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Biomedical subjects

N J Rose

Publications and source records attributed to N J Rose.

At least 19 recordsLinked to original sources
PubMed2001

Chromosomal positioning of human T-lymphotropic type 1 proviruses by fluorescence in situ hybridisation.

Fluorescence in situ hybridisation (FISH) was employed to identify the chromosomal integration site of the human T-cell lymphotropic virus, type 1 (HTLV-1) present in T-cell clones derived from HTLV-1-infected individuals and a virally transformed cell line, C8166-45. Proviral sequences were detected in C8166-45 but not uninfected Jurkat cells. Integration sites were reliably detected in T-cell clones determined previously to be infected with HTLV-1. The results indicated that the transformed cell line and some of the T-cell clones possessed more than one proviral integration site. This hybridisation system is useful for determining the number of integration events and for localising proviruses to specific chromosomal regions.

Cell Line, Transformed↗
PubMed2000

Virus inactivation in a proportion of human T-cell leukaemia virus type I-infected T-cell clones arises through naturally occurring mutations.

Human T-cell leukaemia virus type I (HTLV-I) is the aetiological agent of adult T-cell leukaemia/lymphoma and tropical spastic paraparesis/HTLV-I-associated myelopathy (TSP/HAM). The trans-activating protein (Tax) of HTLV-I is strongly implicated in cellular proliferation. We examined the tax gene and 5' long terminal repeat (LTR) sequences in eight naturally infected T-cell clones derived from TSP/HAM-affected individuals who were either productively (proliferate spontaneously) or silently (do not proliferate spontaneously) infected. In two silently infected clones point mutations within the proviruses resulted in truncation of the Tax protein. One clone harboured both a deleterious tax gene mutation and a point mutation in an enhancer element of the 5' LTR. Sequence changes, immunological escape mutation, integration site context and host cell phenotype may all contribute to the high proportion of latently or silently infected T-cells found in vivo in virus carriers.

5' Untranslated Regions↗
PubMed1999

Sulfation of thyroid hormone by estrogen sulfotransferase.

Sulfation is one of the pathways by which thyroid hormone is inactivated. Iodothyronine sulfate concentrations are very high in human fetal blood and amniotic fluid, suggesting important production of these conjugates in utero. Human estrogen sulfotransferase (SULT1E1) is expressed among other tissues in the uterus. Here we demonstrate for the first time that SULT1E1 catalyzes the facile sulfation of the prohormone T4, the active hormone T3 and the metabolites rT3 and 3,3'-diiodothyronine (3,3'-T2) with preference for rT3 approximately 3,3'-T2 > T3 approximately T4. Thus, a single enzyme is capable of sulfating two such different hormones as the female sex hormone and thyroid hormone. The potential role of SULT1E1 in fetal thyroid hormone metabolism needs to be considered.

Diiodothyronines↗
PubMed1995

A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III.

In general, osteogenesis imperfecta (brittle bone disease) is caused by heterozygous mutations in the genes encoding the alpha 1 or alpha 2 chains of type I collagen (COL1A1 and COL1A2, respectively). In this study we screened these genes in a proband presenting with the severe form (type III) of osteogenesis imperfecta for mutations which might result in the phenotype. Single-strand conformation polymorphism mapping analysis was used to identify a region suspected of harbouring the mutation and subsequent sequence analysis revealed a heterozygous G to A transition in the alpha 2(I) gene of type I collagen in the individual. The resulting substitution of the glycine at position 238 of the alpha chain by serine is the most N-terminal yet reported for this chain.

Base Sequence↗
PubMed1994

Three unrelated individuals with perinatally lethal osteogenesis imperfecta resulting from identical Gly502Ser substitutions in the alpha 2-chain of type I collagen.

