A female monster with developmental abnormality of body stalk.
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Abdominal Muscles↗
Biomedical subjects
V V Rao
Publications and source records attributed to V V Rao.
Expression of recombinant human multidrug resistance P-glycoprotein in insect cells confers decreased accumulation of technetium-99m-sestamibi.
UNLABELLED: The multidrug-resistant P-glycoprotein is a M(r) 170,000 plasma membrane protein encoded by the mammalian multidrug resistance gene (MDR) which appears to function as an efflux transporter of a variety of potent chemotherapeutic agents. METHODS: To directly demonstrate that 99mTc-sestamibi is recognized by the human P-glycoprotein, we overexpressed recombinant human MDR1 P-glycoprotein in host Sf9 insect cells using a baculoviral vector and correlated expression of the gene product with 99mTc-sestamibi accumulation. RESULTS: In parental Sf9 cells and in wild-type baculoviral infected (control) cells, 99mTc-sestamibi accumulation asymptotically approached a plateau of 650 fmoles (mg protein)-1 (nMo)-1 and 337 fmoles (mg protein)-1 (nMo)-1, respectively. In MDR1 baculoviral infected cells, P-glycoprotein expression was maximal at 72 hr postinfection, while 99mTc-sestamibi accumulation was reduced to 12 fmole (mg protein)-1 (nMo)-1. Verapamil (500 microM), the classical MDR modulator, produced an approximately 300% enhancement of 99mTc-sestamibi accumulation in Sf9 cells expressing MDR1 P-glycoprotein, but only a 50% enhancement in parental Sf9 cells, consistent with verapamil-induced inhibition of P-glycoprotein-mediated 99mTc-sestamibi efflux. CONCLUSIONS: These data demonstrate that the recombinant protein is transiently expressed in a functional state capable of drug transport in Sf9 cell membranes and that 99mTc-sestamibi is a transport substrate recognized by the human MDR1 P-glycoprotein. Technetium-99m-sestamibi may prove useful for functionally characterizing P-glycoprotein expression in human tumors in vivo.
ATP Binding Cassette Transporter, Subfamily B, Mem↗
L-pipecolic acid oxidation in rat: subcellular localization and developmental study.
By using a sensitive radioactive assay method, we present here evidence that L-pipecolic acid oxidase is localized in both mitochondria and peroxisomes of rat liver. Brain white matter contained a more than 2-fold higher activity of L-pipecolic acid oxidation than the brain cortex. Suborganellar fractionation studies indicate that while the enzyme is a matrix protein in mitochondria, it is membrane-associated in peroxisomes. Both rotenone and antimycin A completely inhibited the enzyme activity in mitochondria but not in peroxisomes. The enzyme was shown to be inducible in mitochondria and peroxisomes of rat liver and brain tissues by glucagon and di-(2-ethylhexyl)phthalate, respectively. We report here for the first time the developmental aspects of L-pipecolic acid oxidation activity in rat liver and brain tissues. L-Pipecolic acid oxidase activity was detectable in whole rat embryo at 10 days of gestation, suggesting active L-pipecolic acid metabolism early during development. In both liver and brain tissues L-pipecolic acid oxidation activity was highest at 15 days of gestation and decreased with age in prenatal and postnatal conditions.
Aging↗
Cystatin C (CST3), the candidate gene for hereditary cystatin C amyloid angiopathy (HCCAA), and other members of the cystatin gene family are clustered on chromosome 20p11.2.
The cystatin C gene (CST3) encodes a low-molecular-weight cysteine proteinase inhibitor belonging to family II of the cystatin superfamily and is mutated in cases of hereditary cystatin C amyloid angiopathy (HCCAA). CST3, which along with other family II cystatin genes is a member of the cystatin gene family, has been assigned to chromosome 20. To investigate the genomic organization on chromosome 20, the CST3 gene and related sequences were regionally mapped by fluorescence in situ hybridization (FISH), Southern blot, and pulsed-field gel electrophoresis (PFGE) analysis using the cDNA cystatin C probe C6a and three genomic probes, C3E1, C3E2, and C3E2-2. Probe C3E2-2, which like probe C3E2 is specific for CST3, hybridized to only one HindIII and one XbaI fragment on Southern blots and to a 300-kb BssHII PFGE fragment. FISH with probe C3E2 mapped this locus to chromosome 20p11.2, with an FL-pter value of 0.37 +/- 0.07 on the physical map. Probe C3E1 containing the most conserved cystatin gene exon (exon 1) and its flanking sequences hybridized with more fragments, e.g., to eight XbaI and nine HindIII fragments on conventional Southern blots and to eight SmaI, two BssHII (900 and 300 kb), and two NotI fragments after PFGE. FISH with C3E1 revealed only one single site at 20p11.2 with an FL-pter value of 0.37 +/- 0.04, identical to that obtained with C3E2.(ABSTRACT TRUNCATED AT 250 WORDS)
Blotting, Southern↗
Pharmacokinetics of single-dose administration of naproxen at 10:00 and 22:00 hours.
