Biomaterial Database

Protein synthesis in tumor host. I. Enhanced peptide elongation in transplantable tumors and host liver. 1978

Z Dusek, and J Hradec

Protein synthesis was significantly enhanced in subcellular systems containing ribosomes and cytosol from the liver of Walker tumor-bearing rats from the second week following the tumor transplantation and this enhancement persisted for the whole period of tumor growth. Homologous systems from Zajdela hepatoma and host liver showed a markedly increased poly(U)-dependent peptide elongation when compared with normal liver tissue. A stimulation of polyphenylalanine synthesis resulted from the addition of cytosols from tumors or host liver to ribosomes from normal rat liver. Similar results were found for the binding of phenylalanyl-tRNA to ribosomes. Ribosomes from tumors and host liver are more active in peptide elongation than particles from normal liver tissue. A more than 10-fold stimulation of phenylalanine polymerization resulted from the addition of poly(U) to ribosomes from Zajdela hepatoma whereas only less than 2-fold enhancement was found when using ribosomes from normal or host liver. Hepatoma ribosomes apparently contain only a low proportion of polyribosomes carrying natural message. Enhanced protein synthesis in tumors and host liver is apparently due, in particular, to an increased activity of soluble factors required for protein synthesis and less due to an increased activity of ribosomes.

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
D008114	Liver Neoplasms, Experimental	Experimentally induced tumors of the LIVER.	Hepatoma, Experimental,Hepatoma, Morris,Hepatoma, Novikoff,Experimental Hepatoma,Experimental Hepatomas,Experimental Liver Neoplasms,Hepatomas, Experimental,Neoplasms, Experimental Liver,Experimental Liver Neoplasm,Liver Neoplasm, Experimental,Morris Hepatoma,Novikoff Hepatoma
D008297	Male		Males
D009363	Neoplasm Proteins	Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm.	Proteins, Neoplasm
D010441	Peptide Chain Elongation, Translational	A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES.	Chain Elongation, Peptide, Translational,Protein Biosynthesis Elongation,Protein Chain Elongation, Translational,Protein Translation Elongation,Translation Elongation, Genetic,Translation Elongation, Protein,Translational Elongation, Protein,Translational Peptide Chain Elongation,Biosynthesis Elongation, Protein,Elongation, Genetic Translation,Elongation, Protein Biosynthesis,Elongation, Protein Translation,Elongation, Protein Translational,Genetic Translation Elongation,Protein Translational Elongation
D010445	Peptide Elongation Factors	Protein factors uniquely required during the elongation phase of protein synthesis.	Elongation Factor,Elongation Factors, Peptide,Factor, Elongation,Factors, Peptide Elongation
D003600	Cytosol	Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.	Cytosols
D005260	Female		Females
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
D012270	Ribosomes	Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.	Ribosome