Mouse Proteinuria

Finlayson, J. S.; Baumann, C. A.

doi:10.1152/ajplegacy.1957.192.1.69

Cited by 45 publications

(21 citation statements)

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“…The major urinary proteins (MUPs) of mice were originally described as a group of antigenically related low-molecular-weight acidic proteins synthesized in the liver, secreted into the serum, and ultimately excreted in the urine (14)(15)(16). A homologous protein, a2.-globulin, has been described in rats (24,31,32).…”

mentioning

confidence: 99%

Differential, multihormonal regulation of the mouse major urinary protein gene family in the liver.

Knopf¹,

Gallagher²,

Held³

1983

Mol. Cell. Biol.

125

131

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The hormonal requirements for the regulation of the major urinary protein (MUP) mRNA levels in mouse liver have been examined. Previous experiments have shown that administration of testosterone to female or castrated male mice increases MUP mRNA levels approximately fivefold to normal male levels. We have found that thyroxine and the peptide hormone, growth hormone, each had a pronounced effect on MUP mRNA levels. MUP mRNA was reduced 150-fold in growth-hormone-deficient mutant mice (little). The administration of growth hormone and thyroxine induced MUP mRNA approximately 150-fold, and when administered together, they induced MUP mRNA approximately 1,000-fold. testosterone administration. When administered separately to these mice, growth hormone and thyroxine induced with MUP mRNA approximately 150-fold, and when administered together, they induced MUP mRNA approximately 1,000-fold. Testicular feminized mice, which lack a functional major testosterone receptor protein, can also be induced to male levels by treatment with both growth hormone and thyroxine. In addition, we present evidence which indicates that growth hormone, thyroxine, and testosterone differentially regulate the levels of distinct MUP mRNA species.The major urinary proteins (MUPs) of mice were originally described as a group of antigenically related low-molecular-weight acidic proteins synthesized in the liver, secreted into the serum, and ultimately excreted in the urine (14-16). A homologous protein, a2.-globulin, has been described in rats (24,31,32). More recently, hybridization experiments have shown that the MUPs constitute a multigene family of 20 to 30 genes (7,18). Genetic mapping studies with recombinant inbred mice and mouse-hamster hybrid cell lines indicate that the MUP structural genes are clustered on chromosome 4 (5, 7, 20).Although the liver appears to be the major site of MUP synthesis, recent studies have shown that the MUP gene family is expressed in several secretory tissues of mice (18,34). The tissues expressing MUP mRNA sequences are the liver, the submaxillary gland, the lachrymal gland, and the mammary gland. These studies also indicated that expression of MUP mRNA in each of the tissues is under different developmental and hormonal controls (34).Early studies on the regulation of the MUPs examined the urinary levels of those proteins whose major site of synthesis appears to be the liver (36; this paper). Parfentjer (28) ed that male mice exhibit high levels of proteinuria and that the onset of this proteinuria correlated with the onset of sexual maturity. The role of the major male sex steroid, testosterone, was further indicated by demonstrating that either females or castrated males treated with testosterone attain normal male levels of proteinuria (38). Biochemical examination of these urinary proteins by Finlayson et al. (16) revealed a group of low-molecular-weight acidic proteins which exhibit both strain-and sex-specific electrophoretically distinguishable phenotypes (14, 37). Interestingly, these studies a...

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mentioning

confidence: 99%

Differential, multihormonal regulation of the mouse major urinary protein gene family in the liver.

Knopf¹,

Gallagher²,

Held³

1983

Mol. Cell. Biol.

