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Biomedical subjects

J Yoon

Publications and source records attributed to J Yoon.

At least 91 records · Page 5Linked to original sources
PubMed1995

Mycobacterium tuberculosis infection in an orangutan (Pongo pygmaeus).

A respiratory disorder was noted in a 5-year-old female orangutan kept in the Yongin Farmland. Radiographically, multiple radiodense foci ranging from 2 to 6 mm diameter were seen throughout the lung lobes. Grossly, the thoracic cavity revealed a firm texture and grayish-pink discoloration of the left apical lung lobe. Histopathologically, multifocal areas of granulomatous pneumonia present the right and left apical lung lobes. Both primers from IS1081 and IS6110 targeting 196 bp and 245 bp respectively were used in polymerase chain reaction, Mycobacterium tuberculosis was isolated from liver and confirmed by polymerase chain reaction.

Animals↗
PubMed1995

Fatal vascular involvement in systemic lupus erythematosus following epidermolysis bullosa acquisita.

Epidermolysis bullosa acquisita may be associated with various systemic diseases, including systemic lupus erythematosus. We describe the clinical and immunological findings in a 38-year-old women with epidermolysis bullosa acquisita and systemic lupus erythematosus. The epidermolysis bullosa acquisita preceded a dramatic flare of systemic lupus erythematosus and fatal cerebral vasculitis. If serologic evidence of lupus erythematosus develops during the course of epidermolysis bullosa acquisita, a thorough investigation is warranted to rule out potentially life-threatening systemic lupus erythematosus.

Adult↗
PubMed1994

Torsade de pointes induced by terfenadine in a patient with long QT syndrome.

Torsade de pointes is a form of polymorphic ventricular tachycardia that is associated with prolongation of the QT interval. Although torsade de pointes is found in many clinical settings, it is mostly drug induced. Similar problems have been described with nonsedating H1-receptor antagonists, such as astemizole and terfenadine. Terfenadine is a widely used antihistamine. The authors report a case of torsade de pointes in a patient with a possible congenital sporadic form of QT interval prolongation who was receiving a therapeutic dose of terfenadine.

Adult↗
PubMed1993

Evidence for adaptive evolution of the G6pd gene in the Drosophila melanogaster and Drosophila simulans lineages.

Proponents of the neutral theory argue that evolution at the molecular level largely reflects a process of random genetic drift of neutral mutations. Under this theory, levels of interspecific divergence and intraspecific polymorphism are expected to be correlated across classes of nucleotide or amino acid sequences with different degrees of functional constraint, such as synonymous and replacement sites. Nucleotide sites with reduced polymorphism should show comparably reduced levels of interspecific divergence. To examine this hypothesis, we have sequenced 32 and 12 copies of the glucose-6-phosphate dehydrogenase (G6pd) gene in Drosophila melanogaster and Drosophila simulans, respectively. Both species exhibit similar levels of nucleotide polymorphism at synonymous sites. D. melanogaster shows two amino acid polymorphisms, one associated with the cosmopolitan allozyme polymorphism and a second with an allozyme polymorphism endemic to European and North African populations. In contrast, D. simulans shows no replacement polymorphism. While synonymous divergence between species is 10%, which is typical of other genes, there are 21 replacement differences. This level of amino acid sequence divergence, when contrasted with levels of amino acid polymorphism, silent polymorphism, and divergence, is in 10-fold excess over that expected under the neutral model of molecular evolution. We propose that this excess divergence reflects episodes of natural selection on G6pd resulting in fixation of advantageous amino acid mutations in these two recently separated lineages.

Adaptation, Physiological↗
PubMed1993

Sea urchin maternal mRNA classes with distinct development regulation.

Previous studies of newly synthesized proteins during early development in sea urchins have revealed several different patterns of synthesis that can be used to predict the existence of mRNA classes with distinct regulatory controls. We have identified clones for abundant maternal mRNAs that are actively translated during early development by screening a cDNA library prepared from polysomal poly(A)+RNA isolated from 2-cell stage (2-hour) Strongylocentrotus purpuratus embryos. Probes prepared from these cDNA clones and several previously characterized maternal mRNA cDNAs were used to compare relative levels of individual mRNAs in eggs and embryos and their translational status at various developmental stages. These abundant mRNAs can be classified into two major groups which we have termed cleavage stage-specific (CSS) and post cleavage stage (PCS) mRNAs. The relative levels of the CSS mRNAs are highest during the rapid cleavage stage and decrease dramatically at the blastula stage (12-hours). In contrast, PCS mRNAs are present at relatively low levels during the rapid cleavage stage and then increase at the blastula stage. Polysome partition profiles reveal that CSS mRNAs are translated more efficiently than PCS mRNAs in the unfertilized egg, at fertilization, and during the cleavage stages. Following the blastula stage, some CSS transcripts move out of polysomes and accumulate as untranslated RNAs, while newly transcribed PCS mRNAs are recruited into polysomes. These data suggest that the rapid cell cycles following fertilization require high levels of specific cleavage stage proteins, and the synthesis of these proteins occurs preferentially over PCS mRNAs.

Animals↗
PubMed1993

Fluorescent chemosensing of catechol and catecholamines in water.

It has been known for almost 35 years that catechol complexes reversibly to boronic acids. We observe that 2-anthrylboronic acid complexes catechol in water with Kd 330 microM and concomitant 20-fold reduction in fluorescence intensity. L-DOPA and dopamine behave similarly, suggesting a mechanism for the development of real-time sensing schemes.

