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Biomedical subjects

H Ruotsalainen

Publications and source records attributed to H Ruotsalainen.

9 recordsLinked to original sources
PubMed2001

Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase.

Lysyl hydroxylase is an enzyme involved in collagen biosynthesis, catalyzing the hydroxylation of lysyl residues as a post-translational event. Three isoforms have been characterized so far (LH1, LH2, LH3). Our recent findings indicate that LH3 possesses, not only lysyl hydroxylase activity, but also galactosylhydroxylysyl glucosyltransferase activity [Heikkinen et al., J. Biol. Chem. 275 (2000) 36158-36163]. We report here the characterization of mouse LH2 (Plod2) and LH3/glucosyltransferase (Plod3) genes. Plod2 spans approximately 50 kb of the genomic DNA, and is organized in 20 exons, one of the exons being alternatively spliced in the RNA processing. Plod3 spans approximately 10 kb of the genomic DNA, and contains 19 exons. Analysis of the 5' flanking region with many transcription start sites reveals the lack of a TATAA box in both genes. Sequence analysis indicated many retroposon-like elements within the Plod3 gene. A comparison was carried out among the LH1, LH2 and LH3 gene structures characterized so far from different species.

Alternative Splicing↗
PubMed2001

Adenoviral gene transfer restores lysyl hydroxylase activity in type VI Ehlers-Danlos syndrome.

Type VI Ehlers-Danlos syndrome is a disease characterized by disturbed lysine hydroxylation of collagen. The disease is caused by mutations in lysyl hydroxylase 1 gene and it affects several organs including the cardiovascular system, the joint and musculoskeletal system, and the skin. The skin of type VI Ehlers-Danlos syndrome patients is hyperelastic, scars easily, and heals slowly and poorly. We hypothesized that providing functional lysyl hydroxylase 1 gene to the fibroblasts in and around wounds in these patients would improve healing. In this study we tested the feasibility of transfer of the lysyl hydroxylase 1 gene into fibroblasts derived from rats and a type VI Ehlers-Danlos syndrome patient (in vitro) and into rat skin (in vivo). We first cloned human lysyl hydroxylase 1 cDNA into a recombinant adenoviral vector (Ad5RSV-LH). Transfection of human type VI Ehlers-Danlos syndrome fibroblasts (about 20% of normal lysyl hydroxylase 1 activity) with the vector increased lysyl hydroxylase 1 activity in these cells to near or greater levels than that of wild type, unaffected fibroblasts. The adenoviral vector successfully transfected rat fibroblasts producing both beta-galactosidase and lysyl hydroxylase 1 gene activity. We next expanded our studies to a rodent model. Intradermal injections of the vector to the abdominal skin of rats produced lysyl hydroxylase 1 mRNA and elevated lysyl hydroxylase 1 activity, in vivo. These data suggest the feasibility of gene replacement therapy to modify skin wound healing in type VI Ehlers-Danlos syndrome patients.

Adenoviridae↗
PubMed1999

Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse.

We report on the isolation and characterization of cDNA clones for mouse lysyl hydroxylases 1, 2 and 3 (LH1, LH2, LH3). Phylogenetic analysis using nine lysyl hydroxylase sequences from five species indicates that the isoforms are derived from an ancestral gene by two duplication events, isoforms 1 and 2 being more closely related and having resulted from a more recent duplication than isoform 3. Expression of the isoforms is highly regulated in adult mouse tissues. LH1 is strongly expressed in the liver, heart, lung, skeletal muscle and kidney tissue, LH2 expression is high in the heart, lung, kidney, eye, ovary and placenta, whereas LH3 expression is high in the heart, lung, liver and testis tissue.

3' Untranslated Regions↗
PubMed1995

Personal goals of young social drop-outs.

