scholarly journals Proteinuria inducing tubulointerstitial damage

2003 ◽  
Vol 56 (7-8) ◽  
pp. 351-354 ◽  
Author(s):  
Biljana Stojimirovic ◽  
Dejan Petrovic
Keyword(s):  
Molecular Weight ◽  
Plasma Proteins ◽  
Renal Scarring ◽  
Basal Membrane ◽  
Glomerular Permeability ◽  
Complement Components ◽  
Endothelin 1 ◽  
Monocyte Chemoattractant ◽  
Matrix Deposition ◽  
Glomerular Basal Membrane

Introduction Glomerular basal membrane represents a mechanical and electric barrier for plasma proteins. In physiological conditions only plasma proteins of low molecular weight are completely filtered through basal membrane. Due to damages of glomerular basal membrane there is an increase in filtration of plasma proteins of moderate and high molecular weight. Proteinuria In regard to its etiology proteinuria can be prerenal, renal and postrenal. By analyzing albumin, 1-microglobulin, immunoglobulin G and 2-macroglobulin, together with total protein in urine, it is possible to detect and differentiate causes of prerenal, glomerular, tubular and postrenal proteinuria. Abnormal glomerular permeability to macromolecules results in excessive protein delivery and reabsorption in proximal tubules. Excessive reabsorption in turn may cause congestion of intracellular endocytic and biosynthetic compartments leading to NFkB-dependent and -independent gene upregulation. Among those genes, monocyte chemoattractant protein-1 (MCP-1), cytokines, osteopontin and endothelin stimulate processes of interstitial inflammation and fibroblast proliferation and are ultimately responsible for enhanced extracellular matrix deposition and renal scarring. Human tubular cells exposed to albumin and HDL increase production of endothelin-1. Endothelin-1 affects microcirculation and fibroblasts and is a monocyte chemoattractant. Specific proteins that are cytotoxic are transferrin/iron, low-density lipoprotein, and complement components, all of which appear in urine in proteinuric states. Adequate and early diagnosis and differentiation of proteinuria are of immense therapeutic importance.

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.

scholarly journals Clinical importance of proteinuria in diagnostic strategy for kidney diseases

2002 ◽  
Vol 21 (3) ◽  
pp. 291-295 ◽  
Author(s):  
Dejan Petrovic ◽  
Radmila Obrenovic ◽  
Nada Majkic-Singh ◽  
Mileta Poskurica ◽  
Biljana Stojimirovic
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Immunoglobulin G ◽  
Total Protein ◽  
Plasma Proteins ◽  
Kidney Diseases ◽  
Clinical Importance ◽  
Basal Membrane ◽  
Diagnostic Strategy ◽  
Physiological Conditions

Basal glomerular membrane represents mechanical and electrical obstacle for passing of plasma proteins. In physiological conditions only plasma proteins of low molecule weight are completely filtered through basal membrane. Due to damages of basal glomerular membrane there is increase in filtration of plasma protein of middle and high molecular weight. Depending on etiology of proteinuria it can be prerenal, renal and postrenal. By analyzing albumin a1-microglobulin, immunoglobulin G and a2-macroglobulin, together with total protein in urine, it is possible to detect and differentiate causes of prerenal, glomerular, tubular and postrenal proteinuria. The adequate and early differentiation of proteinuria is of an immense diagnostic and therapeutic importance.

Soluble Fibrin Complexes and Fibrinogen Heterogeneity in Diabetes mellitus

1980 ◽  
Vol 44 (03) ◽  
pp. 130-134 ◽  
Author(s):  
E B Tsianos ◽  
N E Stathakis
Keyword(s):  
Diabetes Mellitus ◽  
Molecular Weight ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Lower Molecular Weight ◽  
Polyacrylamide Gels ◽  
Soluble Fibrin ◽  
Α2 Macroglobulin ◽  
Patients With Diabetes

