ADAMTS13 activity is decreased in a septic porcine model

2011 ◽  
Vol 105 (01) ◽  
pp. 131-137 ◽  
Author(s):  
Clemens Bockmeyer ◽  
Philipp Reuken ◽  
Tim Simon ◽  
Ulrich Budde ◽  
Wolfgang Lösche ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Renal Failure ◽  
High Molecular Weight ◽  
Porcine Model ◽  
Haemorrhagic Shock ◽  
Renal Tissue ◽  
Tubular Damage ◽  
Adamts13 Activity ◽  
Human Sepsis ◽  
Sepsis Induction

SummaryDuring sepsis, the balance between abundantly secreted von Wille-brand factor (VWF) and the activity of its size regulating protease ADAMTS13 is assumed to be involved in coagulation abnormalities. We aimed to establish a porcine model with haemorrhagic shock with consecutive sepsis and hypothesised that a decreased ADAMTS13-activity as well as an altered VWF multimer pattern is associated with renal failure. Animals (n=21) were subjected to haemorrhagic shock. After volume replacement, intraperitoneal Escherichia coli sepsis was induced. Blood samples were drawn at baseline, after haemorrhage and sepsis induction. Directly postmortem we examined renal tissue by JONES-silver, CD61, VWF and fibrin staining for characterisation of thrombi. Renal failure was analysed by scoring PAS-stained sections for acute tubular damage. Glomerular microthrombi were observed in six of 21 septic animals. Porcine ADAMTS13 activity declined significantly during sepsis, accompanied by a drop-off in platelet count. At 12 hours after sepsis induction, ADAMTS13 activity was significantly diminished compared to sham controls, and an elevated acute tubular damage score was associated with an increased proportion of high-molecular-weight VWF multimers. Compared to baseline the proportion of high-molecular-weight VWF multimers increased significantly in septic animals. Similar to human sepsis, diminished ADAMTS13 activity was observed in a septic porcine model associated with a shift to rather thrombogenic VWF multimers and deposition of microthrombi. Therefore, this porcine model seems to be appropriate for performing functional and therapeutic studies in sepsis-associated ADAMTS13 deficiency.

Glomerular Permeability to High Molecular Weight Dextrans in Acute Ischaemic Renal Failure and Postural Proteinuria

1970 ◽  
Vol 38 (1) ◽  
pp. 93-99 ◽  
Author(s):  
Pamela R. MacLean ◽  
J. J. B. Petrie ◽  
J. S. Robson
Keyword(s):  
Molecular Weight ◽  
Renal Failure ◽  
High Molecular Weight ◽  
Plasma Protein ◽  
Healthy Subjects ◽  
Plasma Proteins ◽  
Normal Subjects ◽  
Glomerular Permeability ◽  
Molecular Weight Range ◽  
Postural Proteinuria

1. Renal permeability to dextran of a molecular weight range approximating to that of the plasma proteins has been studied in six patients with acute ischaemic renal failure, four patients with postural proteinuria and six healthy subjects. 2. Results are expressed in terms of dextran selectivity indices which relate the clearance of dextran to its molecular weight. Indices of dextran selectivity were found to be high in acute ischaemic renal failure, postural proteinuria and in normal subjects. Comparable indices of plasma protein selectivity in these groups were low. 3. It is suggested that in postural proteinuria and acute ischaemic renal failure the proteinuria is not glomerular in origin, and that in these conditions macromolecules are filtered quite normally and urinary protein arises from a post glomerular source characterized by a lack of selectivity.

Increase in Renal and Urinary Low and High Molecular Weight Kininogens during Chromate-Induced Acute Renal Failure in the Rat: Evidence for Renal Kininogen Production

Nephron ◽  
1993 ◽  
Vol 65 (4) ◽  
pp. 612-618 ◽  
Author(s):  
Guy Bompart ◽  
Allain Collé ◽  
Marina Lemos Dos Reiss ◽  
Christiane Pécher ◽  
Albert Adam ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Renal Failure ◽  
Acute Renal Failure ◽  
High Molecular Weight

scholarly journals Detection of Na+ Transporter Proteins in Urine

2000 ◽  
Vol 11 (11) ◽  
pp. 2128-2132
Author(s):  
J. ANDREW McKEE ◽  
SHAILESH KUMAR ◽  
CAROLYN A. ECELBARGER ◽  
PATRICIA FERNÁNDEZ-LLAMA ◽  
JAMES TERRIS ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Polyclonal Antibodies ◽  
Collecting Duct ◽  
Water Channel ◽  
Kidney Tissue ◽  
Renal Tissue ◽  
Thick Ascending Limb ◽  
Aquaporin 2 ◽  
Nephron Segment

Abstract. Previous studies have established that the vasopressin-regulated water channel of the collecting duct, aquaporin-2, is excreted in the urine, providing a means for assessment of regulation and dysregulation of aquaporin-2 in humans. This article addresses the hypothesis that membrane transporters from upstream nephron segments are normally detectable in urine. The experiments employed rabbit polyclonal antibodies against the major Na transporters of the proximal tubule (the type 3 Na-H exchanger [NHE3]), the thick ascending limb of Henle's loop (the bumetanide-sensitive Na-K-2Cl cotransporter [NKCC2]), and the distal convoluted tubule (the thiazide-sensitive Na-Cl cotransporter [NCC]) in immunoblotting experiments. All three of these transporters were readily detectable as high molecular weight complexes present in lowdensity membrane fractions from urine of normal rats. Cross linking studies of NHE3, NKCC2, and NCC revealed that high molecular weight complexes are normally present in renal tissue. The molecular weights of the complexes in urine matched those of the cross-linked complexes in native kidney tissue. The presence in urine of integral membrane proteins representative of each nephron segment raises the possibility that limited or comprehensive proteomic analysis of urine samples may be useful in clinical settings.

