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.

scholarly journals Proteinuria: The diagnostic strategy based on urine proteins differentiation

2004 ◽  
Vol 132 (3-4) ◽  
pp. 127-132 ◽  
Author(s):  
Biljana Stojimirovic ◽  
Dejan Petrovic
Keyword(s):  
Immunoglobulin G ◽  
Total Protein ◽  
Plasma Proteins ◽  
Heparan Sulphate ◽  
Diagnostic Strategy ◽  
Cylindrical Pores ◽  
Urine Proteins ◽  
Mechanical Barrier ◽  
Interior Side ◽  
Serum And Urine

Basal glomerular membrane represents mechanical and electrical barrier for passing of the plasma proteins. Mechanical barrier is composed of cylindrical pores and filtration fissure, and negative layer charge in exterior and interior side of basal glomerular membrane, made of heparan sulphate and sialoglicoproteine, provides certain electrical barrier. Diagnostic strategy based on different serum and urine proteins enables the differentiation of various types of proteinuria. Depending on etiology of proteinuria it can be prerenal, renal and postrenal. By analyzing albumin, armicroglobulin, immunoglobulin G and armacroglobulin, together with total protein in urine, it is possible to detect and differentiate causes of prerenal, renal (glomerular, tubular, glomerulo-tubular) and postrenal proteinuria. The adequate and early differentiation of proteinuria type is of an immense diagnostic and therapeutic importance.

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

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.

High molecular weight Alzheimer's disease amyloid peptide immunoreactivity in human serum and CSF is an immunoglobulin G

1987 ◽  
Vol 145 (1) ◽  
pp. 241-248 ◽  
Author(s):  
William M. Pardridge ◽  
Harry V. Vinters ◽  
Bruce L. Miller ◽  
Wallace W. Tourtellotte ◽  
Jody B. Eisenberg ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Weight ◽  
Human Serum ◽  
High Molecular Weight ◽  
Immunoglobulin G ◽  
Amyloid Peptide

scholarly journals Effect of surfaces on fluid-phase prekallikrein activation

Blood ◽  
1981 ◽  
Vol 57 (3) ◽  
pp. 553-560
Author(s):  
CF Scott ◽  
EP Kirby ◽  
PK Schick ◽  
RW Colman
Keyword(s):  
Molecular Weight ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
High Molecular Weight ◽  
Bovine Serum ◽  
Plasma Proteins ◽  
Fluid Phase ◽  
Factor Xii ◽  
Cold Insoluble Globulin ◽  
Kallikrein Activity

The activation of prekallikrein by factor XII fragments (XIIf), during incubation in plastic tubes was previously noted to be increased by high molecular weight (HMW) kininogen as well as other plasma proteins. In this report, we investigated the mechanism responsible for this increase. Although we confirmed that HMW kininogen, bovine serum albumin, fibrinogen, cold insoluble globulin, and mixed phospholipids apparently increased prekallikrein activation, we found that the product of prekallikrein activation (kallikrein) lost substantial activity in less than 0.5 min after exposure to a variety of fresh surfaces. This loss was partially prevented by the presence of various proteins and phospholipids. Similar protection against inactivation of XIIf, the enzyme in this reaction, was also found. In contrast, no loss of the substrate, prekallikrein, was observed during incubation. The loss of kallikrein activity was found to be proportional to the surface area of the incubation vessel as well as the concentration of kallikrein. Further loss of kallikrein activity could also be prevented by pretreating the vessel with kallikrein. We therefore conclude that various substances apparently affect prekallikrein activation in a purified system by preventing the enzyme and product in the reaction mixture from losing activity due to adsorption to a surface.

Is High-Molecular-Weight-Renin Binding of Renin to the Protease Inhibitors and Lipoproteins?

