Severe fibronectin-deposit renal glomerular disease in mice lacking uteroglobin

Science

Volumn 276, Issue 5317, 1997, Pages 1408-1412

  Zhang, Zhongjian ^a   Kundu, Gopal C ^a   Yuan, Chiun Jye ^a   Ward, Jerrold M ^b   Lee, Eric J ^a   DeMayo, Francesco ^c   Westphal, Heiner ^a   Mukherjee, Anil B ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

^c BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; ANTIBODY; BOVINE SERUM ALBUMIN; COLLAGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 3; DNA; FIBRONECTIN; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M; LAMININ; LYSOPHOSPHATIDIC ACID; MESSENGER RNA; MONOCLONAL ANTIBODY; OSTEOPONTIN; PHOSPHOLIPASE A2; PROTEIN; SCLEROPROTEIN; UTEROGLOBIN; VITRONECTIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DENSITOMETRY; ELECTROPORATION; GENE TARGETING; GENOTYPE; GLOMERULONEPHRITIS; HISTOPATHOLOGY; IMMUNOBLOTTING; IMMUNOFLUORESCENCE; IMMUNOHISTOCHEMISTRY; MOUSE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN BINDING; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SOUTHERN BLOTTING;

ANIMALS; CELLS, CULTURED; CROSSES, GENETIC; FIBRONECTINS; GENE TARGETING; HUMANS; KIDNEY DISEASES; KIDNEY GLOMERULUS; MICE; MICE, INBRED C57BL; UTEROGLOBIN;

EID: 0030910985     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.276.5317.1408     Document Type: Article

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32. 51. The rabbit antibody to murine Fn (Gibco-BRL) was used at a dilution of 1:1000, and the antibody to UG was used at 1:500.
33. -/- mouse, with glomerular lesions, was fixed in formalin and embedded in epoxy resin. Thin sections stained with uranyl acetate and lead citrate were examined with an electron microscope. Photomicrographs were taken either at x6000 or at x60,000.
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44. +/+ mice were injected with 1 mg of Fn alone in 150 μl of PBS daily for three consecutive days.
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46. Z. Zhang et al., unpublished results.
47. Fn matrix assembly and fibrillogenesis in cultured cells (CRL6336, American Type Culture Collection) were determined as described [D. F. Mosher, J. Sottile, C. Wu, J. A. McDonald, Curr. Biol. 4, 810 (1992)].
48. G. Mazzucco, E. Maran, C. Rollino, G. Monga, Hum. Pathol. 23, 63 (1992); E. H. Strom et al., Kidney Int. 48, 163 (1995); K. J. M. Assmann, R. A. P. Koene, J. F. M. Wetzels, Am. J. Kidney Dis. 25, 781 (1995); O. Gemperle, J. Neuweiler, F. Reutter, F. Hidebrandt, R. Krapf, ibid. 28, 668 (1996).
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52. A Bam HI-Eco RI 3.2-kb DNA fragment containing exon-3 of 129/SVJ mouse UG gene (14) and its flanking sequences were subcloned into the corresponding site of the pPNW vector as described [K. Lei et al., Nature Genet. 13, 203 (1996)]. A 0.9-kb PCR-amplifed fragment containing partial exon-2 and its flanking sequences with built-in Not I and Xho I sites were subcloned into the vector to generate the targeted construct pPNWUG. In pPNWUG, a 1.2-kb DNA fragment, including partial exon-2. was replaced with the PGK-neo cassette, disrupting the UG gene. Not I-linearized targeting construct DNA (25 μg) was electroporated into ES R1 cells. Chimeric mice were mated with C57BL/6 strain of mice, and germline transmission of the mutated UG allele was identified by PCR and Southern blot analyses of offspring tail DNA. The genotyping of progeny was carried out by PCR with a set of neo-specific primers, neo-L (5′-ATA CGC TTG ATC CGG CTA CCT GCC-3′) and neo-R (5′-CAT TTG CAC TGC CGG TAG AAC TCC-3′), which yield a 667-base pair (bp) DNA fragment. A 304-bp DNA fragment was generated with a set of UG-specific primers, mUG-L (5′-ACA TCA TGA AGC TCA CAG GTA TGC-3′) and mUG-R (5′-GTG TGC ACG GTT CAA GCT TGT AGT-3′), derived from the region of the UG gene that was replaced by the PGK-neo cassette. After an initial denaturing step (95°C for 2 min), 40 cycles of PCR were performed (94°C for 1 min, 58°C for 1.5 min. 72°C for 1 min) with a final step at 72°C for 10 min, by using a Perkin-Elmer 480 DNA thermal cycler.
53. The contributions of G.C.K. and C.-J.Y. in delineating the mechanism of UG action should be considered equal. We thank A. Nagy, R. Nagy, and W. Abramow-Newerly for ES R1 cells; L. Miele for statistical analyses; L. Miele and G. Mantile-Selvaggi for facilitating recombinant UG production in Escherichia coli; A. Kulkami, K. M. Yamada, J. Chou, I. Owens, S. W. Levin, J. DeB. Butler, K.-J. Lei, and C.-J. Pan for their assistance, discussions, and suggestions, and Syntex Research for gancyclovir. Supported in part by a USPHS grant (number HL47620 to F.D.).