Plasma concentration of protein Z-dependent protease inhibitor and ZPI exon 3 mutations in preeclampsia

Author(s):  
Peng Zhang ◽  
Yu-Chen Li ◽  
Lei Li ◽  
Yong Lu
2013 ◽  
Vol 131 (3) ◽  
pp. e110-e113 ◽  
Author(s):  
Lukasz Bolkun ◽  
Marzenna Galar ◽  
Jaroslaw Piszcz ◽  
Dorota Lemancewicz ◽  
Janusz Kloczko

2012 ◽  
Vol 129 (4) ◽  
pp. e92-e96 ◽  
Author(s):  
Ewa Sierko ◽  
Marek Z. Wojtukiewicz ◽  
Lech Zimnoch ◽  
Krystyna Ostrowska-Cichocka ◽  
Piotr Tokajuk ◽  
...  

2019 ◽  
Vol 1 (12) ◽  
pp. 1060-1064
Author(s):  
Majid Ghazanfari ◽  
Mohammad Ali Jalali Far ◽  
Saeed Shirali ◽  
Zari Tahannejad Asadi

Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 1751-1751
Author(s):  
Xin Han ◽  
Martin H. Nguyen ◽  
Michael Fernandez ◽  
George J. Broze ◽  
Carlos E. Bueso-Ramos

Abstract Protein Z (PZ) is a vitamin K-dependent protein, whereas PZ-dependent protease inhibitor (ZPI) is a member of the serine protease inhibitor superfamily. ZPI rapidly inhibits factor Xa in the presence of PZ, calcium, and phospholipids and inhibits factor XIa in a PZ-independent fashion (Blood2000; 96:3049–3055). PZ circulates as a complex with ZPI in plasma and deletion of either the PZ or the ZPI gene is associated with the prothrombotic phenotype in mice. In addition, W303X or R67X nonsense mutations in the ZPI gene are reportedly associated with deep venous thrombosis in certain human populations. Western blot analysis of platelets stimulated with thrombin (0–200 mU/mL) showed they contained and released ZPI (approximately 200 ng/109 platelets) with the same molecular weight as plasma ZPI (72 kDa). The majority of the ZPI was released within 1 min. by 25 mU/mL thrombin. PZ was not detected in platelets by western blot analysis. Immunohistochemical staining using a monoclonal anti-ZPI antibody demonstrated a cytoplasmic fine granular staining pattern in maturing megakaryocytes in bone marrow aspirates and in circulating platelets, suggesting that ZPI may be stored in alpha granules. ZPI mRNA, however, was not detected by reverse transcriptase polymerase chain reaction (RT-PCR) in platelets or bone marrow aspirates, but was detected in human liver cDNA. RT-PCR for platelet factor 4 and glyceraldehyde 3-phosphate dehydrogenase mRNA showed amplified products with expected sizes. In conclusion, thrombin-releasable ZPI, but not PZ, is present in platelets and is most likely derived from the uptake of ZPI from plasma. ZPI released from activated platelets may play a role in the regulation of local coagulation at a site of injury.


AIDS ◽  
2003 ◽  
Vol 17 (7) ◽  
pp. 1096-1099 ◽  
Author(s):  
Ségolène Duran ◽  
Gilles Peytavin ◽  
Patrizia Carrieri ◽  
François Raffi ◽  
Jean-Luc Ecobichon ◽  
...  

2009 ◽  
Vol 7 (5) ◽  
pp. 731-735 ◽  
Author(s):  
F. SOFI ◽  
F. CESARI ◽  
Y. TU ◽  
G. PRATESI ◽  
R. PULLI ◽  
...  

1998 ◽  
Vol 95 (16) ◽  
pp. 9250-9255 ◽  
Author(s):  
Xin Han ◽  
Ryan Fiehler ◽  
George J. Broze

Human protein Z (PZ) is a 62,000-Mr, vitamin K-dependent plasma protein whose structure is similar to coagulation factors VII, IX, X, protein C, and protein S, but whose function is not known. The procoagulant activity of factor Xa in a one-stage plasma coagulation assay is reduced when factor Xa is first incubated with PZ. This apparent inhibitory effect is time dependent, requires the presence of calcium ions and procoagulant phospholipids (rabbit brain cephalin), and appears predominantly related to the incubation period of PZ with cephalin. In serum the initial rate of inhibition of factor Xa with calcium ions and cephalin also is enhanced in the presence PZ. A PZ-dependent protease inhibitor (ZPI) has been isolated from plasma. ZPI is a 72,000-Mrsingle-chain protein with an N-terminal amino acid sequence of LAPSPQSPEXXA (X = indeterminate) and an estimated concentration in citrate-treated plasma of 1.0–1.6 μg/ml. In systems using purified components, the factor Xa inhibition produced by ZPI is rapid (>95% within 1 min by coagulation assay) and requires the presence of PZ, calcium ions, and cephalin. The inhibitory process appears to involve the formation of a factor Xa–PZ–ZPI complex at the phospholipid surface.


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