scholarly journals Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases

2014 ◽  
Vol 54 (1) ◽  
pp. 5-16 ◽  
Author(s):  
Gregory R. Wagner ◽  
Matthew D. Hirschey
Keyword(s):  
Protein Acylation ◽  
Carbon Stress

Sirt5 Plays a Critical Role in Mitochondrial Protein Acylation and Mitochondrial Metabolic Homeostasis in Brown Fat

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 274-OR ◽  
Author(s):  
GUOXIAO WANG ◽  
JESSE G. MEYER ◽  
WEIKANG CAI ◽  
MENGYAO E. LI ◽  
SAMIR SOFTIC ◽  
...  
Keyword(s):  
Critical Role ◽  
Mitochondrial Protein ◽  
Brown Fat ◽  
Metabolic Homeostasis ◽  
Protein Acylation

scholarly journals The acylation of proteins by xenobiotic amphipathic carboxylic acids in cultured rat hepatocytes

1988 ◽  
Vol 254 (1) ◽  
pp. 39-44 ◽  
Author(s):  
R Hertz ◽  
J Bar−Tana
Keyword(s):  
Protein Synthesis ◽  
Carboxylic Acids ◽  
Mode Of Action ◽  
Biological Effects ◽  
Rat Hepatocytes ◽  
Protein Adducts ◽  
Cultured Rat Hepatocytes ◽  
Acylated Proteins ◽  
Dose Dependent ◽  
Protein Acylation

Three xenobiotic amphipathic carboxylates, namely MEDICA 16, nafenopin and bezafibrate, which differ remarkably in their hydrophobic backbones, were found to acylate membrane and cytosolic liver proteins in cultured rat hepatocytes. The acylation patterns observed were time- and dose-dependent, and the acylated residue consisted of the original xenobiotic. The acylation patterns generated by the three xenobiotic carboxylates included common proteins which were acylated by the three xenobiotics (e.g. proteins of 32, 52, 56 and 72 kDa) as well as unique proteins which were specifically acylated by the respective xenobiotics. The acylation of liver proteins by either MEDICA 16 or nafenopin remained unaffected under conditions where protein synthesis was completely inhibited by cycloheximide. Protein acylation thus offers a common mode of action of xenobiotic amphipathic carboxylates, which may, however, result in diverse xenobiotyl-protein adducts. The xenobiotyl-acylated proteins might be involved in triggering some of the biological effects exerted by xenobiotic amphipathic carboxylates employed as hypolipidaemic effectors, peroxisomal proliferators or preadipocyte convertors.

scholarly journals The acylation of megakaryocyte proteins: glycoprotein IX is primarily myristoylated while glycoprotein Ib is palmitoylated

Blood ◽  
1996 ◽  
Vol 87 (4) ◽  
pp. 1377-1384 ◽  
Author(s):  
PK Schick ◽  
J Walker
Keyword(s):  
Fatty Acids ◽  
Myristic Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Amide Bond ◽  
Endogenous Protein ◽  
Sds Page ◽  
Palmitic Acids ◽  
Protein Acylation

The acylation of megakaryocyte proteins was studied with special emphasis on the myristoylation and palmitoylation of the glycoprotein (GP) Ib complex. Guinea pig megakaryocytes were purified and separated into subpopulations at different phases of maturation. Cells were incubated with [3H]myristate, [3H]palmitate, or [3H]acetate to study endogenous protein acylation. Cycloheximide was used to distinguish between cotranslational and posttranslational acylation and hydroxylamine to distinguish between thioester and amide linkages. After incubations, delipidated proteins or GPIb complex subunits, immunoprecipitated with PG-1, AN-51 or FMC-25 monoclonal antibody, were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and assessed by fluorography. Radiolabeled fatty acids bound to GPIX and GPIb were also analyzed by high pressure liquid chromatography (HPLC) and scintillation spectrometry. With [3H]myristic acid and [3H]acetate, GPIX was found to be a major myristoylated protein in megakaryocytes and CHRF-288 cells. Myristic acid was linked to GPIX by an amide bond, and this process occurred cotranslationally. With [3H]acetate, GPIb was primarily palmitoylated, but with [3H]myristate, GPIb was acylated with about equal mounts of myristic acid and palmitic acids. Both fatty acids were linked to GPIb by thioester bonds, and acylation was posttranslational. The myristoylation of GPIX while the palmitoylation of GPIb occurred throughout megakaryocyte maturation. Myristoylation and palmitoylation may have different functions relevant to the assembly of the GPIb complex in megakaryocytes.