SummaryThe presence of soluble fibrin complexes (SFC) measured by gel filtration of plasma on 4% agarose columns, fibrinogen heterogeneity on 3.5% SDS-polyacrylamide gels and the concentrations of several plasma proteins were evaluated in 39 patients with diabetes mellitus (DM) and 19 matched control subjects. A small but significant increase of SFC was found in DM (p<0.01). On individual basis 51.2% of the patients had increased SFC (>M + 2 SD of the controls). Polyacrylamide gel electrophoresis of the SFC showed no evidence of cross-linking or proteolysis. Plasma clots formed in the presence of EDTA and trasylol were analysed in SDS-polyacrylamide gels in a normal and two lower molecular weight fibrin bands (band I, II, III). The percentage of band I fibrinogen was in diabetics (65.3 ± 4.7%) lower than that of the controls (71.8 ± 4.5%) (p < 0.01). Fibrinogen levels, antithrombin III, α1-antitrypsin, α2-macroglobulin and plasminogen were significantly increased in DM. We suggest that in DM there is an enhancement of intravascular fibrin formation and accelerated fibrinogen degradation to lower molecular weight forms.

Comparison of the Non-Specific Binding of Unfractionated Heparin and Low Molecular Weight Heparin (Enoxaparin) to Plasma Proteins

1993 ◽  
Vol 70 (04) ◽  
pp. 625-630 ◽  
Author(s):  
Edward Young ◽  
Benilde Cosmi ◽  
Jeffrey Weitz ◽  
Jack Hirsh
Keyword(s):  
Molecular Weight ◽  
Unfractionated Heparin ◽  
Plasma Proteins ◽  
Low Molecular Weight Heparin ◽  
Specific Binding ◽  
Anticoagulant Activity ◽  
Factor Xa ◽  
Low Molecular Weight ◽  
Heparin Binding ◽  
Fixed Amount

SummaryThe non-specific binding of anticoagulantly-active heparin to plasma proteins may influence its anticoagulant effect. We used low affinity heparin (LAH) essentially devoid of anti-factor Xa activity to investigate the extent and possible mechanism of this non-specific binding. The addition of excess LAH to platelet-poor plasma containing a fixed amount of unfractionated heparin doubled the anti-factor Xa activity presumably because it displaces anticoagulantly-active heparin from plasma proteins. Although dextran sulfates of varying molecular weights also increased the anti-factor Xa activity, less sulfated heparin-like polysaccharides had no effect. These findings suggest that the ability to displace active heparin from plasma protein binding sites is related to charge and may be independent of molecular size. In contrast to its effect in plasma containing unfractionated heparin, there was little augmentation in anti-factor Xa activity when LAH was added to plasma containing low molecular weight heparin (LMWH), indicating that LMWH binds less to plasma proteins than unfractionated heparin. This concept is supported by studies comparing the anticoagulant activity of unfractionated heparin and LMWH in plasma with that in buffer containing antithrombin III. The anti-factor Xa activity of unfractionated heparin was 2-fold less in plasma than in the purified system. In contrast, LMWH had identical anti-factor Xa activity in both plasma and buffer, respectively. These findings may be clinically relevant because the recovered anti-factor Xa activity of unfractionated heparin was 33% lower in plasma from patients with suspected venous thrombosis than in plasma from healthy volunteers. The reduced heparin recovery in patient plasma reflects increased heparin binding to plasma proteins because the addition of LAH augmented the anti-factor Xa activity. In contrast to unfractionated heparin, there was complete recovery of LMWH added to patient plasma and little increase of anti-factor Xa activity after the addition of LAH. These findings may explain why LMWH gives a more predictable dose response than unfractionated heparin.

Low Molecular Weight Heparin Therapy: Is Monitoring Needed?