To examine the extent to which personal goals and their appraisals are associated with problems in socialization, 20 young 'social drop-outs' (15 men, 5 women) and 21 students from a vocational school (20 men, 1 woman) were interviewed about their personal goals, related views of internality, externality, and likelihood of accomplishing goals. Analysis indicated that young adults who showed problems in socialization mentioned less frequently personal goals related to future education and housing than did the control group. Second, social drop-outs held more external and less internal views and were less optimistic about accomplishing personal goals than was the control group.

Adolescent↗
PubMed1988

Crystal structure, thermal behaviour, protonation and mass spectroscopic studies of racemic 4-[1-(2,3-dimethylphenyl)ethyl]-1H-imidazole hydrochlorides.

The crystal structure, thermal behaviour, mass spectrum and protonation of 4-[1-(2,3-dimethylphenyl)ethyl]-1H-imidazole (medetomidine) hydrochloride have been investigated. The title compound crystallizes in both hydrated and anhydrous forms, and their structures have been determined by three-dimensional X-ray structure analysis. The crystals of the anhydrous form are monoclinic and those of the hydrated form (containing one hydrate water molecule) are triclinic with unit-cell dimensions: a = 23.861(9), b = 7.721(4), c = 22.037(9) A, beta = 140.20(4) degrees, Z = 8, and space group C2/c, and a = 7.841(4), b = 8.380(3), c = 12.743(6) A, alpha = 93.66(3), beta = 102.90(3), gamma = 116.85(3) degrees, Z = 2, and space group P1, respectively. Thermal decomposition of the title compound has been interpreted from the TG, DTG and DSC curves with the help of mass spectrometry. Medetomidine hydrochloride monohydrate decomposes in four stages. The first is dehydration at 45-100 degrees C, the second is evaporation of HCl and medetomidine base at 200-320 degrees C, and the third and fourth are decomposition at 340-570 degrees C. The protonation constant is 7.04 in aqueous 0.1 M NaClO4 (25 degrees C).

Adrenergic alpha-Agonists↗
PubMed1987

A cyclic isomer of 2-hydroxymelatonin: a novel metabolite of melatonin.

A previously unknown melatonin metabolite was isolated by chloroform extraction and reverse phase HPLC from human and rat urine after administration of synthetic melatonin and characterized by mass spectroscopy and proton magnetic resonance spectroscopy to 1-acetyl-1,2,3,3a,8,8a-hexahydro-8a-hydroxy-5-methoxypyrrolo[2,3-b ]indole, a cyclic isomer of 2-hydroxymelatonin. This isolation was based on the fact that our melatonin antibody (a-MT-K1) cross-reacted against this novel metabolite at a level of 0.1% (melatonin 100%). In our HPLC program for indoles the cyclic 2-hydroxymelatonin eluted at 25 min, separately from synthetic indoles, between 6-hydroxymelatonin (19 min) and melatonin (35 min). In [3H] melatonin studies it was found to be present (at 25 min in our HPLC), accounting for 5% of the urinary metabolites of melatonin in the rat. Since beta-glucuronidase-arylsulfatase treatment of rat urine did not liberate the cyclic 2-hydroxymelatonin this would appear to be excreted into urine as the free form.

Adult↗
PubMed1984

Iodinated melatonin: preparation and characterization of the molecular structure by mass and 1H NMR spectroscopy.

Synthetic melatonin was iodinated by treatment with potassium iodide in the presence of an oxidizing agent, Iodo-Gen. The iodination products of melatonin were extracted with chloroform and separated by HPLC. The fraction showing immunoreactivity with respect to melatonin antisera was characterized as iodomelatonin by mass spectrometry, so that the substitution of iodine had occurred at a ring carbon atom. 1H NMR spectra showed the iodine to be incorporated at the C-2 position of the indole moiety. The N-[2-(2-iodo-5-methoxy-1H-indol-3-yl)ethyl]acetamide (2-iodomelatonin) reported here is more useful than [3H]melatonin as a tracer in melatonin radioimmunoassay. This method offers also the possibility of preparing iodinated serotonin and other indoleamines for biological studies.

Binding Sites↗