatic acetyl-CoA carboxylase (ACC). Cellular organelles involved in fatty acid oxidation that contain a malonyl-CoA sensitive carnitine palmitoyltransferase (CPT) activity or that are linked to the control of this activity were analysed for the presence of ACC. No significant amount of ACC was observed in the mitochondrial fraction prepared from isolated rat hepatocytes. Furthermore, no association of ACC activity and mass with isolated hepatic peroxisomes could be detected. Incubation of isolated hepatocytes with compounds known to affect the integrity of the cytoskeleton like okadaic acid or taxol indicates that ACC is associated with this subcellular structure of the hepatocyte. Such association may allow for efficient regulation of CPT activity and thus of fatty acid oxidation.
منابع مشابه
Genetic Polymorphism Detection of the Exon 1 Region of Acetyl-CoA Carboxylase Alpha Gene in Iranian Mahabadi Goat Breed
Acetyl-coenzyme A carboxylase α (ACC-alpha) is considered as the key regulatory enzyme in fatty acid biosynthesis. ACC-alpha gene is located on Caprine chromosome 11 and is polymorphic in many goat breeds. In the current study, we aimed to find possible single nucleotide polymorphisms (SNPs) in the exon 1 region of the ACC-alpha gene in Iranian Mahabadi goat breed. Genomic DNA was extracted fro...
متن کاملResistance of various biotypes of Canary grass (phalaris. Spp) to acetyl-CoA carboxylase-inhibiting herbicides.
Little seed canary grass (Phalaris minor L.) is a major weed in wheat fields in some parts of Iran. To evaluate the efficacy of molecular and greenhouse methods in detecting the resistance of 49 biotypes of canary grass(Phalaris. Spp) to acetyl-CoA carboxylase-inhibiting herbicides, two methods including whole plant screening and PCR-based molecular methods were applied. Results showed that the...
متن کاملIncreasing the acetyl-CoA pool in the presence of overexpressed phosphoenolpyruvate carboxylase or pyruvate carboxylase enhances succinate production in Escherichia coli.
An in vivo strategy to apply the activation effect of acetyl-CoA on phosphoenolpyruvate carboxylase (PEPC) and pyruvate carboxylase (PYC) to increase succinate production in Escherichia coli was studied. This approach relies on the increased intracellular acetyl-CoA and CoA levels by overexpressing E. coli pantothenate kinase (PANK). The results showed that coexpression of PANK and PEPC, and PA...
متن کاملPrimary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence.
The complete amino acid sequence of acetyl-CoA carboxylase from chicken liver has been deduced by cloning and sequence analysis of DNA complementary to its messenger RNA. The results were confirmed by Edman degradation of peptide fragments obtained by digestion of the enzyme polypeptide with Achromobacter proteinase I or staphylococcal serine proteinase. Chicken liver acetyl-CoA carboxylase is ...
متن کاملNegative feedback regulation of fatty acid production based on a malonyl-CoA sensor-actuator.
Engineering metabolic biosynthetic pathways has enabled the microbial production of many useful chemicals. However, pathway productivities and yields are often limited by metabolic imbalances. Synthetic regulatory circuits have been shown to be able to balance engineered pathways, improving titers and productivities. Here we developed a negative feedback regulatory circuit based on a malonyl-Co...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Biochemical and biophysical research communications
دوره 233 1 شماره
صفحات -
تاریخ انتشار 1997