1994 ◽  
Vol 72 (03) ◽  
pp. 330-334 ◽  
Author(s):  
B Boneu
Keyword(s):  
Molecular Weight ◽  
Clinical Trials ◽  
Plasma Proteins ◽  
Bleeding Risk ◽  
Heparin Therapy ◽  
Low Molecular Weight ◽  
Vein Thrombosis ◽  
Meta Analyses ◽  
Deep Vein ◽  
Initial Check

SummaryRecent meta-analyses indicate that low molecular weight heparins (LMWH) are more effective than unfractionated heparin (UH) in preventing and treating deep vein thrombosis. This article presents the arguments for and against the need for laboratory monitoring. At the present time, the only tests currently available for monitoring LMWH therapy are those which measure the anti Xa activity in the plasma. Due to lower binding to plasma proteins and to cell surfaces,the plasma anti Xa activity generated by a given dose of LMWH is more predictable than for UH.Some clinical trials suggest that LMWH delivered at the recommended dose expose the patient to less bleeding risk than UH. Several . meta-analyses indicate comparable risk while any overdose unaccept-ably increases the haemorrhagic risk. The lowest dose of LMWH still effective in treating established DVT is presently unknown; some reports indicate that inadequate doses of LMWH are associated with a lack of efficacy for prevention. An overview of the published clinical trials indicates that the LMWH dose has never been monitored for prevention of DVT. In the treatment of established DVT, several trials have been performed without any monitoring, while in others the dose was adapted to target a given anti Xa activity. These considerations suggest that in prevention of DVT, monitoring the dose is not required. In the treatment of established DVT, considering the haemorrhagic risk of LMWH, the risk of undertreating the patient and the absence of large clinical trials comparing the advantages of monitoring the dose or not, it might be useful to check anti Xa activity at least once at the beginning of the treatment but the need for this initial check remains to be established. Because a large proportion of patients will be in the desired range, dose adjustments will be far less frequent than for UH.

Neutralisation of Heparan Sulphate and Low Molecular Weight Heparin by Protamine

1985 ◽  
Vol 53 (01) ◽  
pp. 086-089 ◽  
Author(s):  
A R Hubbard ◽  
C A Jennings
Keyword(s):  
Molecular Weight ◽  
Plasma Proteins ◽  
Low Molecular Weight Heparin ◽  
Heparan Sulphate ◽  
Activated Partial Thromboplastin Time ◽  
Weight Basis ◽  
Low Molecular Weight ◽  
Protamine Sulphate ◽  
At Iii ◽  
Reference Preparation

SummaryThe neutralisation by protamine sulphate (PS) of heparan sulphate (HS), a low molecular weight heparin (LMWH), and a reference preparation of unfractionated heparin (UH), was studied by activated partial thromboplastin time (APTT) and anti-Xa clotting assays. UH was most easily neutralised in the APTT assay by PS (on a weight for weight basis), followed by LMWH and HS. The neutralisation of APTT activity by PS closely followed the loss of activity in the anti-Xa clotting assay, when plasma was used as the source of At III. When the anti-Xa clotting assay was carried out using purified At III in place of plasma, HS and LMWH were neutralised by much lower amounts of PS and resembled UH neutralisation more closely. Resistance of HS anti-Xa activity to PS neutralisation decreased with increasing plasma dilution. The presence of bovine albumin with purified At III concentrate increased the resistance of HS to PS neutralisation. It is concluded that PS binding to UH, HS and LMWH is probably related more to their degree of sulphation than molecular weight and that non-specific interactions between PS and plasma proteins inhibit the binding of PS to HS and LMWH.

scholarly journals Activation of final complement components after kidney transplantation as a marker of delayed graft function severity

2020 ◽  
Author(s):  
Carlos E Arias-Cabrales ◽  
Marta Riera ◽  
María José Pérez-Sáez ◽  
Javier Gimeno ◽  
David Benito ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Graft Function ◽  
Basal Membrane ◽  
Factor H ◽  
Delayed Graft Function ◽  
Control Group ◽  
Complement Factor ◽  
Tubular Epithelial Cells ◽  
Complement Components ◽  
Protocol Biopsies

