Characterization of protein c inhibitor (PCI)-binding glycosaminoglycans (GAGs) of epithelial kidney tumor cells (TCL-598)

1994 ◽  
Vol 8 ◽  
pp. 63
Author(s):  
U. Priglinger ◽  
M. Geiger ◽  
E. Bielek ◽  
E. Vanvek ◽  
B.R. Binder
Keyword(s):  
Tumor Cells ◽  
Protein C ◽  
Kidney Tumor ◽  
Protein C Inhibitor

Characterization of a cDNA for Rhesus Monkey Protein C Inhibitor – Evidence for N-Terminal Involvement in Heparin Stimulation

1995 ◽  
Vol 74 (04) ◽  
pp. 1079-1087 ◽  
Author(s):  
Klaus-P Radtke ◽  
José A Fernández ◽  
Bruno O Villoutreix ◽  
Judith S Greengard ◽  
John H Griffin
Keyword(s):  
Rhesus Monkey ◽  
Protein C ◽  
Activated Protein C ◽  
Pcr Amplification ◽  
Amino Acid Sequences ◽  
Heparin Binding ◽  
Reactive Center ◽  
Protein C Inhibitor ◽  
Polymerase Chain

SummarycDNAs for protein C inhibitor (PCI) were cloned from human and rhesus monkey 1 liver RNAs by reverse transcription and polymerase chain reaction (PCR) amplification. Sequencing showed that rhesus monkey and human PCI cDNAs were 93% identical. Predicted amino acid sequences differed at 26 of 387 residues. Pour of these differences (T352M, N359S, R362K, L3631) were in the reactive center loop that is important for inhibitory specificity, and two were in the N-terminal helix (M8T, E13K) that is implicated in glycosaminoglycan binding. PCI in human or rhesus monkey plasma showed comparable inhibitory activity towards human activated protein C in the presence of 10 U/ml heparin. However, maximal acceleration of the inhibition of activated protein C required 5-fold lower heparin concentration for rhesus monkey than for human plasma, consistent with the interpretation that the additional positive charge (E13K) in a putative-heparin binding region increased the affinity for heparin.

Purification and characterization of plasma protein C inhibitor

1989 ◽  
Vol 55 (3) ◽  
pp. 369-384 ◽  
Author(s):  
Francisco España ◽  
Mauro Berrettini ◽  
John H. Griffin
Keyword(s):  
Plasma Protein ◽  
Protein C ◽  
Purification And Characterization ◽  
Protein C Inhibitor

Characterization of recombinant human protein C inhibitor expressed in Escherichia coli

2005 ◽  
Vol 1748 (1) ◽  
pp. 57-65 ◽  
Author(s):  
Sophie M. Réhault ◽  
Margareta Zechmeister-Machhart ◽  
Yolanda M. Fortenberry ◽  
Julia Malleier ◽  
Nikki M. Binz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein C ◽  
Human Protein ◽  
Protein C Inhibitor ◽  
Recombinant Human Protein

Activated Protein C−Protein C Inhibitor Complex Formation:  Characterization of a Neoepitope Provides Evidence for Extensive Insertion of the Reactive Center Loop

Biochemistry ◽  
2000 ◽  
Vol 39 (51) ◽  
pp. 15713-15720 ◽  
Author(s):  
Karin Strandberg ◽  
Margareta Kjellberg ◽  
Eva-Maria Erb ◽  
Ulla Persson ◽  
Deane F. Mosher ◽  
...  
Keyword(s):  
Complex Formation ◽  
Protein C ◽  
Activated Protein C ◽  
C Protein ◽  
Inhibitor Complex ◽  
Reactive Center Loop ◽  
Reactive Center ◽  
Protein C Inhibitor

Protein C Inhibitor from Human Plasma: Characterization of Native and Cleaved Inhibitor and Demonstration of Inhibitor Complexes with Plasma Kallikrein

1989 ◽  
Vol 62 (03) ◽  
pp. 885-891 ◽  
Author(s):  
Martin Laurell ◽  
Johan Stenflo
Keyword(s):  
Sequence Analysis ◽  
Human Plasma ◽  
Protein C ◽  
Activated Protein C ◽  
Immunoaffinity Chromatography ◽  
Plasma Kallikrein ◽  
Cleavage Sites ◽  
Protein C Inhibitor ◽  
Secondary Cleavage

SummaryProtein C inhibitor (PCI) was purified from human plasma using immunoaffinity chromatography and heparin Sepharose chromatography, a method that allowed the purification of active and inactive inhibitor. PCI purified from outdated plasma was inactive and either in complex with plasma kallikrein or proteo-lytically degraded. Sequence analysis of cleaved PCI and of complexes between PCI and activated protein C or urokinase identified the previously recognized inhibitor cleavage site Arg354-Ser355. Two additional cleavage sites were observed in the modified inhibitor i.e. Arg357-Leu358 and Arg362-Leu363 which probably represent secondary cleavage of the inhibitor. Furthermore the sequence analysis of the inhibitor, whether purified from fresh or outdated plasma, revealed that it was microheterogeneous in the NH2-terminus as a result of cleavage by a trypsin like enzyme(s).

Further characterization of dextran sulfate as a cofactor of protein C inhibitor

1989 ◽  
Vol 54 (5) ◽  
pp. 499-504 ◽  
Author(s):  
Yoshiaki Kazama ◽  
Takehiko Koide ◽  
Nobuo Sakuragawa
Keyword(s):  
Protein C ◽  
Dextran Sulfate ◽  
Protein C Inhibitor
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