PMID- 8383426
OWN - NLM
STAT- MEDLINE
DCOM- 19930402
LR  - 20171213
IS  - 0002-9513 (Print)
IS  - 0002-9513 (Linking)
VI  - 264
IP  - 2 Pt 1
DP  - 1993 Feb
TI  - Human plasmin induces a receptor-mediated arachidonate release coupled with G 
      proteins in endothelial cells.
PG  - C271-81
AB  - Treatment of cultured bovine carotid artery endothelial cells with 10(-7) M 
      plasmin increased arachidonate release coupled with the increase in prostacyclin 
      production. The stimulatory effect of plasmin on arachidonate release could be 
      divided into the early and late phases according to its calcium dependency and 
      pertussis toxin sensitivity. The early phase of plasmin-induced arachidonate 
      release was a calcium-dependent and pertussis toxin-sensitive response, which was 
      observed within 20 min after plasmin treatment. The late phase was a 
      calcium-independent and pertussis toxin-insensitive response, which was induced 
      gradually from 20 to 60 min. Induction of the early phase of plasmin's effect 
      required both the lysine binding and catalytic sites in plasmin molecule because 
      it was inhibited either by the binding antagonist tranexamic acid or by the 
      serine protease inhibitor aprotinin. Guanosine 5'-O-(2-thiotriphosphate) 
      potentiated the effect of plasmin in permeabilized or nonpermeabilized cells, 
      indicating that the early phase effect was mediated by a pertussis 
      toxin-sensitive guanosine 5'-triphosphate (GTP)-binding protein. The late phase 
      of plasmin's effect was due to the catalytic activity because it was inhibited by 
      aprotinin but not by tranexamic acid. Microplasmin structurally having the 
      catalytic sites induced a similar late phase effect. Plasmin did not elicit the 
      metabolism of phosphatidyl polyphosphoinositides. These studies demonstrate that 
      the activation of phospholipase A2, which results in arachidonate release, in the 
      early phase of plasmin's effect is a receptor-mediation via GTP-binding protein 
      that is not coupled through phospholipase C activation.
FAU - Chang, W C
AU  - Chang WC
AD  - Department of Pharmacology, College of Medicine, National Cheng Kung University, 
      Taiwan.
FAU - Shi, G Y
AU  - Shi GY
FAU - Chow, Y H
AU  - Chow YH
FAU - Chang, L C
AU  - Chang LC
FAU - Hau, J S
AU  - Hau JS
FAU - Lin, M T
AU  - Lin MT
FAU - Jen, C J
AU  - Jen CJ
FAU - Wing, L Y
AU  - Wing LY
FAU - Wu, H L
AU  - Wu HL
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Am J Physiol
JT  - The American journal of physiology
JID - 0370511
RN  - 0 (Calcium Channel Blockers)
RN  - 0 (Phosphatidylinositol 4,5-Diphosphate)
RN  - 0 (Phosphatidylinositols)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Virulence Factors, Bordetella)
RN  - 27YG812J1I (Arachidonic Acid)
RN  - 9012-63-9 (Cholera Toxin)
RN  - DCR9Z582X0 (Epoprostenol)
RN  - EC 2.4.2.31 (Pertussis Toxin)
RN  - EC 3.4.21.7 (Fibrinolysin)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - K3Z4F929H6 (Lysine)
SB  - IM
MH  - Animals
MH  - Arachidonic Acid/*metabolism
MH  - Calcium Channel Blockers/pharmacology
MH  - Catalysis
MH  - Cattle
MH  - Cells, Cultured
MH  - Cholera Toxin/pharmacology
MH  - Endothelium, Vascular/cytology/*metabolism
MH  - Epoprostenol/biosynthesis
MH  - Fibrinolysin/*pharmacology
MH  - GTP-Binding Proteins/*metabolism
MH  - Humans
MH  - Lysine/metabolism
MH  - Pertussis Toxin
MH  - Phosphatidylinositol 4,5-Diphosphate
MH  - Phosphatidylinositols/metabolism
MH  - Receptors, Cell Surface/*physiology
MH  - Virulence Factors, Bordetella/pharmacology
EDAT- 1993/02/01 00:00
MHDA- 1993/02/01 00:01
CRDT- 1993/02/01 00:00
PHST- 1993/02/01 00:00 [pubmed]
PHST- 1993/02/01 00:01 [medline]
PHST- 1993/02/01 00:00 [entrez]
AID - 10.1152/ajpcell.1993.264.2.C271 [doi]
PST - ppublish
SO  - Am J Physiol. 1993 Feb;264(2 Pt 1):C271-81. doi: 10.1152/ajpcell.1993.264.2.C271.