PMC:1382200 / 29547-39658
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/1382200","sourcedb":"PMC","sourceid":"1382200","source_url":"http://www.ncbi.nlm.nih.gov/pmc/1382200","text":"Methods\n\nCloning and sequencing of the mouse Capn2 locus\nThe mouse Capn2 gene encodes the 700 amino acids of the m-calpain large subunit (m-80 k) and consists of 21 exons extending over 50-kb on chromosome 1. A cDNA clone encoding a portion of the mouse m-80 k subunit was purchased (dbEST Id, 807416, Image:606689, Image Consortium, LLNL). It was found to contain 2.8-kb of sequence from position 247 of the coding sequence to the stop codon at position 2,101, including the 3'-UTR to the polyA signal. A fragment of this cDNA was subcloned and used to screen a 129Sv mouse genomic library in λ-Dash II. Overlapping genomic clones were obtained covering 15,354 bp, extending from a BamHI site in intron 3 to a BamHI site in intron 15. These clones were sequenced completely on both strands and the data were submitted to GenBank (accession no. AF497625). The submitted sequences agreed precisely with the public databases, and also filled in several small gaps corresponding to short repetitive sequences which could only be firmly established by repeated sequencing in non-standard conditions.\n\nConstruction of the Capn2 targeting vector\nA targeting construct was designed to replace a 785 bp BamHI-HindIII fragment, containing exon 7 of the Capn2 gene, with the PGK-Neo cassette (Figure 1). Exon 7 encodes 24 amino acids in the active-site region, including Asn286, one of the catalytic triad residues. The short (upstream) arm of the targeting construct was provided by a 2.7-kb HindIII-BamHI fragment, containing exons 5 and 6, which was inserted into the pPNT vector upstream of the PGK-Neo cassette [48]. During cloning, the BamHI site at the 3' end of the short arm was abolished. The loss of this BamHI site in the mutant allele, coupled with the introduction of a new BamHI site at the 3' end of the PGK-Neo cassette, provided a basis for distinguishing the wild-type and mutant alleles by Southern blotting. The long (downstream) arm of homology was provided by a 7-kb HindIII-KpnI fragment, extending from intron 7 to intron 12, inserted between the PGK-Neo and thymidine kinase (tk) cassettes.\nFigure 1 Targeting strategy for disruption of the murine Capn2 gene. The murine Capn2 gene, encoding the m-80 k subunit, was disrupted in ES cells by homologous recombination. The structures of the wild-type allele (top), the targeting vector (middle), and the mutant allele (bottom) are depicted. In the mutant allele, a PGK-Neo cassette replaces a 0.8-kb genomic fragment containing exon 7 (grey rectangle) which encodes the active site asparagine residue (Asn286) In the targeting vector, the PGK-Neo cassette is flanked by 2.7-kb of Capn2 homologous sequence in the upstream (short) arm and 7.9-kb of homology in the downstream (long) arm. A probe located immediately outside of the short arm detects a 3.5-kb BamHI fragment from the wild-type allele and a 5.3-kb BamHI fragment from the mutant allele. Exons are depicted as open vertical rectangles except for exon 7 which is represented by a solid vertical rectangle. The probe used in most Southern blot analyses is shown as a solid, horizontal rectangle, while triangles mark the positions of PCR primers also used for genotyping purposes.\n\nES cell culture, transfection and selection of targeted clones\nMouse R1 ES cells [49] were maintained on gelatin-coated plates with feeder layers of mouse embryonic fibroblasts at 37°C under 5% CO2 in ES cell medium (DMEM [high glucose] supplemented with 15% fetal bovine serum, 0.1 mM non-essential amino acids, 2 mM glutamine, 1 mM sodium pyruvate, 0.1 mM 2-mercaptoethanol, 100 U/ml penicillin, 100 μg/ml streptomycin, 25 μg/ml amphotericin, and 1,000 U/ml of ESGro [Chemicon]). Fetal bovine serum from HyClone Laboratories Inc (Logan, Utah) was tested for its ability to support ES cell growth. Gelatin was from Sigma-Aldrich Canada (Oakville, Ontario). Unless otherwise specified, all other tissue culture reagents were from Gibco-BRL.\nThe targeting construct was linearized by NotI digestion and electroporated into R1 ES cells. Cells were plated without feeder layers on gelatin-coated plates and transformed clones were selected in the presence of 200 μg/ml G418 (Gibco- BRL) and 2 μM ganciclovir (Syntex, Inc.) for eight days. Drug-resistant clones were picked, expanded on gelatin-coated plates, and genotyped by Southern blotting and PCR analysis (see below).\n\nGeneration of targeted mice\nCapn2+/- ES cells were aggregated overnight with 8-cell embryos recovered from CD1 matings, as previously described [31]. On the next day, blastocysts were transferred to pseudopregnant CD1 females. Chimeric animals were identifiable at birth by black eye pigmentation and subsequently by patches of agouti coat colour. Chimeric males were bred with CD1 females to identify those males capable of germline transmission. These were then bred with 129SvJ females to establish the mutation in an inbred genetic background. Mouse protocols were approved by the Queen's University Animal Care Committee according to the guidelines of the Canadian Council on Animal Care.