BIOMAT Database Logo BIOMAT Database Logo

Requirement of GM2 ganglioside activator for phospholipase D activation. 1998

S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
Department of Biochemistry, Kobe University School of Medicine, Kobe 650-0017, Japan.

Sequence analysis of a heat-stable protein necessary for the activation of ADP ribosylation factor-dependent phospholipase D (PLD) reveals that this protein has a structure highly homologous to the previously known GM2 ganglioside activator whose deficiency results in the AB-variant of GM2 gangliosidosis. The heat-stable activator protein indeed has the capacity to enhance enzymatic conversion of GM2 to GM3 ganglioside that is catalyzed by beta-hexosaminidase A. Inversely, GM2 ganglioside activator purified separately from tissues as described earlier [Conzelmann, E. & Sandhoff, K. (1987) Methods Enzymol. 138, 792-815] stimulates ADP ribosylation factor-dependent PLD in a dose-dependent manner. At higher concentrations of ammonium sulfate, the PLD activator protein apparently substitutes for protein kinase C and phosphatidylinositol 4,5-bisphosphate, both of which are known as effective stimulators of the PLD reaction. The mechanism of action of the heat-stable PLD activator protein remains unknown.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010739 Phospholipase D An enzyme found mostly in plant tissue. It hydrolyzes glycerophosphatidates with the formation of a phosphatidic acid and a nitrogenous base such as choline. This enzyme also catalyzes transphosphatidylation reactions. EC 3.1.4.4. Lecithinase D,Phosphatidylcholine Phosphohydrolase
D011493 Protein Kinase C An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters. Calcium Phospholipid-Dependent Protein Kinase,Calcium-Activated Phospholipid-Dependent Kinase,PKC Serine-Threonine Kinase,Phospholipid-Sensitive Calcium-Dependent Protein Kinase,Protein Kinase M,Calcium Activated Phospholipid Dependent Kinase,Calcium Phospholipid Dependent Protein Kinase,PKC Serine Threonine Kinase,Phospholipid Sensitive Calcium Dependent Protein Kinase,Phospholipid-Dependent Kinase, Calcium-Activated,Serine-Threonine Kinase, PKC
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017386 Sequence Homology, Amino Acid The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species. Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein
D049289 G(M2) Activator Protein An essential cofactor for the degradation of G(M2)GANGLIOSIDE by lysosomal BETA-N-ACETYLHEXOSAMINIDASES. Genetic mutations resulting in loss of G(M2) activator protein are one of the causes of TAY-SACHS DISEASE, AB VARIANT. GM(2) Activating Protein,GM2 Activator Protein,Hexosaminidase Activator,Activator Protein, GM2

Related Publications

S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
Characterization of phospholipase D activation by GM2 activator in a cell-free system.
August 1999, The Kobe journal of medical sciences,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
[GM2 ganglioside activator protein deficiency].
January 1998, Ryoikibetsu shokogun shirizu,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
GM2 ganglioside activator occurs in multiple forms.
March 1994, Biochimica et biophysica acta,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
Membrane lipids regulate ganglioside GM2 catabolism and GM2 activator protein activity.
September 2015, Journal of lipid research,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
A protein activator for the enzymic hydrolysis of GM2 ganglioside.
June 1981, The Journal of biological chemistry,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
Synthesis of 6'-GM2, a regioisomer of ganglioside GM2, for studying the mechanism of action of GM2 activator.
August 1997, Carbohydrate research,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
Adipokine ganglioside GM2 activator protein stimulates insulin secretion.
August 2011, FEBS letters,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
Photoaffinity labelling of the human GM2-activator protein. Mechanistic insight into ganglioside GM2 degradation.
February 2004, European journal of biochemistry,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
Formation of a ternary complex between GM2 activator protein, GM2 ganglioside and hexosaminidase A.
June 1997, Biochimica et biophysica acta,
S Nakamura, and T Akisue, and H Jinnai, and T Hitomi, and S Sarkar, and N Miwa, and T Okada, and K Yoshida, and S Kuroda, and U Kikkawa, and Y Nishizuka
Location of ganglioside GM2 activator protein gene expression in sheep.
November 1998, Clinical and experimental pharmacology & physiology. Supplement,
Copied contents to your clipboard!