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Quantitative Immunological Determination of 12 Plasma Proteins Excreted in Human Urine Collected Before and After Exercise

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Quantitative Immunological Determination of 12 Plasma Proteins Excreted in Human Urine Collected Before and After Exercise Quantitative immunological determination of 12 plasma proteins excreted in human urine collected before and after exercise Jacques Poortmans, Roger W. Jeanloz J Clin Invest. 1968;47(2):386-393. https://doi.org/10.1172/JCI105735. Research Article Urine was collected from 6 healthy male adults at rest and from 20 male adults after a marathon race (25 miles). The concentrated urines were quantitatively analyzed, by single radial immunodiffusion, for their content in 12 different plasma proteins: tryptophan-rich prealbumin, albumin, α1-acid glycoprotein, α1-antitrypsin, ceruloplasmin, haptoglobin, Gc- globulin, transferrin, hemopexin, β2-glycoprotein I, γA-globulin, and γG-globulin. Albumin, γA-globulin, and γG-globulin represent the major part of the plasma proteins detected in normal urine excreted by humans at rest (12, 0.5, and 2.5 mg respectively, out of a total excretion of 17.5 mg of plasma proteins per 24 hr). The other plasma proteins were excreted at a lower rate (< 0.4 mg/24 hr). The relative content of tryptophan-rich prealbumin, α1-antitrypsin, Gc-globulin, transferrin, and γG-globulin was lower in normal urine than in normal serum, whereas that of α1-acid glycoprotein, β2-glycoprotein I, and γA-globulin was higher. The ratio of γG-globulin to γA-globulin was 4.9:1. When plotted on a logarithmic scale, no direct relationship between the molecular weight of a protein and the value of its renal clearance could be observed. Strenuous exercise increased (up to 50-fold) the excretion of plasma proteins which represent 82% of the total proteins found in urine, instead of 57% in urine collected from humans at rest. There was particularly a significant rise of tryptophan-rich albumin, albumin, α1-acid glycoprotein, transferrin, γA-globulin, […] Find the latest version: https://jci.me/105735/pdf Quantitative Immunological Determination of 12 Plasma Proteins Excreted in Human Urine Collected before and after Exercise JACQUES POoRTMANS and ROGER W. JFAwoz From the Laboratory of Carbohydrate Research, Departments of Biological Chemistry and Medicine, Harvard Medical School, and the Massachusetts General Hospital, Boston, Massachusetts A B S T R A C r Urine was collected from 6 healthy the excretion of plasma proteins which represent male adults at rest and from 20 male adults after 82% of the total proteins found in urine, instead a marathon race (25 miles). The concentrated of 57%o in urine collected from humans at rest. urines were quantitatively analyzed, by single ra- There was particularly a significant rise of trypto- dial immunodiffusion, for their content in 12 dif- phan-rich albumin, albumin, a1-acid glycoprotein, ferent plasma proteins: tryptophan-rich prealbu- transferrin, yA-globulin, and yG-globulin (0.26, min, albumin, a,-acid glycoprotein, a1-antitrypsin, 127, 11.8, 3.3, 1.2, and 2.0 jug respectively, out of ceruloplasmin, haptoglobin, Gc-globulin, transfer- a total excretion of 167 ug of plasma proteins per rin, hemopexin, f82-glycoprotein I, yA-globulin, min). The ratio of yG-globulin to yA-globulin was and yG-globulin. 16: 1. After exercise, the renal clearance of pro- Albumin, yA-globulin, and yG-globulin repre- teins increased from 2 to 40 times, but, as for the sent the major part of the plasma proteins detected urine of normal subjects at rest, no direct relation- in normal urine excreted by humans at rest (12, ship between molecular weight and renal clearance 0.5, and 2.5 mg respectively, out of a total excre- could be observed. tion of 17.5 mg of plasma proteins per 24 hr). The other plasma proteins were excreted at a INTRODUCTION lower rate (< 0.4 mg/24 hr). The relative con- tent of tryptophan-rich prealbumin, a1-antitrypsin, In earlier studies, the amount of protein excreted Gc-globulin, transferrin, and yG-globulin was in the urine in 24 hr by healthy humans at rest lower in normal urine than in normal serum, was estimated between 30 and 70 mg (1-5), al- whereas that of al-acid glycoprotein, 82-glyco- though values of 100-400 mg have also been protein I, and yA-globulin was higher. The ratio observed (6-8). Poortmans has reported that of yG-globulin to yA-globulin was 4.9:1. When strenuous exercise causes an increase of protein plotted on a logarithmic scale, no direct relation- excretion up to a hundred times the content pres- ship between the molecular weight of a protein ent before exercise (9, 10). and the value of its renal clearance could be Immunological investigations have established observed. the presence of several plasma proteins in normal Strenuous exercise increased (up to 50-fold) urine, collected from individuals both at rest and Dr. Poortmans' present address is Laboratoire de after exercise (9-13). In the latter case, immuno- l'Effort, Universit6 Libre de Bruxelles, 28 Avenue P. precipitation techniques showed an increase in the Heger, Bruxelles 5, Belgium. in the Received for publication 18 July 1967 and in revised number of plasma proteins (9) as well as form 5 October 1967. number of proteins not present in plasma (10). 