\n\nGenotyping methods\nSeveral Southern blot and PCR strategies were exploited in order to determine the genotype of the Capn2 locus. Southern blotting was carried out using the digoxigenin (DIG) non-radioactive system (Roche). In most cases, membranes were blotted with BamHI-digested genomic DNA and hybridized with a DIG-labeled 823 bp exon 4-containing BamHI-HindIII fragment located immediately upstream of the short arm of homology (Figure 1). A 681 bp PstI-XbaI fragment from the PGK-Neo cassette was also used to probe Southern blots in order to verify a single integration event in targeted clones.\nGenotyping was also carried out by PCR analysis of genomic DNA. The sequences of all oligonucleotide primers are listed in Table 1. A single-step PCR strategy was sufficient for genotyping ES cells or biopsies from post-implantation embryos and weanlings (Figure 1). A 2,748 bp segment of the wild-type allele and a 2,711 bp segment of the mutant allele were amplified in separate reactions using a common (intron 4) sense primer, located outside the short arm of homology, and distinct antisense primers which hybridized to either wild-type (exon 7) or mutant (PGK-Neo) sequence (Table I). The thermocycling parameters included a five minute initial denaturation step at 95°C, 30 cycles of one minute denaturation at 95°C, one minute annealing at 56°C, and one minute extension at 72°C, with a ten minute final extension step.\nTable 1 Oligonucleotide primers used to genotype the Capn2 locus\nAllele Primer Location Oligonucleotide Sequence\nSingle-Step\nBoth Sense Intron 4 5'-GGGCCCCCATTGCCTCTTAGC-3'\nWild-type Antisense Exon 7 5'- GGATTCCTGATGCGGATCAATTTCTGC-3'\nMutant Antisense PGK-Neo 5'-CCTCGAAGTCGAGGTCGATCC-3'\nNested PCR\nWild-Type (Diagnostic) Sense #1 Intron 6 5'-CAACATCATAAGCAACGGAGAACGC-3'\nSense #2 Intron 6 5'-GCCTGTGACAGAAGTACCACCAG-3'\nAntisense #1 Intron 7 5'-CTCCTCGGCCCTCCCTGTAG-3'\nAntisense #2 Exon 7 5'-GGATTCCTGATGCGGATCAATTTCTGC-3'\nMutant (Diagnostic) Sense #1 Intron 6 5'-CAACATCATAAGCAACGGAGAACGC-3'\nSense #2 Intron 6 5'-GCCTGTGACAGAAGTACCACCAG-3'\nAntisense #1 PGK-Neo 5'-CCTACCCGGTAGAATTGACCTGC-3'\nAntisense #2 PGK-Neo 5'-GACCTGCAGGGGCCCTC-3'\nBoth (Internal Control) Sense #1 Intron 4 5-GGGATGAAGGCTCCCTGTTGC-3'\nSense #2 Exon 5 5'-GGGGGTGCCACCACGGAA -3'\nAntisense #1 Intron 5 5'-CCCCTAGAGGACTATTGCCTGG-3'\nAntisense #2 Intron 5 5'-GATGCACCCATGCCTTAAGGAGC-3' Due to the limited amount of genetic material available in pre-implantation embryos, a nested PCR strategy was developed to yield reliable genotyping information (Figure 4). Whole embryos were first digested in 20 μL of proteinase K buffer (see below). The lysate was then divided in two, with half (10 μL) being used in the amplification of the wild-type allele and the remaining 10 μL in the amplification of the mutant allele.\nThe first reaction in the nested PCR amplification of the wild-type allele was carried out in a final reaction volume of 50 μL, using an intron 6 sense primer and an antisense primer located in intron 7. Two μL of the first reaction were used as template in the second PCR amplification using another intron 6 sense primer and an antisense primer in exon 7. The nested amplification of the mutant allele was carried out similarly. The first primer pair consisted of the intron 6 sense primer and an antisense primer in the PGK-Neo cassette. The nested primer pair was comprised of the second intron 6 sense primer and an antisense primer also located within the PGK-Neo sequence. It should be noted that amplification of both sequences involved the same sense primers in both steps of the nested PCR strategy. In addition, the two sets of reactions included a common internal control designed to amplify a genomic region within the short arm of the targeting vector that is preserved in both the wild-type and mutant alleles. The first primer pair of the control PCR was made up of an intron 4 sense primer and an intron 5 antisense primer. The second primer pair comprised an exon 5 sense primer and a nested intron 5 antisense primer. The final products were 213 bp for the control PCR, 429 bp for the wild-type PCR, and 389 bp for the mutant PCR. All reactions were carried out using identical PCR conditions entailing an initial five minute denaturation at 95°C, 35 cycles of one minute denaturation at 95°C, one minute annealing at 56°C, and one minute extension at 72°C, with a final extension step of ten minutes.\n\nIsolation of pre-implantation embryos\nTime of fertilization was determined by observation of copulation plugs, and noon of that day was defined as E0.5. Pre-implantation embryos were obtained by dissecting the uteri out of pregnant females at E2.5 or E3.5 and flushing the oviducts with ES cell medium. Isolated embryos were then digested for five hours at 55°C in 20 μL of lysis buffer (50 mM Tris-HCl, 0.5% Triton X-100, 200 μL/mL proteinase K, pH 8.0), followed by ten minutes at 95°C to inactivate the proteinase K. 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