In general, osteogenesis imperfecta is caused by heterozygous mutations in either of the genes encoding the alpha 1 or alpha 2 chains of type I collagen (COL1A1 and COL1A2, respectively). Usually, these mutations are unique to the affected individual or individuals within a family. In this study, single-strand conformation polymorphism mapping analysis has been coupled with sequence analysis to identify a single base mutation in the alpha 2(I) gene of type I collagen; this mutation is identical in three unrelated individuals with perinatal lethal osteogenesis imperfecta. The heterozygous G to A transition at a CpG dinucleotide results in a Gly502Ser substitution in the alpha 2 chain of type I collagen.

Base Sequence↗
PubMed1992

Structural studies of oxygen-bridged iron compounds.

Compound (I): cis-dichloro[mu-[bis[mu-[[2,6-diacetylpyridine dioximato](2-)-O:O']]dihydroxodiphenyl-diborato](3-)]- mu- mithoxydiiron, [Fe2(C30H29B2N6-O6)Cl2(CH3O)], M(r) = 804.9, monoclinic, Cc, a = 21.228 (6), b = 8.020 (2), c = 20.865 (5) A, beta = 105.2 (1) degrees, V = 3428 (2) A3, Z = 4, Dx = 1.56 g cm-3, lambda(Mo K alpha) = 0.7107 A, mu = 10.6 cm-1, F(000) = 1648, T = 275 K, R = 0.055 for 3018 unique reflections. Compound (I) contains a pseudo-twofold axis relating the two pyridine dioxime groups bound to the Fe atoms. In addition, two O atoms from the phenylborate moieties bridge the iron atoms, as does a methoxide. The two Cl atoms are bound to the seven coordinate metals axial to the methoxide. Compound (II): cis-dichloro[mu-[bis[mu-[[2,6-diacetylpyridine dioximato](2-)-O:O']]dihydroxodiphenyldiborato](3-)]-mu- hydroxodiiron, [Fe2(C30H29B2N6-O6)Cl2(OH)].H2O.2C2H3N, M(r) = 891.0, monoclinic, P2(1)/n, a = 11.860 (2), b = 20.911 (5), c = 16.175 (3) A, beta = 92.88 (1) degrees, V = 4006 (3) A3, Z = 4, Dx = 1.48 g cm-3, lambda(Mo K alpha) = 0.7107 A, mu = 9.1 cm-1, F(000) = 1832, T = 275 K, R = 0.051 for 7034 unique reflections. Compound (II) contains a hydroxide group replacing the methoxide in compound (I). The crystals also contain two acetonitriles of solvation. The bond lengths in the complex and the hydrogen-bonding pattern in the crystals are consistent with one of the bridging borate O atoms being protonated.(ABSTRACT TRUNCATED AT 250 WORDS)

Bridged-Ring Compounds↗
PubMed1982

An in vivo evaluation of iron-chelating drugs derived from pyridoxal and its analogs.

Chelating agents related to the newly described iron binding drug, pyridoxal isonicotinoyl hydrazone, were screened for their effects on iron excretion in the rat, employing a new and highly sensitive radioisotopic procedure. Pyridoxal itself induced significant iron excretion when given either parenterally or orally, the excreted iron being derived from the same pool as that tapped by the drug currently used in treating iron overload in man, desferrioxamine B. Schiff base derivatives of pyridoxal produced varying amounts of iron excretion, the hydrazone derivatives being much more effective than pyridoxal alone. These data suggested a number of possible mechanisms for the chelation of endogenous iron by such agents. Pyridoxal benzoyl hydrazone induced approximately 50% more iron excretion than did an equivalent dose of the parent isonicotinoyl analog and bile cannulation studies showed this difference to be associated with a prolonged duration of action of the benzoyl derivative. When give i.v., the benzoyl and isonicotinoyl hydrazones of pyridoxal and the benzoyl hydrazone of salicylaldehyde all produced levels of iron excretion which exceeded that seen with an equivalent dose of desferrioxamine B. It is concluded that the range of active Schiff base derivatives is likely to be large and that some of these, although not necessarily any of the particular compounds described here, may prove to be of clinical use.

Animals↗