Microtubule motors and other maps

1990 ◽  
Vol 48 (3) ◽  
pp. 1-1
Author(s):  
Richard B. Vallee
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cytoplasmic Dynein ◽  
Organelle Transport ◽  
Structural Components ◽  
Microtubule Associated Proteins ◽  
Microtubule Motors ◽  
Associated Proteins ◽  
The Subject ◽  
Intracellular Motility

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.

877: The Effect of Arterial Versus Arteriovenous Clamping on Renal Tissue Oxygenation in a Porcine Model

2006 ◽  
Vol 175 (4S) ◽  
pp. 283-284
Author(s):  
Luke M. Fazio ◽  
Alexandra E. Perks ◽  
Brian D.M. Blew ◽  
Greg T. Hare ◽  
David Mazer ◽  
...  
Keyword(s):  
Tissue Oxygenation ◽  
Porcine Model ◽  
Renal Tissue

Studies on the Functionality of Newly Synthesized Fibrinogen after Treatment of Acute Myocardial Infarction with Streptokinase, Increase in the Rate of Fibrinopeptide Release

1993 ◽  
Vol 70 (06) ◽  
pp. 0978-0983 ◽  
Author(s):  
Edelmiro Regano ◽  
Virtudes Vila ◽  
Justo Aznar ◽  
Victoria Lacueva ◽  
Vicenta Martinez ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Molecular Weight ◽  
Steady State ◽  
High Molecular Weight ◽  
Coronary Arteries ◽  
Risk Index ◽  
Weight Fraction ◽  
High Molecular Weight Fraction ◽  
Fibrinopeptide A

SummaryIn 15 patients with acute myocardial infarction who received 1,500,000 U of streptokinase, the gradual appearance of newly synthesized fibrinogen and the fibrinopeptide release during the first 35 h after SK treatment were evaluated. At 5 h the fibrinogen circulating in plasma was observed as the high molecular weight fraction (HMW-Fg). The concentration of HMW-Fg increased continuously, and at 20 h reached values higher than those obtained from normal plasma. HMW-Fg represented about 95% of the total fibrinogen during the first 35 h. The degree of phosphorylation of patient fibrinogen increased from 30% before treatment to 65% during the first 5 h, and then slowly declined to 50% at 35 h.The early rates of fibrinopeptide A (FPA) and phosphorylated fibrinopeptide A (FPAp) release are higher in patient fibrinogen than in isolated normal HMW-Fg and normal fibrinogen after thrombin addition. The early rate of fibrinopeptide B (FPB) release is the same for the three fibrinogen groups. However, the late rate of FPB release is higher in patient fibrinogen than in normal HMW-Fg and normal fibrinogen. Therefore, the newly synthesized fibrinogen clots faster than fibrinogen in the normal steady state.In two of the 15 patients who had occluded coronary arteries after SK treatment the HMW-Fg and FPAp levels increased as compared with the 13 patients who had patent coronary arteries.These results provide some support for the idea that an increased synthesis of fibrinogen in circulation may result in a procoagulant tendency. If this is so, the HMW-Fg and FPAp content may serve as a risk index for thrombosis.

The Effect of Dextran of Various Molecular Weight on the Coagulation in Dogs

1961 ◽  
Vol 06 (01) ◽  
pp. 015-024 ◽  
Author(s):  
Sven Erik Bergentz ◽  
Oddvar Eiken ◽  
Inga Marie Nilsson
Keyword(s):  
Molecular Weight ◽  
Body Weight ◽  
High Molecular Weight ◽  
Bleeding Time ◽  
Factor Vii ◽  
Low Molecular Weight ◽  
Factor V ◽  
Coagulation Mechanism ◽  
Coagulation Defects

Summary1. Infusions of low molecular weight dextran (Mw = 42 000) to dogs in doses of 1—1.5 g per kg body weight did not produce any significant changes in the coagulation mechanism.2. Infusions of high molecular weight dextran (Mw = 1 000 000) to dogs in doses of 1—1.5 g per kg body weight produced severe defects in the coagulation mechanism, namely prolongation of bleeding time and coagulation time, thrombocytopenia, pathological prothrombin consumption, decrease of fibrinogen, prothrombin and factor VII, factor V and AHG.3. Heparin treatment of the dogs was found to prevent the decrease of fibrinogen, prothrombin and factor VII, and factor V otherwise occurring after injection of high molecular weight dextran. Thrombocytopenia was not prevented.4. In in vitro experiments an interaction between fibrinogen and dextran of high and low molecular weight was found to take place in systems comprising pure fibrinogen. No such interaction occurred in the presence of plasma.5. It is concluded that the coagulation defects induced by infusions of high molecular weight dextran are due to intravascular coagulation.

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