Abstract Background Ischaemia–reperfusion (I/R) damage is a relevant cause of delayed graft function (DGF). Complement activation is involved in experimental I/R injury, but few data are available from kidney transplant (KT) patients. We studied the dynamics of membrane attack complex (C5b-9) as a soluble fraction (SC5b-9) and the histological deposit pattern of C3b, complement Factor H (FH) and C5b-9 in DGF patients. Methods We evaluated SC5b-9 levels in 59 recipients: 38 with immediate graft function and 21 with DGF. The SC5b-9 was measured at admission for KT and 7 days after KT. DGF-kidney biopsies (n = 12) and a control group of 1-year protocol biopsies without tissue damage (n = 4) were stained for C5b-9, C3b and FH. Results SC5b-9 increased significantly in DGF patients (Day 0: 6621 ± 2202 mAU/L versus Day 7: 9626 ± 4142  mAU/L; P = 0.006), while it remained stable in non-DGF patients. Days 0–7 increase &gt;5% was the better cut-off associated with DGF versus non-DGF patient discrimination (sensitivity = 81%). In addition, SC5b-9 increase was related to DGF duration and worse graft function, and independently associated with DGF occurrence. SC5b-9, C3b and FH stains were observed in tubular epithelial cells basal membrane. DGF-kidney biopsies showed a more frequently high-intensity stain, a higher number of tubules with positive stain and larger perimeter of tubules with positive stains for SC5b-9, C3b and FH than control patients. Conclusions Both SC5b-9 levels and SC5b-9, C3b and FH deposits in tubular epithelial cells basal membrane are highly expressed in patients experiencing DGF. SC5b-9 levels increase could be useful as a marker of DGF severity.

Homocysteinylation score of high-molecular weight plasma proteins

Amino Acids ◽  
2013 ◽  
Vol 46 (4) ◽  
pp. 893-899 ◽  
Author(s):  
Alexandr A. Zhloba ◽  
Tatiana F. Subbotina
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Plasma Proteins

Low molecular weight plasma proteins in the cerebrospinal fluid of children with hematological malignancies

1984 ◽  
Vol 12 (2) ◽  
pp. 131-136 ◽  
Author(s):  
M. B. Duggan ◽  
J. A. Whittaker ◽  
E. H. Cooper ◽  
C. C. Bailey ◽  
E. A. Robinson
Keyword(s):  
Molecular Weight ◽  
Cerebrospinal Fluid ◽  
Plasma Proteins ◽  
Hematological Malignancies ◽  
Low Molecular Weight

scholarly journals Green tea and bilberry protective effect against gentamicin-induced nephrotoxicity in rats

2020 ◽  
Vol 37 (3) ◽  
pp. 261-266
Author(s):  
Milica Veljković ◽  
Dragana Pavlović ◽  
Ivan Ilić ◽  
Dušan Sokolović
Keyword(s):  
Protective Effect ◽  
Green Tea ◽  
Biochemical Analysis ◽  
Histological Analysis ◽  
Basal Membrane ◽  
Bactericidal Effect ◽  
Proximal Tubules ◽  
Glomerular Basal Membrane ◽  
Complete Disruption ◽  
Distal Tubules

The aim of our study was to investigate if green tea and bilberry have protective effect on gentamicin-induced kidney damage, when applied together, and to make a connection between their effects. GM group of rats received only gentamicin, GT group received green tea only, B group received only bilberry, whereas control (C) group received saline only. GT+GM group received green tea together with gentamicin, and B+GM group received bilberry together with gentamicin. Biochemical analysis showed significantly increased urea and creatinine levels in GM group when compared to groups that also received bilberry or green tea. Histological analysis showed complete disruption of glomerular basal membrane as well as basal membranes of both proximal and distal tubules in GM group. These destructive effects were significantly milder and limited only to proximal tubules when bilberry or green tea was applied simultaneously with gentamicin. Both green tea and bilberry protective effect on gentamicin-induced nephrotoxicity is manifested because of their strong antioxidant activity. Since they are strong antioxidants, widely distributed in nature, they can offer available and inexpensive adjuvant therapy in Gram-negative infections, which can relieve gentamicin nephrotoxicity, but will not affect its bactericidal effect.

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