Disparition de protéines urinaires spécifiques dans le syndrome néphrotique à la Puromycine

Dinh, Bao-Linh; Tremblay, Angelo; Brassard, André; Dufour, D

doi:10.1007/bf02151557

Cited by 3 publications

(6 citation statements)

References 8 publications

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“…These results are similar to those of Roy & Neuhaus ( 3 ) , but differ from those of Dinh et al (2). The latter authors reported the presence of three components in the RU-aWRS system and four components in the RS-aWRU system described above.…”

Section: Discussionsupporting

confidence: 84%

“…Dinh et al (2) reported five components distributed in the rho, albumin and alpha, globulin zones. Dinh et al (2) reported five components distributed in the rho, albumin and alpha, globulin zones.…”

Section: Discussionmentioning

confidence: 99%

“…In male rat urine, only three tissue-like proteins were identified: one with the renal constituents (13,2,14), and two with the accessory genital gland constituents (15,5). Our purpose is to study further the immunological relationships between the tissue-like proteins and proteins extracted from organs related to the urinary system.…”

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confidence: 99%

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Urinary Proteins of the Normal Rat

Perassi

Martín

1973

International Journal of Peptide and Protein Research

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The protein composition of normal male rat urine and the possible origin of its components were studied immunologically.A t least sixteen antigenic components were identified, eight of which showed immunological identity to serum proteins. These are: albumin, three alpha, (ahha,B, aIpha,c, and a/pha,D), two alpha,, beta,c, and gamma globulin. These components seem to arise from the blood by glomerular filtration.The other eight components did not show immunologic identity with serum proteins. Two components migrated in the rho zone,Jive or six in the alpha, zone, and one in the beta zone.The antigenic relationship between tissue-like proteins in the urine, and proteins extracted from the kidney, urinary tract or related organ tissues, was also studied. Antiserum to whole rat urine absorbed with rat serum gave two precipitin lines with kidney extract, one with the ureter, one with the bladder, three with the prostate, three with the bulbo urethral glands, two with the mixture of testis, epididymis, and ductus deferens, and two with the mixture of seminal vesicle and coagulating glands. With this same antiserum some of the tissue extracts gave reactions of identity among themselves.Rat urine contains about 15 protein components which have been classified according to their antigenicity, biological activity, electrophoretic mobilities and origins (1-5). Some of them showed 268, 1-9.

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Section: Discussionsupporting

confidence: 84%

Section: Discussionmentioning

confidence: 99%

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Urinary Proteins of the Normal Rat

Perassi

Martín

1973

International Journal of Peptide and Protein Research

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“…In urine of fertile male rats, androgen-dependent ␣ 2u -globulin, a member of the lipocalin superfamily (10), is the quantitatively major protein (9). Therefore, ␣ 2u -globulin was purified from male urine as described by Holmquist et al (21) and assessed for its capability to induce IP 3 formation.…”

Section: Selective Activation Of Distinct G Proteins In the Vnomentioning

confidence: 99%

“…Major urinary proteins have been suggested to be involved in puberty acceleration (5,7,8), an endocrinological effect prevented by lesions of the VNO or the accessory olfactory bulb (1). Major urinary proteins of mice and the rat equivalent ␣ 2u -globulin (9) belong to the superfamily of lipocalins, a structurally homologous but diverse family of extracellular proteins, characterized by their ability to bind small, principally hydrophobic molecules (10). Although recent structural studies have characterized the naturally bound volatile substances (11), major urinary proteins lacking the natural volatiles remain active (8) suggesting that proteins themselves act as pheromones.…”

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confidence: 99%

Selective Activation of G Protein Subtypes in the Vomeronasal Organ upon Stimulation with Urine-derived Compounds

