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Biomedical subjects

N Davidson

Publications and source records attributed to N Davidson.

At least 199 records · Page 11Linked to original sources
PubMed1985

Gone tomorrow? CEOs speak out on institutional survival.

In this second of two articles based on a national survey of hospital CEOs, the authors probe the issue of survival as it pertains both to hospitals and their respective CEOs, and what actions CEOs believe are required to help ensure their well-being. The first article, which appeared in the April issue of Trustee, compared the thinking of hospital CEOs and their peers in nonhospital corporate positions on management succession and retirement issues.

Attitude of Health Personnel↗
PubMed1984

Release of labelled taurine from the rat dorsal medulla and cerebellum in vivo.

Stimulus-induced release of labelled taurine has been studied in the superfused rat cerebellar cortex and dorsal medulla in vivo. In the cerebellum both elevated potassium and electrically induced depolarization consistently produced marked increases in the efflux of exogenously applied taurine in a calcium-dependent fashion. Veratridine-stimulation evoked a large Ca2+-independent taurine efflux which was, however, prevented by tetrodotoxin. In the dorsal medulla, both high K+ and veratridine induced a clear Ca2+-independent increase in taurine efflux. Electrical stimulation was always ineffective in changing taurine efflux from the dorsal medulla. These data strongly support a possible neurohumoral role for taurine in the cerebellum but not in the dorsal medulla.

Animals↗
PubMed1984

Transcription and expression of the herpes simplex virus tk gene inserted into proviral sequences of feline leukemia virus.

Recombinant DNA molecules containing the herpesvirus tk gene inserted near the middle of a cloned feline leukemia virus proviral genome, in the same transcriptional orientation as the long terminal redundancies (LTRs), were used to transform human tk- cells. Analysis of RNA from cloned lines indicates that the 5' LTR promotes a high level of transcription which, as a result of differing RNA splicing and polyadenylation pathways, results in three large, abundant RNAs, two of which contain the entire tk coding region. The tk promoter itself initiates transcription of a smaller, relatively rare tk mRNA, of the same length and abundance as found in cells transformed with the tk gene alone. Assays indicate that there is little if any thymidine kinase (TK) enzymatic activity contributed by the abundant LTR-promoted transcripts. This is presumably due to inefficient initiation of tk translation from the longer LTR-initiated transcripts because of upstream AUG codons in the viral sequences. RNA blots indicate that the viral LTR is stronger as a promoter than the tk promoter. The results also indicate that about one-third of the LTR-initiated transcripts are polyadenylated at the tk poly(A) site, while the rest use the poly(A) site of the 3' LTR.

Cloning, Molecular↗
PubMed1984

Isolation and characterization of a cDNA clone for the complete protein coding region of the delta subunit of the mouse acetylcholine receptor.

A mouse cDNA clone has been isolated that contains the complete coding region of a protein highly homologous to the delta subunit of the Torpedo acetylcholine receptor (AcChoR). The cDNA library was constructed in the vector lambda 10 from membrane-associated poly(A)+ RNA from BC3H-1 mouse cells. Surprisingly, the delta clone was selected by hybridization with cDNA encoding the gamma subunit of the Torpedo AcChoR. The nucleotide sequence of the mouse cDNA clone contains an open reading frame of 520 amino acids. This amino acid sequence exhibits 59% and 50% sequence homology to the Torpedo AcChoR delta and gamma subunits, respectively. However, the mouse nucleotide sequence has several stretches of high homology with the Torpedo gamma subunit cDNA, but not with delta. The mouse protein has the same general structural features as do the Torpedo subunits. It is encoded by a 3.3-kilobase mRNA. There is probably only one, but at most two, chromosomal genes coding for this or closely related sequences.

Amino Acid Sequence↗
PubMed1984

Isolation of the Drosophila melanogaster dunce chromosomal region and recombinational mapping of dunce sequences with restriction site polymorphisms as genetic markers.

Using the method of chromosomal walking, we have isolated a contiguous region of the Drosophila melanogaster X chromosome which corresponds to salivary gland chromosome bands 3C12 to 3D4. This five-band region contains approximately 100 kilobases of DNA, including those sequences comprising dunce, a gene which functions in memory and cyclic nucleotide metabolism. Genome blots of DNA from flies carrying several different chromosomal aberrations with breakpoints in the region have been probed with the isolated clones to map the breakpoints on the cloned DNA and to delimit dunce sequences. This has localized dunce to a 50-kilobase region. In addition, we have searched this 50-kilobase region for restriction site polymorphisms between X chromosomes from different Drosophila strains by genome blotting experiments, and we have followed the segregation of detected polymorphisms and dunce alleles after meiotic recombination. The data map one dunce mutation between two polymorphisms located 10 to 12 kilobases apart.

Animals↗
PubMed1984

Drosophila melanogaster has only one myosin alkali light-chain gene which encodes a protein with considerable amino acid sequence homology to chicken myosin alkali light chains.

A chimeric lambda DNA molecule containing the myosin alkali light-chain gene of Drosophila melanogaster was isolated. The encoded amino acid sequence was determined from the nucleic acid sequence of a cDNA homologous to the genomic clone. The identity of the encoded protein was established by two criteria: (i) sequence homology with the chicken alkali light-chain proteins and (ii) comparison of the two-dimensional gel electrophoretic pattern of the peptides synthesized by in vitro translation of hybrid-selected RNA to that of myosin alkali light-chain peptides extracted from Drosophila myofibrils. There is only one myosin alkali light-chain in D. melanogaster; its chromosomal location is region 98B . This gene is abundantly expressed during the development of larval as well as adult muscles. The Drosophila protein appears to contain one putative divalent cation-binding domain (an EF hand) as compared with the three EF hands present in chicken alkali light chains.