386 The Journal of Clinical Investigation Volume 47 1968 The quantitative determination of individual The final concentration of protein in the concentrated plasma proteins in normal urine is of major inter- urine was determined with the Lowry method (23). est for an understanding of the mechanism of pro- Proteins of urine collected from healthy humans after strenuous exercise. The urine from 20 individual ath- teinuria itself. An explanation based on the pres- letes was collected within 1 hr after a marathon race ence of proteins in normal urine has been presented (Boston Marathon 1966: 26 miles). Each was treated by Hardwicke and Squire (14). It consists of the in the manner previously described for urine collected glomerular filtration of most of the plasma pro- from humans at rest. teins, associated with a nonselective process of Single radial immunodiffusion technique. Quantita- tive determination of the following proteins in concen- tubular reabsorption. Another mechanism, sug- trated urines was performed according to the original gested by the results obtained in the present work, technique of Mancini et al. (24): tryptophan-rich pre- would also consider a glomerular filtration, but albumin, albumin, a,-acid glycoprotein, a1-antitrypsin, combined with a selective tubular reabsorption and haptoglobin, Gc-globulin, hemopexin, and 2-glycoprotein I. with a Ceruloplasmin, transferrin, 'yA-globulin, and -yG-globu- secretion from the nephron. Little is known, lin were determined with Hyland immunodiffusion plates. however, of the fate of proteins in the kidney. aL-Antitrypsin and hemopexin used as standard were The concept of selective permeability introduced isolated from pooled normal human sera according to by Hardwicke and Squire (14) has been sup- the procedure of Heide and Haupt (25). The following ported by the results of paper electrophoresis antisera were purchased: tryptophan-rich prealbumin (Behringwerke No. 846), a,-acid glycoprotein (Mann (15), of gel filtration (16, 17), and of semiquanti- No. R2648), ai-antitrypsin (Behringwerke No. 882), tative imminunodiffusion (18), but the absolute haptoglobin (Mann No. R1790), Gc-globulin (Behring- value of the content of each individual plasma werke No. 848), #2-glycoprotein I (Behringwerke No. protein in normal urine is not avaiable. Only 845). The human albumin antiserum was prepared by im- albumin has been quantitatively determined in munization of a rabbit for a period of 3 wk. The size of the ring-shaped precipitates was measured human urine (19, 20), with the results being after the plates had been washed and stained according expressed in terms of milligrams of protein ex- to the method of Mancini et al. (24). creted per 24 hr. In the present study, several plasma proteins RESULTS found in the urine collected from healthy humans Urine from normal subjects at rest. The total both after rest, and after exercise, were quantita- amount of protein excreted in urine is about 0.046 tively estimated in order to show whether or not mg/ml or 0.035 mg/min (Table I). The amounts exercise proteinurina is similar to the physiologi- of each of the 12 plasma proteins investigated are cal lproteinuria of subjects at rest. The -results presented in Table II. Whereas 98.5% of the pro- showed that normal physiological proteinuria is teins of plasma have been identified (if the lipo- related only in part to the glomerular filtration proteins and macroglobulins that are not present accor(ling to the molecular weight of the macro- in normal urines are taken into consideration), molecuiles. In addition, not all the results are ex- only 57.1% of the proteins of serum could be iden- plainle(l by the hypothesis of nonselective tubular tified in urine. reabsorption, anal other mechanisms are proposed. The ratios of the content of each individual protein to the total protein content show major METHODS differences between normal urine and normal Proteins of urine collected from healthy humans at serum (Table II). Albumin remains the major rest. Urine samples were collected during 48 hr from 6 component of normal urine, although its relative healthy male adults. None of the samples showed any content is lower than in normal serum. Deter- protein content when examined with the boiling acetic acid test. Sodium merthiolate (0.01 g/100 ml) was added mination with an immunological method showed as a preservative, and the samples were kept overnight the proportion of albumin to globulins to be 1.30: 1 at 40C. Then the urines were filtered to remove the uro- in normal serum, whereas it was 0.67: 1 in normal mucoid fraction, and the protein content of the filtrates urine. The relative content of the following plasma was determined with the Amidoschwartz microtechnique proteins was lower in normal urine than in normal (21).
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