Histomorphometry and cell kinetics of normal human bladder mucosa in vitro

1987 ◽  
Vol 15 (6) ◽  
Author(s):  
E.A. Reedy ◽  
B.M. Heatfield
2002 ◽  
Vol 31 (06) ◽  
pp. 366 ◽  
Author(s):  
Anna Lavezzi ◽  
Mario Mantovani ◽  
Lorenzo Grillo della Berta ◽  
Luigi Matturri

Blood ◽  
2010 ◽  
Vol 116 (21) ◽  
pp. 1415-1415
Author(s):  
Hanspeter Rottensteiner ◽  
Katalin Varadi ◽  
Susanne Vejda ◽  
Hartmut J. Ehrlich ◽  
Friedrich Scheiflinger ◽  
...  

Abstract Abstract 1415 A recombinant human CHO-expressed von Willebrand factor (rVWF) consisting of ultra-high molecular weight (UHMW) multimers resembles the VWF stored in Weibel-Palade bodies of endothelial cells. Once secreted into plasma, UHMW multimers are rapidly cleaved by ADAMTS13 and are usually missing in plasma-derived VWF (pdVWF). Here we analyzed in vitro whether the kinetics of cleavage of rVWF by ADAMTS13 is similar to that of pdVWF. The kinetics of ADAMTS13-mediated proteolysis of rVWF were explored under denaturing conditions (1.5 M urea) or under shear stress so as to expose the ADAMTS13 cleavage site of VWF. Multiple assays showed that rVWF was efficiently cleaved by ADAMTS13. UHMW multimers disappeared within seconds at physiological concentrations of ADAMTS13. Using lower concentrations of ADAMTS13 (10-30 mU/ml, equivalent to 1–3% of normal human plasma), UHMW were cleaved within 30 minutes. The typical satellite bands appeared very early in an ADAMTS13 dose-dependent manner. Virtually the same results were obtained when human plasma was used as a source for ADAMTS13. Although pdVWF differs from rVWF in its multimeric structure, the decrease in activity was similar for rVWF and pdVWF. Finally, the extent of ADAMTS13 cleavage was similar for rVWF and pdVWF when exposed to shear stress using a cone-plate viscometer. Our data clearly indicate that rVWF is a good substrate for ADAMTS13. Ongoing phase 1 studies demonstrated that rVWF is indeed processed by the protease when administered in humans with severe VWD. Disclosures: Rottensteiner: Baxter Innovations GmbH: Employment. Varadi:Baxter Innovations GmbH: Employment. Vejda:Baxter Innovations GmbH: Employment. Ehrlich:Baxter Innovations GmbH: Employment. Scheiflinger:Baxter Innovations GmbH: Employment. Schwarz:Baxter Innovations GmbH: Employment. Turecek:Baxter Innovations GmbH: Employment.


1993 ◽  
Vol 2 (5) ◽  
pp. 387-392 ◽  
Author(s):  
P S Rooney ◽  
P A Clarke ◽  
K-A Gifford ◽  
M H Robinson ◽  
J D Hardcastle ◽  
...  

1991 ◽  
Vol 24 (4) ◽  
pp. 367-374 ◽  
Author(s):  
I. D. Bassukas ◽  
A. Arai ◽  
H. Schell ◽  
O. P. Hornstein

Parasitology ◽  
2001 ◽  
Vol 122 (5) ◽  
pp. 521-529 ◽  
Author(s):  
A. BEE ◽  
F. J. CULLEY ◽  
I. S. ALKHALIFE ◽  
K. B. BODMAN-SMITH ◽  
J. G. RAYNES ◽  
...  

Infective metacyclic promastigote forms ofLeishmania mexicanaare introduced by the bite of sandfly vectors into their human hosts where they transform into the amastigote form. The kinetics of this process was examinedin vitroin response to different combinations of temperature (26 °C or 32 °C), pH (7.2 or 5.5), and exposure to human serum. Little transformation occurred at 26 °C/pH 7.2, intermediate levels at 26 °C/pH 5.5 and 32 °C/ pH 7.2, and the greatest response at 32 °C/pH 5.5. Transformation was stimulated by exposure to normal human serum, but was markedly reduced when serum previously incubated at 56 °C for 1 h was used (complement heat-inactivated). This stimulatory effect was reproduced by exposure to a single purified component of human serum, C-reactive protein (CRP). Binding of CRP to the whole surface ofL. mexicanametacyclic promastigotes, including the flagella, was demonstrated by an indirect fluorescent antibody test. The effect of purified CRP was dose dependent and occurred using normal serum concentrations. The stimulatory effect of whole serum was oblated by CRP depletion and restored by addition of purified CRP. The effects of cAMP analogues indicated that transformation could be mediated via an adenylate cyclase cascade.


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