Binding Sites↗
PubMed1993

Relapsing syphilis.

Although penicillin still remains highly effective for syphilis, concerns have been raised that current regimens may be inadequate for the treatment of early syphilis. We report the failure of benzathine penicillin in the treatment of secondary syphilis. Extensive tracing of sexual contact history failed to identify sources of possible reinfection; therefore, we believe that this case represents a treatment failure and an ensuing relapse of secondary syphilis.

Adult↗
PubMed1991

A Drosophila phospholipase C gene that is expressed in the central nervous system.

A Drosophila phospholipase C (PLC) gene, designated as plc-21, was isolated by screening a genomic DNA library using a cDNA for a previously isolated Drosophila PLC gene, norpA, as probe under reduced stringency hybridization conditions. The gene maps to 21C on the left arm of the second chromosome. Two proteins of 1305 and 1312 amino acids, respectively, were deduced from two classes of cDNA which were isolated. The two putative plc-21 proteins are similar in sequence and overall structure to the beta-class of PLCs found in mammals and differ from each other only by 7 amino acid residues that are present near the C terminus of one of the proteins but not the other. Hybridization of plc-21 cDNA probes to blots of poly(A)+ RNA revealed that the gene encodes a 7.0-kilobase transcript that could be detected in the head but not in the body of adult flies and a 5.6-kilobase transcript that could be detected throughout development and in both heads and bodies of adults. In situ hybridization of cDNA sequences to tissue sections showed that the gene is expressed in the neuronal cell bodies of the optic lobe, central brain, and thoracic ganglia of adults and the brain of larvae. This tissue distribution of plc-21 transcripts is identical to the distribution of transcripts from a Drosophila Go alpha-subunit gene that we reported previously.

Amino Acid Sequence↗
PubMed1989

Molecular characterization of Drosophila gene encoding G0 alpha subunit homolog.

A Drosophila melanogaster gene (dgo) encoding a G protein alpha subunit has been isolated by screening genomic and adult head cDNA libraries using bovine transducin alpha subunit cDNA as probe. The gene, which maps to 47A on the second chromosome, encodes two proteins which are both 354 amino acids long but differ in seven amino acids in the amino-terminal region. The deduced amino acid sequences of the two proteins are 81% identical to that of a rat Go alpha subunit. Analysis of genomic clones revealed that there are eight coding exons and that the putative transcripts for the two proteins differ in the 5'-noncoding regions and the first coding exons but share the remaining six coding exons. The arrangement of two different 5'-noncoding regions on the gene suggests that two different promoters regulate the expression of the transcripts encoding the two proteins. RNA blot analysis detected three transcripts: a 3.9-kilobase (kb) transcript found at all stages of development; a 5.4-kb transcript present predominantly in adult heads; and a 3.4-kb transcript present only in adult bodies. In situ hybridizations of a cDNA probe to adult tissue sections showed that the gene is expressed abundantly in neuronal cell bodies in the brain, optic lobe, and thoracic ganglia.

Amino Acid Sequence↗
PubMed1987

Mechanism of suppression in Drosophila: regulation of tryptophan oxygenase by the su(s)+ allele.

The suppressor gene, su(s)2, in Drosophila melanogaster restores the production of red and brown eye pigments for some purple and vermilion mutant alleles, respectively. We showed previously that the product of the su(s)+ allele caused inhibition of the sepiapterin synthase A produced by the purple mutant but did not affect the wild-type enzyme. Suppression was accomplished by removing su(s)+ from the genome. We now report that the tryptophan oxygenase, produced by suppressible vermilion alleles, is also inhibited by extracts from su(s)+ flies. The inhibition of the vermilion enzyme can be reduced or eliminated, respectively, by prior storage of the extract at 4 or -20 degrees C or by boiling, whereas the wild-type enzyme is not affected by extracts of su(s)+ flies. Also, when the suppressible vermilion strain is raised on certain diets, brown eye pigment production occurs. This epigenetic suppression was reduced by the presence of an extra copy of su(s)+ in the genome. These data support a posttranslational mechanism for regulation of enzyme activity in which the activity of the mutant enzyme is reduced by the product of the su(s)+ allele. How the su(s)+ gene product can distinguish between the normal and the mutant forms of these two enzymes is discussed, along with other mechanisms for suppression that are currently under investigation.

Alleles↗
PubMed1985

Messenger RNA structure participating in the initiation of synthesis of cucumber mosaic virus coat protein.

The sequence of the 5'-terminal 106 nucleotides of cucumber mosaic virus (strain Y) RNA 4, the mRNA coding for viral coat protein, has been determined. The first AUG was located at 77 nucleotides from the 5'-terminus and was confirmed to be an initiation codon by analysis of the N-terminal amino acid sequence of the protein. The nucleotide sequence (positions 77-106) beyond the AUG codon predicted the sequence of ten amino acids corresponding to the N-terminal region of the protein, which exactly matched the determined amino acid sequence containing an acetyl methionine as the N-terminal amino acid. The distance of the initiation codon AUG from the cap structure was 76 nucleotides and the longest among the mRNAs for coat protein of plant viruses so far reported (9-36 nucleotides). This noncoding region is rich in U residues (40%) and the number of G residues (21 nucleotides) is the largest among these mRNAs (usually 1 or 2 residues). A possible secondary structure is postulated for the region, which might be implicated in efficient translation of the RNA 4 in vivo.

Amino Acid Sequence↗