The pharmacokinetics of naproxen was studied in 12 healthy male volunteers after a single oral dose of 500 mg at 10:00 and 22:00 h. Ingestion of drug at 22:00 h delayed the occurrence of peak serum levels (p < 0.0212). None of the other pharmacokinetic parameters exhibited any significant diurnal variations.
Administration, Oral↗
Gene structure of semenogelin I and II. The predominant proteins in human semen are encoded by two homologous genes on chromosome 20.
The genes for semenogelin I and II, the major protein constituents of the human seminal fluid, have been characterized by three overlapping clones in bacteriophage lambda, encompassing 31.5 kilobases (kb) of genomic DNA. The two genes are located 11.5 kb apart in the region q12-q13.1 on chromosome 20. Both genes are relatively compact, spanning only 2.7 and 3.1 kb, respectively. The transcription units are composed of three exons, of which the first encodes the signal peptide, the second encodes the secreted protein, while the third solely contains 3'-noncoding nucleotides. The nucleotide sequences exhibit a similarity of close to 90% in the exons and exceeding 80% in the introns and flanking nucleotides.
Amino Acid Sequence↗
Assay for L-pipecolate oxidase activity in human liver: detection of enzyme deficiency in hyperpipecolic acidaemia.
A direct assay method is described for L-pipecolate oxidase. The assay uses NaHSO3 to trap the L-alpha-amino [3H]adipate delta-semialdehyde (AAS) formed as a direct reaction product of L-pipecolate oxidase from L-[3H]pipecolic acid. The adduct so formed was separated from the substrate on Dowex 50 (H+) column. The product was identified as [3H]AAS by amino acid analysis after breaking down the adduct by boiling under acidic conditions. The assay is simpler and more specific than fluorometric methods; it is also more sensitive, requiring at most 16 micrograms of liver peroxisome-enriched protein per assay. We have used this assay procedure to detect L-pipecolate oxidase in skin fibroblasts obtained from a control subject and from patients of hyperpipecolic acidaemia and Zellweger syndrome and found that this enzyme activity is present in the control, but absent or decreased in the patients with the peroxisomal disorders.
Humans↗
The gene for bone morphogenetic protein 2A (BMP2A) is localized to human chromosome 20p12 by radioactive and nonradioactive in situ hybridization.
Bone morphogenetic protein 2A (BMP2A), a member of the decapentaplegic-Vg-related family, belongs to the transforming growth factor beta superfamily and has a striking sequence similarity to the decapentaplegic locus in Drosophila melanogaster, a major determinant of pattern specification during embryogenesis. BMP2A is thought to be involved in cartilage and bone formation during embryogenesis, but may have additional functions in morphogenesis as implied by its expression in various organs and embryonic tissues of mice. Human BMP2A, assigned to chromosome 20 by the use of human-Chinese hamster ovary cell hybrids, is considered to be a reasonable candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva. We have confirmed the localization of BMP2A to chromosome 20 and regionally assigned the locus to 20p12 by radioactive and nonradioactive in situ hybridization.
Bone Morphogenetic Proteins↗
Developmental changes of L-lysine-ketoglutarate reductase in rat brain and liver.
1. Developmental aspects of L-lysine-ketoglutarate reductase, the first enzyme in saccharopine pathway of L-lysine degradation in rat liver and brain tissues were studied. 2. Although the adult rat brain shows negligible activity, the enzyme activity was shown to be highly active during the early stages of development. 3. The enzyme activity gradually decreased through development in the brain, whereas it gradually increased in the liver, establishing the fact that the saccharopine pathway is the major pathway in liver. 4. Our results also show that glucagon stimulated the induction of this enzyme by 2-3-fold in both adult liver and brain tissues.
Aging↗
The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is assigned to human chromosome 20p12-pter by in situ hybridization (ISH and FISH).
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Chromosome Mapping↗
Pax1, a member of the paired box-containing class of developmental control genes, is mapped to human chromosome 20p11.2 by in situ hybridization (ISH and FISH).
Pax-1, a member of a murine multigene family, belongs to the paired box-containing class of developmental control genes first identified in Drosophila. The Pax-1 gene encodes a sequence-specific DNA-binding protein with transcriptional activating properties and has been found to be mutated in the autosomal recessive mutation undulated (un) on mouse chromosome 2 with vertebral anomalies along the entire rostrocaudal axis. By radioactive in situ hybridization (ISH) using a fragment from the murine Pax-1 paired box that is almost identical to the respective sequences from the cognate human gene HuP48 and fluorescence in situ hybridization (FISH) using a complete mouse Pax-1 cDNA, we have assigned the human homologue of murine Pax-1, the PAX1 locus, to chromosome 20p. The map position of PAX1 after FISH (FL-pter value of 0.34 +/- 0.04) corresponds to band p11.2. These results confirm the exceptional homology between human chromosome 20 and the distal segment of mouse chromosome 2, extending from bands F to G, and add PAX1 to the group of genes on 20p like PTPA, PRNP, SCG1, BMP2A, which are located in proximity on both chromosomes.