125

131

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“…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). The sexual development of female mice is accelerated by exposure to these pheromones, which are either part of or bound to the protein.…”

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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“…These pheromones are excreted in male mouse urine (Novotny et al 1990); SBT induces estrus synchrony (Jemiolo et al 1986) and puberty acceleration in females (Novotny et al 1999a) and aggression in males (Novotny et al 1985), whereas HMH has an accelerating effect on female puberty onset (Novotny et al 1999b). MUPs (members of the lipocalin protein family) are a group of highly homologous soluble proteins that are either excreted in the urine or expressed in the nasal mucosa and lachrymal, parotid, sublingual, and submaxillary glands of mice (Finlayson and Braumann 1958;Sampsell and Held 1985;Shahan et al 1987). They bind to pheromones, and are proposed to play roles in regulating the release of pheromones from urine (Bacchini et al 1992;Robertson et al 1993), the capture of pheromones in the nose, and/or the delivery of pheromones to their receptors (Pelosi 1994;Marie et al 2000;Timm et al 2001;Sharrow et al 2002).…”

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Thermodynamic consequences of disrupting a water‐mediated hydrogen bond network in a protein:pheromone complex

et al. 2005

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The mouse pheromones (±)-2-sec-butyl-4,5-dihydrothiazole (SBT) and 6-hydroxy-6-methyl-3-heptanone (HMH) bind into an occluded hydrophobic cavity in the mouse major urinary protein (MUP-1). Although the ligands are structurally unrelated, in both cases binding is accompanied by formation of a similar buried, water-mediated hydrogen bond network between the ligand and several backbone and side chain groups on the protein. To investigate the energetic contribution of this hydrogen bond network to ligand binding, we have applied isothermal titration calorimetry to measure the binding thermodynamics using several MUP mutants and ligand analogs. Mutation of Tyr-120 to Phe, which disrupts a hydrogen bond from the phenolic hydroxyl group of Tyr-120 to one of the bound water molecules, results in a substantial loss of favorable binding enthalpy, which is partially compensated by a favorable change in binding entropy. A similar thermodynamic effect was observed when the hydrogen bonded nitrogen atom of the heterocyclic ligand was replaced by a methyne group. Several other modifications of the protein or ligand had smaller effects on the binding thermodynamics. The data provide supporting evidence for the role of the hydrogen bond network in stabilizing the complex.Keywords: enthalpy; hydrogen bond; major urinary protein; pheromone; thermodynamics; water Supplemental material: see www.proteinscience.orgThere is widespread interest in the roles that water molecules play in the stabilization and function of macromolecules and their complexes. X-ray crystal structures of proteins typically reveal many localized water molecules on the protein surface, in crevices, and sometimes buried within the protein interior or in the interfaces between proteins and bound ligands (Janin 1999;Mattos 2002). In favorable cases, NMR experiments can reveal the residence times of these water molecules (Halle and Denisov 2001). However, the contributions made by water molecule interactions to the stability of a folded structure or a complex cannot be reliably deduced from structural and dynamic data. One approach to establishing the importance of buried water has been to compare the positions of these solvent molecules in multiple high-resolution structures, obtained for different members of the same protein family or for the same protein under different crystallization conditions (Sadasivan et al. 1998;Loris et al. 1999;Nakasako 1999). An alternative approach has been to disrupt interactions with the water molecules by mutation of the relevant protein groups; such Abbreviations: HEWL, hen egg white lysozyme; HMH, 6-hydroxy-6-methyl-3-heptanone; ITC, isothermal titration calorimetry; MCP, 1-methyl-1-cyclopentene; MF, 4,5-dihydro-2-methylfuran; MO, 2-methyloxazoline; MP, 2-methyl-1-pyrroline; MT, 2-methyl-4,5-dihydrothiazole; MUP, major urinary protein; SBT, (±)-2-sec-butyl-4,5-dihydrothiazole.Article and publication are at http://www.proteinscience.org/cgi

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Mouse Proteinuria

Cited by 45 publications

References 0 publications

Differential, multihormonal regulation of the mouse major urinary protein gene family in the liver.

Differential, multihormonal regulation of the mouse major urinary protein gene family in the liver.

Proteinuria in rats in relation to age-dependent renal changes

Thermodynamic consequences of disrupting a water‐mediated hydrogen bond network in a protein:pheromone complex

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