DNA probe localization at 18p113 band by in situ hybridization and identification of a small supernumerary chromosome

Mattei, Marie-Genevı̀eve; Philip, Nicole; Passage, E.; Moisan, Jean‐Paul; Mandel, Jean‐Louis; Mattéi, Jean-François

doi:10.1007/bf00293038

Cited by 306 publications

(103 citation statements)

References 8 publications

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“…Concavalin A-stimulated lymphocytes were cultured at 37°C for 72 h with 5-bromodeoxyuridine added for the final 6 h of culture (60 g/ml of medium), to ensure a chromosomal R-banding of good quality. The pB2-16 clone containing a 2-kb insert in pBluescript was tritium-labeled by nick-translation to a specific activity of 2 ϫ 10 8 dpm/ g. The radiolabeled probe was hybridized to metaphase spreads at final concentration of 25 ng/ml hybridization solution as described previously (18). After coating with nuclear track emulsion (Kodak NTB2), the slides were exposed for 20 days at 4°C, then developed.…”

Section: Methodsmentioning

confidence: 99%

Characterization of Two Age-induced Intracisternal A-particle-related Transcripts in the Mouse Liver

Puech

Dupressoír

Loireau

et al. 1997

Journal of Biological Chemistry

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Intracisternal A-particle (IAP) sequences are endogenous retrovirus-like elements present at 1,000 copies in the mouse genome. We had previously identified IAPrelated transcripts of unusual size (6 and 10 kilobases (kb)), which are observed exclusively in the liver of the aging mouse. In this report, using cDNA libraries that we have constructed from the liver mRNAs of an aged DBA/2 mouse, we have cloned and entirely sequenced the corresponding cDNAs. Both are initiated within the 5 long terminal repeat of a type I⌬1 IAP sequence, and correspond to a read-through into a unique flanking cellular sequence containing a 966-nucleotide open reading frame, located 3 to the IAP sequence. The 6-kb IAP-related transcript corresponds to a post-transcriptional modification of the 10-kb mRNA, and is generated by a splicing event with the donor site in the IAP sequence, and the acceptor site 5 to the open reading frame. This open reading frame is located on chromosome 3, is evolutionarily conserved, and discloses significant similarity to the yeast CCR4 transcription factor at the amino acid level. The specific expression of these age-induced transcripts, which account for more than 50% of the IAP-related transcripts in the liver of old mice, is therefore entirely consistent with the induction of a single genomic locus, thus strengthening the importance of position effects for the expression of transposable elements. Characterization of this locus should now allow studies on its chromatin and methylation status, and on the "molecular factors of senescence" possibly involved in its induction.

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Section: Methodsmentioning

confidence: 99%

Characterization of Two Age-induced Intracisternal A-particle-related Transcripts in the Mouse Liver

Puech

Dupressoír

Loireau

et al. 1997

Journal of Biological Chemistry

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“…Hybridization to metaphase chromosome, Giemsa staining after R-banding and autoradiography were performed as previously described [16].…”

Section: In Situ Hybridizationmentioning

confidence: 99%

Molecular characterization of a new urea transporter in the human kidney

et al. 1996

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A eDNA clone (HUT2) sharing 61.1% and 89.9% sequence identity with the human erythroid (HUTll) and the rabbit (UT2) urea transporters, respectively, was isolated by homology cloning from a human kidney library. HUT2 transcripts were restricted to the kidney and the HUT2 polypeptide was not immunoprecipitated with blood group Kidd-related antibodies (anti-Jk3) in coupled transcriptiontranslation assays. Functional expression studies in Xenopus oocytes demonstrated that HUT2-mediated urea transport was not inhibited by p-chloromercuribenzene sulfonate (pCMBS) which, however, inhibited the urea flux mediated by HUTll. These findings demonstrate that at least two distinct urea transporters are present in human tissues. By in situ hybridization, the gene encoding HUT2 has been assigned to chromosome 18q12.l-q21-1, as found previously for the Kidd/urea transporter HUT11, suggesting that both genes evolved from duplication of a common ancestor.

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“…The clone pSAmT3 was tritium labeled by nick-translation to a specific activity of 5 x lo7 dpm/Fg. The radiolabeled probe was hybridized to metaphase spreads at a final concentration of 100 nglpl of hybridization fluid as previously described (Mattei et al, 1985).…”

Section: Chromosomal Mapping Of the Timp-3 Gene By In Situ Hybridizationmentioning

confidence: 99%

Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP‐3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10

Apte

Hayashi

Seldin

et al. 1994

Developmental Dynamics

129

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Remodeling of the extracellular matrix (ECM) is an essential component of normal development and is also involved in the pathogenesis of arthritis and the spread of cancer. The matrix metalloproteinases and their natural inhibitors, the tissue inhibitors of metalloproteinases (TIMPs), play an important role in this context. We have isolated mouse cDNA clones encoding a novel member of the TIMP family, designated TIMP-3. We have assigned the Timp-3 locus to the [Cl-D11 region of mouse chromosome 10 using both genetic and cytogenetic methods. The conceptual translation product of the Timp-3 cDNA shows a high degree of similarity with ChIMP-3, a recently cloned chicken metalloproteinase inhibitor, as well as significant structural similarity with the amino acid sequences of the previously isolated members of this family, TIMP-1 and TIMP-2. The pattern of expression of Timp-3 in the developing mouse embryo is distinct from that previously reported for Timp-1. Timp-3 is expressed in cartilage and skeletal muscle, in myocardium, in the skin, oral and nasal epithelium, in the newborn mouse liver, in the epithelium of some tubular structures such as the developing bronchial tree, oesophagus, colon, urogenital sinus, bile duct, in the kidney, salivary glands, and in the choroid plexus of the brain. The patterns of Timp-3 expression in surface epithelia and in the epithelial lining of many tubular organs suggests that TIMP-3 may be involved in regulating ECM remodeling during the folding of epithelia and during the formation, branching, and expansion of epithelial tubes. In the mouse placenta, expression is seen in the trophoblast, raising the possibility that TIMP-3 may be involved in regulating trophoblastic invasion of the uterus. We propose a role for TIMP-3 in musculoskeletal and cardiac development, in the morphogenesis of certain epithelial structures, and placental implantation.

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DNA probe localization at 18p113 band by in situ hybridization and identification of a small supernumerary chromosome

Cited by 306 publications

References 8 publications

Characterization of Two Age-induced Intracisternal A-particle-related Transcripts in the Mouse Liver

Characterization of Two Age-induced Intracisternal A-particle-related Transcripts in the Mouse Liver

Molecular characterization of a new urea transporter in the human kidney

Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP‐3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10

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