Amino Acid Sequence↗
PubMed1984

Isolation and characterization of the Beadex locus of Drosophila melanogaster: a putative cis-acting negative regulatory element for the heldup-a gene.

We isolated recombinant lambda phage clones spanning 49 kilobases of DNA which contain the Beadex and heldup-a loci of Drosophila melanogaster. These cloned DNAs were used to analyze the structure of eight dominant mutant alleles of the Beadex locus which show increased gene activity. A region, only 700 base pairs in length, is altered in each of these mutants. Six of the mutations have DNA insertions within this segment. Most of these insertions resemble retrovirus-like transposable elements. In one case (Beadex2) the inserted sequences are homologous to the gypsy transposon family. The other two Beadex alleles were induced by hybrid dysgenesis and suffered deletions which included at least part of the 700-base-pair segment. These deletions appear to have resulted from imprecise excision or deletion of a nearby P element found in the wild-type parental strain. Analysis of one heldup-a allele (heldup-aD30r) indicates that a similar P element-mediated event is responsible for this lesion. In this mutant, deletion of sequences no more than 1,600 base pairs from the Beadex locus accompanies the loss of heldup-a function. The deleted sequences in heldup-aD30r include the entire 700-base-pair segment within which at least part of the Beadex locus resides, yet these flies have no Beadex phenotype. This indicates that a functional heldup-a gene is necessary for expression of the Beadex phenotype. Together, these results suggest that the Beadex functional domain is contained within a short segment of DNA near the heldup-a gene and support the hypothesis that the Beadex locus functions as a cis-acting negative regulatory element for the heldup-a gene.

Alleles↗
PubMed1983

Two gene families clustered in a small region of the Drosophila genome.

Three Drosophila genes that are clustered within 8 X 10(3) bases of DNA at the chromosomal region 44D have been identified and mapped, and the gene cluster entirely sequenced. The three genes are 55 to 60% homologous in DNA sequence. One gene contains an intron in its 5'-proximal protein coding sequence while the other two have none at this position; similarly, another gene has an intron in its 3'-proximal protein coding sequence which is not found in the other genes. All three genes are abundantly expressed together in Drosophila first, second, and early third instar larval stages and in adults, but they are not abundantly expressed in either embryonic, late third instar larval, or pupal stages. This gene family lies 11 X 10(3) bases away from another cluster containing four Drosophila larval cuticle protein genes plus a pseudogene. The cuticle genes are all abundantly expressed throughout third instar larval development. Thus, at least seven protein-coding genes and one pseudogene lie within 27 X 10(3) bases of DNA. Moreover, two small gene families can lie adjacent on a chromosome and exhibit different patterns of developmental regulation, even though individual genes within each clustered family are co-ordinately expressed.

Animals↗
PubMed1983

Expression of complete transplantation antigens by mammalian cells transformed with truncated class I genes.

Mouse L cells transformed with the cloned class I genes of the major histocompatibility complex of the mouse express transplantation antigens with serological determinants of the donor haplotype. However, transformation with the truncated subclones of a BALB/c H-2Ld gene containing the exons encoding the external domains also leads to the production of cells which express complete cell-surface molecules. Moreover, full-length products of the foreign haplotype, as judged by serological and biochemical criteria, are generated independently of the use of carrier DNA in transformation. However, the frequency of productive transformation is substantially less than that obtained with a complete gene. The most plausible explanation for these phenomena involves homologous recombination between host chromosomal and donor class I sequences.

Animals↗
PubMed1983

Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner.

We have surveyed expression of the six Drosophila actin genes during ontogeny. Unique portions of cloned actin genes were used to monitor levels of respective mRNAs in developmentally staged whole organisms and dissected body parts. We find that each gene is transcribed to form functional mRNA, which accumulates with a distinct pattern. Two of the genes, act5C and act42A, are expressed in undifferentiated cells and probably encode cytoplasmic actins. Act57A and act87E are expressed predominantly in larval, pupal, and adult intersegmental muscles; act88F in muscles of the adult thorax; and act79B in the thorax and leg muscles. These composite data define three main patterns of actin gene expression which are correlated with changing Drosophila morphology, particularly muscle differentiation and reorganization.

Actins↗
PubMed1983

Drosophila has one myosin heavy-chain gene with three developmentally regulated transcripts.

We have isolated overlapping genomic clones that contain a single-copy myosin heavy-chain gene of Drosophila melanogaster. By the criteria of hybridization under nonstringent conditions, this is the only myosin heavy-chain gene of the fly. The gene is localized to the chromosomal region 36B. The transcriptional unit has a length of about 19 kb and contains at least nine introns. There are three mature mRNA species expressed from the gene, with molecular lengths of 7.2 kb, 8.0 kb and 8.6 kb. The former two are expressed abundantly during those stages of development when larval muscle proteins are being synthesized; the latter two are expressed when the principal muscle proteins of the adult are made. The three transcripts differ primarily in their respective patterns of splicing at the 3' ends.

Animals↗