BIOMAT Database Logo BIOMAT Database Logo

Protein kinase C in signal transduction and carcinogenesis. 1994

P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Molecular Mechanisms of Tumor Promotion Section, National Cancer Institute, Bethesda, MD.

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D007783 Lactones Cyclic esters of hydroxy carboxylic acids, containing a 1-oxacycloalkan-2-one structure. Large cyclic lactones of over a dozen atoms are MACROLIDES. Lactone
D008809 Mice, Inbred C3H An inbred strain of mouse that is used as a general purpose strain in a wide variety of RESEARCH areas including CANCER; INFECTIOUS DISEASES; sensorineural, and cardiovascular biology research. Mice, C3H,Mouse, C3H,Mouse, Inbred C3H,C3H Mice,C3H Mice, Inbred,C3H Mouse,C3H Mouse, Inbred,Inbred C3H Mice,Inbred C3H Mouse
D010703 Phorbol Esters Tumor-promoting compounds obtained from CROTON OIL (Croton tiglium). Some of these are used in cell biological experiments as activators of protein kinase C. Phorbol Diester,Phorbol Ester,Phorbol Diesters,Diester, Phorbol,Diesters, Phorbol,Ester, Phorbol,Esters, Phorbol
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
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
D011956 Receptors, Cell Surface Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D002273 Carcinogens Substances that increase the risk of NEOPLASMS in humans or animals. Both genotoxic chemicals, which affect DNA directly, and nongenotoxic chemicals, which induce neoplasms by other mechanism, are included. Carcinogen,Oncogen,Oncogens,Tumor Initiator,Tumor Initiators,Tumor Promoter,Tumor Promoters,Initiator, Tumor,Initiators, Tumor,Promoter, Tumor,Promoters, Tumor
D002471 Cell Transformation, Neoplastic Cell changes manifested by escape from control mechanisms, increased growth potential, alterations in the cell surface, karyotypic abnormalities, morphological and biochemical deviations from the norm, and other attributes conferring the ability to invade, metastasize, and kill. Neoplastic Transformation, Cell,Neoplastic Cell Transformation,Transformation, Neoplastic Cell,Tumorigenic Transformation,Cell Neoplastic Transformation,Cell Neoplastic Transformations,Cell Transformations, Neoplastic,Neoplastic Cell Transformations,Neoplastic Transformations, Cell,Transformation, Cell Neoplastic,Transformation, Tumorigenic,Transformations, Cell Neoplastic,Transformations, Neoplastic Cell,Transformations, Tumorigenic,Tumorigenic Transformations
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

Related Publications

P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Signal transduction through protein kinase C.
March 2000, Pediatric nephrology (Berlin, Germany),
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Modulating protein kinase C signal transduction.
January 1998, Advances in pharmacology (San Diego, Calif.),
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Nuclear protein kinase C and signal transduction.
January 1993, Receptor,
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Nonmutagenic mechanisms in carcinogenesis: role of protein kinase C in signal transduction and growth control.
June 1991, Environmental health perspectives,
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Postischemic function and protein kinase C signal transduction.
June 1998, The Annals of thoracic surgery,
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Protein kinase C in IL-2 signal transduction.
January 1997, Immunologic research,
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Protein kinase C isoenzymes: divergence in signal transduction?
April 1993, The Biochemical journal,
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Signal transduction by protein kinase C in mammalian cells.
December 1998, Clinical and experimental pharmacology & physiology,
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
[Roles of protein kinase C substrates in signal transduction].
May 1991, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
P M Blumberg, and G Acs, and L B Areces, and M G Kazanietz, and N E Lewin, and Z Szallasi
Adaptor proteins in protein kinase C-mediated signal transduction.
October 2001, Oncogene,
Copied contents to your clipboard!