1978 ◽  
Vol 55 (s4) ◽  
pp. 125s-128s
Author(s):  
K. Poulsen ◽  
A. H. Nielsen ◽  
S. Lykkegaard ◽  
C. Malling ◽  
J. Krøll ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Protease Inhibitors ◽  
Plasma Proteins ◽  
Tertiary Structure ◽  
Limited Proteolysis ◽  
Submaxillary Gland ◽  
Enzymic Activity ◽  
Molecular Weights ◽  
Α2 Macroglobulin

1. Two high-molecular-weight forms of renin (molecular weights 800 000 and 70 000) are present in mouse plasma. 2. The 800 000 form could be activated and converted into the fully active 40 000 form, by acid or limited proteolysis. The 70 000 form was activated without change in molecular weight. 3. In addition to its enzymic activity, renin was measured by a direct radioimmunoassay, which revealed that the current acid treatment of plasma did not activate all the renin present. 4. Renin is stored as fully active 40 000 renin, with a specific enzymic reactivity of 0·4 × 10−3 GU ng−1, in the submaxillary gland of mice. 5. Pure 125I-labelled 40 000 submaxillary renin did not bind to plasma proteins. However, by changing the tertiary structure of renin, it was bound to some of the plasma protease inhibitors; α2-macroglobulin, inter-α-trypsin inhibitor and α2-antithrombin. It was also bound to α1- and β1-lipoprotein, albumin and an unidentified plasma protein. No binding was seen to more than 50 other studied plasma proteins.

scholarly journals Proteinuria in rats in relation to age-dependent renal changes

1980 ◽  
Vol 14 (2) ◽  
pp. 95-101 ◽  
Author(s):  
Jeannette M. Alt ◽  
H. Hackbarth ◽  
F. Deerberg ◽  
H. Stolte
Keyword(s):  
Molecular Weight ◽  
Total Protein ◽  
Plasma Proteins ◽  
Disc Electrophoresis ◽  
Male Rats ◽  
Low Molecular Weight ◽  
Urinary Proteins ◽  
Protein Excretion ◽  
Age Dependent ◽  
Renal Changes

A variety of sex-dependent urinary proteins of low molecular weight, absent in females and in castrated males, can be identified in male rats by disc electrophoresis. In the urine of male rats of age 5·5 months, albumin comprises only 1-2% of the total protein. Albumin excretion increases greatly with age and associated kidney disease. Total protein excretion, however, stays the same or even decreases slightly as the rat ages, due to a loss of low molecular weight, sex-dependent, proteins. These are virtually absent in senescent rats (38 months of age), although total protein excretion rises tenfold in these animals due to high molecular weight plasma proteins passing into the urine; the glomerular filtration rate decreases to 70% of the value measured at 5·5 months of age.

Renin Precursor Synthesis and Renin-Binding Proteins in the Mouse

1979 ◽  
Vol 57 (s5) ◽  
pp. 109s-110s ◽  
Author(s):  
K. Poulsen
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Protease Inhibitors ◽  
Plasma Proteins ◽  
Tertiary Structure ◽  
Submaxillary Gland ◽  
Α2 Macroglobulin ◽  
Precursor Synthesis ◽  
Predominant Form ◽  
Molecular Nature

1. The precursor synthesis of renin, the storage form in the kidney and the submaxillary gland, and the molecular nature of the forms in plasma were studied in the mouse. 2. Renin is synthesized as a precursor (pre-prorenin) with a molecular weight of 50 000. 3. Renin is stored in the submaxillary gland and the kidneys as fully active renin with a molecular weight of 40 000. 4. The predominant form of renin in plasma is the active mol. wt. 40 000 form. High-molecular-weight forms of renin (800 000 and 70 000) are also present in plasma. 5. Pure 125I-labelled mol. wt. 40 000 renin binds, after a change in the tertiary structure, to the plasma protease inhibitors α2-macroglobulin, inter-α-trypsin inhibitor and α2-antithrombin. It binds also to lipoprotein and an unidentified plasma protein. No binding was seen to more than 50 other studied plasma proteins. 6. The high-molecular-weight forms of renin in plasma may be complexes of renin with plasma protease inhibitors and lipoprotein.

Sign in / Sign up

Export Citation Format

Share Document