Studies of in vivo phosphorylated proteins in BC3H-1 myocytes suggest that protein kinase C is involved in insulin action.
نویسندگان
چکیده
Insulin (10 and 100 nM) and phorbol esters increased the phosphorylation of several proteins, including 40, 47 and 80 kDa proteins, which are markers for protein kinase C activation. Insulin effects were evident at 2 min and increased over 20 min. These findings suggest that insulin activates protein kinase C in BC3H-1 myocytes.
منابع مشابه
The Role of Fetuin-A in Diabetes and Obesity: The Mechanism and Action
Fetuin-A is a phosphorylated glycoprotein produced by liver.It by binding to calcium ion inhibits ectopic calcium deposition and protects vascular calcification. Fetuin-A acts as a multifactorial protein and its role has been documented from brain development to bone remodeling and immune function, regulation of insulin activity, hepatocyte growth factor activity and inhibition lymphocyte blast...
متن کاملSimultaneous Effects of Metformin and Sitagliptin on the Contents of Insulin Resistance Proteins Glucose Transporter 4 and Protein Kinase B in Diabetic Patients\' Adipose Tissue
Objective: Obesity is a factor in the development of insulin resistance and type 2 diabetes. Obesity contributes a wide variety of metabolic changes such as insulin resistance. The insulin signal mechanism to intra-cells occurs in insulin resistance, primarily in adipose tissue cells, which can be appropriate targets for therapeutic approaches by recognizing the proteins in this pathway. The st...
متن کاملEffects of insulin and phorbol esters on MARCKS (myristoylated alanine-rich C-kinase substrate) phosphorylation (and other parameters of protein kinase C activation) in rat adipocytes, rat soleus muscle and BC3H-1 myocytes.
To evaluate the question of whether or not insulin activates protein kinase C (PKC), we compared the effects of insulin and phorbol esters on the phosphorylation of the PKC substrate, i.e. myristoylated alanine-rich C-kinase substrate (MARCKS). In rat adipocytes, rat soleus muscle and BC3H-1 myocytes, maximally effective concentrations of insulin and phorbol esters provoked comparable, rapid, 2...
متن کاملPertussis toxin treatment attenuates some effects of insulin in BC3H-1 murine myocytes.
The effects of pertussis toxin (PT) treatment on insulin-stimulated myristoyl-diacylglycerol (DAG) generation, hexose transport, and thymidine incorporation were studied in differentiated BC3H-1 myocytes. Insulin treatment caused a biphasic increase in myristoyl-DAG production which was abolished in myocytes treated with PT. There was no effect of PT treatment on basal (nonstimulated) myristoyl...
متن کاملThe adapter protein ZIP binds Grb14 and regulates its inhibitory action on insulin signaling by recruiting protein kinase Czeta.
Grb14 is a member of the Grb7 family of adapters and acts as a negative regulator of insulin-mediated signaling. Here we found that the protein kinase Czeta (PKCzeta) interacting protein, ZIP, interacted with Grb14. Coimmunoprecipitation experiments demonstrated that ZIP bound to both Grb14 and PKCzeta, thereby acting as a link in the assembly of a PKCzeta-ZIP-Grb14 heterotrimeric complex. Mapp...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- FEBS letters
دوره 244 1 شماره
صفحات -
تاریخ انتشار 1989