Biomaterial Database

G-CSF increases secretion of urokinase-type plasminogen activator by human lung cancer cells. 1998

X H Pei, and Y Nakanishi, and K Takayama, and F Bai, and M Kawasaki, and N Hara

Research Institute for Diseases of the Chest, Faculty of Medicine, Kyushu University, Fukuoka, Japan.

We reported previously that granulocyte colony-stimulating factor (G-CSF) can promote the invasion of human lung cancer cell lines in vitro. However, the exact mechanism of its stimulatory effect on invasion remains to be elucidated. In the present study we mainly focused our attention on the components of the plasminogen activation system in human lung cancer cell lines, because of the central role that plasminogen activators play in regulating extracellular proteolysis. We showed that G-CSF induced a dose-dependent increase in the urokinase-type plasminogen activator (uPA) activity in the conditioned medium of a PC-9 lung cancer cell line. When the amounts of uPA activity were quantitated by densitometry, we found that even at a concentration of 0.01 microg/ml, G-CSF had a stimulatory effect on the uPA release, while high concentrations caused a 3.6-fold increase at a maximum concentration of 1 microg/ml. A Western blot analysis of the conditioned medium confirmed the findings observed in a zymographic analysis. The observed increase in uPA protein was paralleled by a significant increase in the uPA mRNA levels after treatment with G-CSF. However, our experiments failed to identify any alteration in the plasminogen activator inhibitor (PAI) secretion caused by G-CSF. In addition, we also found the expression of G-CSF receptor by PC-9 cells, suggesting the possible pathway activated by G-CSF.

UI	MeSH Term	Description	Entries
D008175	Lung Neoplasms	Tumors or cancer of the LUNG.	Cancer of Lung,Lung Cancer,Pulmonary Cancer,Pulmonary Neoplasms,Cancer of the Lung,Neoplasms, Lung,Neoplasms, Pulmonary,Cancer, Lung,Cancer, Pulmonary,Cancers, Lung,Cancers, Pulmonary,Lung Cancers,Lung Neoplasm,Neoplasm, Lung,Neoplasm, Pulmonary,Pulmonary Cancers,Pulmonary Neoplasm
D009361	Neoplasm Invasiveness	Ability of neoplasms to infiltrate and actively destroy surrounding tissue.	Invasiveness, Neoplasm,Neoplasm Invasion,Invasion, Neoplasm
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
D004305	Dose-Response Relationship, Drug	The relationship between the dose of an administered drug and the response of the organism to the drug.	Dose Response Relationship, Drug,Dose-Response Relationships, Drug,Drug Dose-Response Relationship,Drug Dose-Response Relationships,Relationship, Drug Dose-Response,Relationships, Drug Dose-Response
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012333	RNA, Messenger	RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.	Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D014407	Tumor Cells, Cultured	Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.	Cultured Tumor Cells,Neoplastic Cells, Cultured,Cultured Neoplastic Cells,Cell, Cultured Neoplastic,Cell, Cultured Tumor,Cells, Cultured Neoplastic,Cells, Cultured Tumor,Cultured Neoplastic Cell,Cultured Tumor Cell,Neoplastic Cell, Cultured,Tumor Cell, Cultured
D014568	Urokinase-Type Plasminogen Activator	A proteolytic enzyme that converts PLASMINOGEN to FIBRINOLYSIN where the preferential cleavage is between ARGININE and VALINE. It was isolated originally from human URINE, but is found in most tissues of most VERTEBRATES.	Plasminogen Activator, Urokinase-Type,U-Plasminogen Activator,Urinary Plasminogen Activator,Urokinase,Abbokinase,Kidney Plasminogen Activator,Renokinase,Single-Chain Urokinase-Type Plasminogen Activator,U-PA,Single Chain Urokinase Type Plasminogen Activator,U Plasminogen Activator,Urokinase Type Plasminogen Activator
D015849	Plasminogen Inactivators	Important modulators of the activity of plasminogen activators. The inhibitors belong to the serpin family of proteins and inhibit both the tissue-type and urokinase-type plasminogen activators.	Plasminogen Activator Inhibitor,Plasminogen Activator Inhibitors,Endothelial Plasminogen Activator Inhibitors,Placental Plasminogen Activator Inhibitors,Plasminogen Activator Inhibitors, Endothelial,Plasminogen Activator Inhibitors, Placental,Activator Inhibitor, Plasminogen,Inactivators, Plasminogen,Inhibitor, Plasminogen Activator,Inhibitors, Plasminogen Activator
D016133	Polymerase Chain Reaction	In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.	Anchored PCR,Inverse PCR,Nested PCR,PCR,Anchored Polymerase Chain Reaction,Inverse Polymerase Chain Reaction,Nested Polymerase Chain Reaction,PCR, Anchored,PCR, Inverse,PCR, Nested,Polymerase Chain Reactions,Reaction, Polymerase Chain,Reactions, Polymerase Chain