Immunological Studies on the Sex-Dependent Prealbumin in Mouse Urine and on Its Occurrence in the Serum

Rümke, P; Thung, P.J.

doi:10.1530/acta.0.0470156

Cited by 52 publications

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“…The mouse excretes some serum proteins and a major urinary protein isolated by Bao Linh et al [l], was found to be of renal origin. Later, Finlayson et al [2] showed hepatic synthesis of this last protein, this finding being in agreement with the results of Rumke and Thung [3] who found an immuno precipitation reaction of mouse serum treated with an antiserum against mouse urinary proteins.…”

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Isolation and Properties of a Mouse Serum Prealbumin Excreted in Urine

Reuter

Hamoir

Marchand

et al. 1968

European Journal of Biochemistry

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A method is described for the isolation ofthe fastest preal bumin fractionPA, from mouse serum. This fraction appears to behave identically to the urinary prealbumin fraction in electroMolecular weight is determined by diffusion and sedimentation as well as by sedimentation-The apparent lower molecular weight of serum prealbumin is due to its contamination by phoretic migration, strain and sex dependency and in immunological reactions. diffusion equilibrium.polysaccharides extracted from starch gel in the course of its isolation.Small laboratory rodents such as rats and mice are known to present an unusually high proteinuria. The mouse excretes some serum proteins and a major urinary protein isolated by Bao Linh et al. [l], was found to be of renal origin. Later, Finlayson et al. [2] showed hepatic synthesis of this last protein, this finding being in agreement with the results of Rumke and Thung [3] who found an immuno precipitation reaction of mouse serum treated with an antiserum against mouse urinary proteins. At pH 5.5 Finlayson et al. [4]found a separation of the major urinary protein into three peaks and made a phenotypic classification of mice on the basis of relative amounts of these components.In a previous publication [5] we have shown that urinary proteins of mice a t pH 8.6 migrate in starch gel almost entirely in the prealbumin zone as a single band and in agar as two bands I and 11. Moreover, 3 -4 bands are observed by agar electrophoresis in certain strains of mice. The fastest of the serum prealbumins observed by starch gel electrophoresis a t pH 8.6 called PA, has the same mobility as the urinary proteins and a considerable increase of this fraction in serum is observed after nephrectomy. Nevertheless, no immunochemical reaction is observed in the prealbumin zone after immunoelectrophoresis against antiurine rabbit serum.In the present work it will be shown that a positive result can be obtained with preparations having a higher prealbumin content. An original method will be described to isolate the component PA, from serum and urine. The properties of the preparations will be compared in order to show the identity of these fractions. MATERlAL AND METHODS Serum and Urine CollectionBlood was collected after decapitation of male mice from the BALB/cf and C5'bl/Rij strains. After 16'coagulation the serum was separated by centrifugation for 10 min a t 12,000 xg and stored a t -12". Usually 400 ml of serum, obtained by killing 800 mice, was collected for a preparation. Urine was collected in tubes after a slight massage of the bladder region. Isolation of Prealburnin from SerumThe fractionation was carried out a t 2-4". To 400 rnl of serum were added 30 g of sodium chloride and then dropwise one volume of 5"/, phenol. After centrifugation for 10min a t 31,COOxg the supernatant was collected and dialysed for 48 h against distilled water, then concentrated by freeze-drying to a volume of 2 ml and submitted to preparative starch gel electrophoresis.After migration under the conditions described for ana...

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confidence: 80%

Isolation and Properties of a Mouse Serum Prealbumin Excreted in Urine

Reuter

Hamoir

Marchand

et al. 1968

European Journal of Biochemistry

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“…Examination of 27 family 2 males which spanned four generations that were all null type indicated that family 2 is breeding true for the null phenotype. The total quantity of MUP excreted by MUP-null unplanned comparisons among pairs of means performed on log-transformed data (29).…”

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Genes that modify expression of major urinary proteins in mice.

Duncan¹,

Matthai²,

Hüppi³

et al. 1988

Mol. Cell. Biol.

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A survey of major urinary proteins (MUPs) from eight BALB/c mouse substrains by isoelectric focusing identified a common pattern with about 10 protein bands in males. One substrain, BALB/cJPt, differed The major urinary proteins (MUPs) of the mouse are a group of 19,000-molecular-weight, structurally and antigenically related proteins with isoelectric points (pls) in the range of pH 4.2 to 4.7. MUPs are synthesized predominantly in the liver but also in salivary, mammary, and other secretary glands. The MUPs produced in the liver are secreted into the plasma and excreted through the kidneys into the urine (9). Normal males excrete 5 to 20 times as much MUP as females. Gonadectomy reduces the quantity of MUP excreted by males to the female level (10). Administration of testosterone induced females and castrated males to excrete levels of MUP characteristic of normal males, indicating the regulatory role of this hormone.A genetic locus originally designated Mup-a (now called

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“…Sex-dependent proteins are also known to be present in the urine of male mice (Riimke & Thung, 1964;Reuter, Kennes, Leonard & Sassen, 1968). In mice these proteins, with an average molecular weight of 17 800 (Finlayson & Baumann, 1958), are probably synthesized in the liver (Finlayson, Asofsky, Potter & Runner, 1965) and are associated with a pheromonal activity (Vandenbergh, Whitsett & Lombardi, 1975;Lombardi, Vandenbergh & Whitsett, 1976).…”

Section: Sex-dependent Protein Excretionmentioning

confidence: 99%

Proteinuria in rats in relation to age-dependent renal changes

et al. 1980

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Wiechert-A llee 9, 3000 Hannover 6I, and 3Zentralinstitut fiir Versuchstiere, Let/ow-Vorbeck-A llee 57, 3000Hannover 91, Federal Republic of Germany 95 Summary 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.

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Immunological Studies on the Sex-Dependent Prealbumin in Mouse Urine and on Its Occurrence in the Serum

Cited by 52 publications

References 0 publications

Isolation and Properties of a Mouse Serum Prealbumin Excreted in Urine

Isolation and Properties of a Mouse Serum Prealbumin Excreted in Urine

Genes that modify expression of major urinary proteins in mice.

Proteinuria in rats in relation to age-dependent renal changes

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