Krieger

Schmitt

Löbel

et al. 1999

Journal of Biological Chemistry

145

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Chemosensory neurons in the vomeronasal organ (VNO) detect pheromones related to social and reproductive behavior in most terrestrial vertebrates. Current evidence indicate that the chemoelectrical transduction process is mediated by G protein-coupled second messenger cascades. In the present study, attempts were made to identify the G protein subtypes which are activated upon stimulation with urinary pheromonal components. G protein-specific antibodies were employed to interfere specifically with inositol 1,3,4-trisphosphate formation induced by urinary stimuli and to immunoprecipitate G␣-subunits, activation dependently labeled with [␣-32 P]GTP azidoanilide. The results of both experimental approaches indicate that stimulation of female VNO membrane preparations with male urine samples induces activation of G i as well as G o subtypes. Experiments using different fractions of urine revealed that upon stimulation with lipophilic volatile odorants, only G i proteins were activated, whereas G o activation was elicited by ␣ 2u -globulin, a major urinary protein, which is a member of the lipocalin superfamily. Since each G protein subtype is stereotypically coexpressed with one of the two structurally different candidate pheromone receptors (V1R and V2R), the results provide the first experimental evidence that V1Rs coexpressed with G i may be activated by lipophilic probably volatile odorants, whereas V2Rs coexpressed with G o seem to be specialized to interact with pheromonal components of proteinaceous nature.Terrestrial vertebrates detect chemical signals via sensory neurons located in two anatomically distinct systems: the nasal olfactory epithelium (OE) 1 and the vomeronasal organ (VNO). Whereas the main olfactory system is responsible for the "conventional" sense of smell, the VNO appears to specifically detect pheromones, thereby inducing a distinct social or sexual behavior or endocrine response (1-3). In rodents, the major source of phermones seems to be the urine, however, only few volatile (4) and non-volatile (5) urinary substances producing a definite endocrine or behavioral response have been identified. The best characterized non-volatile urinary components in male mouse urine are the "major urinary proteins" (6). Major urinary proteins have been suggested to be involved in puberty acceleration (5,7,8), an endocrinological effect prevented by lesions of the VNO or the accessory olfactory bulb (1). Major urinary proteins of mice and the rat equivalent ␣ 2u -globulin (9) belong to the superfamily of lipocalins, a structurally homologous but diverse family of extracellular proteins, characterized by their ability to bind small, principally hydrophobic molecules (10). Although recent structural studies have characterized the naturally bound volatile substances (11), major urinary proteins lacking the natural volatiles remain active (8) suggesting that proteins themselves act as pheromones.The molecular mechanisms responsible for the detection of pheromones and the signal transduction processes in the VN...

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The X-ray structure of a recombinant major urinary protein at 1.75 Å resolution. A comparative study of X-ray and NMR-derived structures

Kuser

Franzoni

Ferrari

et al. 2001

Acta Crystallogr D Biol Cryst

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Major urinary proteins belong to the lipocalin family and are present in the urine of rodents as an ensemble of isoforms with pheromonal activity. The crystal structure of a recombinant mouse MUP (rMUP) was solved by the molecular‐replacement technique and refined to an R factor and Rfree of 20 and 26.5%, respectively, at 1.75 Å resolution. The structure was compared with an NMR model and with a crystallographic structure of the wild‐type form of the protein. The crystal structures determined in different space groups present significantly smaller conformational differences amongst themselves than in comparison with NMR models. Some, but not all, of the conformational differences between the crystal and solution structures can be explained by the influence of crystallographic contacts. Most of the differences between the NMR and X‐ray structures were found in the N‐terminus and loop regions. A number of side chains lining the hydrophobic pocket of the molecule are more tightly packed in the NMR structure than in the crystallographic model. Surprisingly, clear and continuous electron density for a ligand was observed inside the hydrophobic pocket of this recombinant protein. Conformation of the ligand modelled inside the density is coherent with the results of recent NMR experiments.

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Disparition de protéines urinaires spécifiques dans le syndrome néphrotique à la Puromycine

Cited by 3 publications

References 8 publications

Urinary Proteins of the Normal Rat

Urinary Proteins of the Normal Rat

Selective Activation of G Protein Subtypes in the Vomeronasal Organ upon Stimulation with Urine-derived Compounds

The X-ray structure of a recombinant major urinary protein at 1.75 Å resolution. A comparative study of X-ray and NMR-derived structures

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