Animals↗
The polymorphic DNA sequence D20S14 is assigned to human chromosome 20p12----p11.2 by in situ hybridization.
The polymorphic DNA marker D20S14 was previously mapped to human chromosome 20 and shown to be linked to two other DNA markers, D20S5 and D20S6, located at 20p12. This segment has been implicated in several human diseases. Because of its importance, we mapped the D20S14 locus to 20p12----p11.2 by radioactive in situ hybridization.
Chromosome Mapping↗
The human gene for oxytocin-neurophysin I (OXT) is physically mapped to chromosome 20p13 by in situ hybridization.
Two posterior pituitary hormones oxytocin and arginine-vasopressin control the important activities of water excretion, parturition and lactation. Both these hormones are synthesized as inactive precursors in the hypothalamus along with their carrier proteins neurophysin I and neurophysin II respectively and are activated upon transport to posterior pituitary. Human genes for both oxytocin-neurophysin I (OXT) and arginine-vasopressin-neurophysin II (ARVP) are cloned and found to be linked on chromosome 20 separated by approximately 12 kb of intergenic sequences. Though OXT is not yet associated with any disease, ARVP is linked to the autosomal dominant disease neurohypophyseal diabetes insipidus (AD-NDI). We have mapped regionally the OXT locus to chromosome 20p13 by both radioactive (ISH) and fluorescence in situ hybridization (FISH).
Arginine Vasopressin↗
Chronopharmacokinetics of rifampicin.
Chronopharmacokinetics of rifampicin was studied in four healthy adult male human volunteers after drug (2.0 g) ingestion at 6.00, 12.00, 18.00 and 24.00 hr. The absorption rate constant was found to be lower and the time to reach peak concentration was longer after drug administration at 24.00 hr than at other dosing times. A second peak was observed in all individual volunteers between 6-12 hr after drug dosing at 24.00 hr. This may be due to the influence of biliary rhythms on the disposition kinetics of rifampicin.
Adult↗
Physical mapping of two Xp markers DXS16 and DXS143.
Lymphocyte karyotyping of an infant girl with the clinical features of microphthalmia, iridoschisis, goiter, hip joint dysplasia, labium synechia and craniotabes revealed an Xp deletion. The lymphocyte karyotypes of the parents were normal. Bromodeoxyuridine incorporation studies showed that, in 42 out of 43 metaphases, the deleted X chromosome was late replicating. In one metaphase, the normal X chromosome was observed to be allocyclic. Using DNA markers from the Xp22 region, the breakpoint was assigned distal to DXS16 (pXUT23) and proximal to DXS143 (dic56). Dosage intensity measurements confirmed that the STS gene and the DNA marker DXS31 were involved in the deleted area. Restriction fragment length polymorphism analysis revealed that the paternally derived X-chromosome was deleted.
Abnormalities, Multiple↗
Mapping of the ribophorin II (RPN II) gene to human chromosome 20q12-q13.1 by in-situ hybridization.
Ribophorin I and II (RPN I and RPN II), two specific glycoproteins, span the rough regions of the endoplasmic reticulum (RER) and are thought to play an important role either in translocation or in the maintenance of RER. Studies with human-mouse somatic cell hybrids have localized the gene for RPN I on human chromosome 3q, while RPN II is on chromosome 20. Using a radioactive labelled cDNA probe, we have regionally mapped the RPN II gene to human chromosome 20q12-q13.1 by in situ hybridization. This assignment predicts a location of the murine homologue, Rpn-2, to the syntenic segment on mouse chromosome 2 in close proximity to Ada, Src and Gnas.
Chromosome Mapping↗
The gene for the novel vasoactive peptide endothelin 3 (EDN3) is localized to human chromosome 20q13.2-qter.
Endothelin 3 is a novel vasoactive peptide of unique structure and belongs to the endothelin gene family. Though it mainly functions as a vasoconstrictor/pressor, it plays a major role in a wide variety of other biological functions, possibly as a novel neuropeptide. Studies with human-mouse somatic cell hybrids have suggested that the gene EDN3 is localized on human chromosome 20. We confirmed this localization and regionally mapped the gene to the region 20q13.2-q13.3.
Animals↗
G protein Gs alpha (GNAS 1), the probable candidate gene for Albright hereditary osteodystrophy, is assigned to human chromosome 20q12-q13.2.
Guanine nucleotide-binding proteins, also known as G proteins, mediate intracellular responses to a wide variety of extracellular stimuli. A variety of genes that specify the synthesis of the components of guanine nucleotide proteins have been identified. One of these proteins, termed Gs alpha (GNAS1), is the G protein component of the olfactory signal transduction cascade. Mutations in the GNAS1 gene leading to Gs alpha protein deficiency are known to be associated with pseudohypoparathyroidism Ia (Albright hereditary osteodystrophy) and certain pituitary tumors with acromegaly. Studies on the human--mouse somatic cell hybrids provisionally assigned this gene to chromosome 20. We have now confirmed this localization on chromosome 20 and regionally assigned the GNAS1 gene to 20q12-q13.2 by in situ hybridization.
Chromosome Banding↗