Effects of thrombin and thrombin peptide activating receptor (SFLLRN) on proteoglycan synthesis and distribution in human endothelial cells. 1994

F Peracchia, and A Tamburro, and M Zanni, and D Rotilio
Istituto di Ricerche Farmacologiche Mario Negri Consorzio Mario Negri Sud, S. Maria Imbaro, Italy.

In the present study we compared the effect of alpha-thrombin and the active receptor peptide (SFLLRN) on proteoglycan (PG) release from human endothelial cells (HUVEC) exposed for 24 h in the presence of 35S-sulfate and 3H-glucosamine. The effect of thrombin (5U/ml) and receptor peptide (100 microM) was evaluated on the distribution of PGs in the conditioned medium, cellular extract and extracellular matrix. In the conditioned medium, thrombin increased the amount of PGs. In extracellular matrix thrombin decreased radioactive PGs measured by both isotopes; no difference was observed in cell extracts. SFLLRN peptide showed a consistent increase in PG content in the medium. At variance with thrombin, in cell extracts the peptide increased the amount of PGs. No relevant differences were observed in PG content of extracellular matrix. These results indicate that thrombin and the peptide act differently on PG distribution and underline the different role of the serine protease and of the receptor binding activities of thrombin.

UI MeSH Term Description Entries
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
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011509 Proteoglycans Glycoproteins which have a very high polysaccharide content. Proteoglycan,Proteoglycan Type H
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D004730 Endothelium, Vascular Single pavement layer of cells which line the luminal surface of the entire vascular system and regulate the transport of macromolecules and blood components. Capillary Endothelium,Vascular Endothelium,Capillary Endotheliums,Endothelium, Capillary,Endotheliums, Capillary,Endotheliums, Vascular,Vascular Endotheliums
D005109 Extracellular Matrix A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere. Matrix, Extracellular,Extracellular Matrices,Matrices, Extracellular
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
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
D013917 Thrombin An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN. Thrombase,Thrombin JMI,Thrombin-JMI,Thrombinar,Thrombostat,alpha-Thrombin,beta,gamma-Thrombin,beta-Thrombin,gamma-Thrombin,JMI, Thrombin
D018179 Receptors, Thrombin A family of proteinase-activated receptors that are specific for THROMBIN. They are found primarily on PLATELETS and on ENDOTHELIAL CELLS. Activation of thrombin receptors occurs through the proteolytic action of THROMBIN, which cleaves the N-terminal peptide from the receptor to reveal a new N-terminal peptide that is a cryptic ligand for the receptor. The receptors signal through HETEROTRIMERIC GTP-BINDING PROTEINS. Small synthetic peptides that contain the unmasked N-terminal peptide sequence can also activate the receptor in the absence of proteolytic activity. Thrombin Receptors,TRAP Peptide,Thrombin Receptor,Thrombin Receptor Activating Peptide Ligand,Thrombin Receptor Activating Peptides,Thrombin Receptor Activator Peptide,Peptide, TRAP,Receptor, Thrombin

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