Mass Spectrometric Methods for Peptide Sequencing: Applications to Immunology and Protein Acylation

1996 ◽  
pp. 281-305 ◽  
Author(s):  
Pamela H. Gulden ◽  
Murray Hackett ◽  
Theresa A. Addona ◽  
Lin Guo ◽  
Carthene B. Walker ◽  
...  
Keyword(s):  
Peptide Sequencing ◽  
Mass Spectrometric ◽  
Protein Acylation

scholarly journals Modulation of protein function by protein-acylation.

1992 ◽  
Vol 32 (5) ◽  
pp. 243-248
Author(s):  
Toshihiko UTSUMI
Keyword(s):  
Protein Function ◽  
Protein Acylation

Quantitation of Reactive Acyl-CoA Species Mediated Protein Acylation by HPLC–MS/MS

2019 ◽  
Vol 91 (19) ◽  
pp. 12336-12343 ◽  
Author(s):  
Tim Baldensperger ◽  
Simone Di Sanzo ◽  
Alessandro Ori ◽  
Marcus A. Glomb
Keyword(s):  
Protein Acylation

PHB accumulation in Nostoc muscorum under different carbon stress situations

2011 ◽  
Vol 24 (2) ◽  
pp. 157-162 ◽  
Author(s):  
Sandra Mareike Haase ◽  
Bernhard Huchzermeyer ◽  
Thomas Rath
Keyword(s):  
Nostoc Muscorum ◽  
Carbon Stress

scholarly journals Time-dependent potentiation of the beta-cell is a Ca2+-independent phenomenon

2002 ◽  
Vol 172 (2) ◽  
pp. 345-354 ◽  
Author(s):  
S Yamada ◽  
M Komatsu ◽  
T Aizawa ◽  
Y Sato ◽  
H Yajima ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Glucose Metabolism ◽  
Underlying Mechanism ◽  
Subsequent Treatment ◽  
Time Dependent ◽  
Kinase C ◽  
High K ◽  
Camp Levels ◽  
Protein Acylation ◽  
Isolated Rat

When isolated rat pancreatic islets are treated with 16.7 mM glucose, a time-dependent potentiation (TDP) of insulin release occurs that can be detected by subsequent treatment with 50 mM KCl. It has been thought that TDP by glucose is a Ca2+-dependent phenomenon and only occurs when exposure to glucose is carried out in the presence of Ca2+. In contrast to this, we now demonstrate TDP under stringent Ca2+-free conditions (Ca2+-free buffer containing 1 mM EGTA). In fact, under these Ca2+-free conditions glucose caused an even stronger TDP than in the presence of Ca2+. TDP induced by glucose in the absence of extracellular Ca2+ was unaffected by inhibitors of protein kinase C (PKC). However, cerulenin or tunicamycin, two inhibitors of protein acylation, eradicated TDP without affecting glucose metabolism. The TDP by glucose was not associated with an increase in the cytosolic free Ca2+ concentration ([Ca2+]i) during subsequent treatment with high K+. Exposure of islets to forskolin under Ca(2+)-free conditions did not cause TDP despite a large increase in the cellular cAMP levels. In conclusion, glucose alone induces TDP under stringent Ca2+-free conditions when [Ca2+]i was significantly lowered. Protein acylation is implicated in the underlying mechanism of TDP.

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