Eero Vuorio - Academia.edu (original) (raw)

Papers by Eero Vuorio

Research paper thumbnail of Construction and partial characterization of two recombinant cDNA clones for procollagen from chicken cartilage

Nucleic Acids Research, 1982

Research paper thumbnail of Co-expression of collagens II and XI and alternative splicing of exon 2 of collagen II in several developing human tissues

Biochemical Journal, Sep 1, 1993

Research paper thumbnail of Epidermal growth factor increases collagen production in granulation tissue by stimulation of fibroblast proliferation and not by activation of procollagen genes

Biochemical Journal, Oct 15, 1987

Research paper thumbnail of Localization of types I, II, and III collagen mRNAs in developing human skeletal tissues by in situ hybridization

Journal of Cell Biology, Apr 1, 1987

Research paper thumbnail of Conservation of the sizes of 53 introns and over 100 intronic sequences for the binding of common transcription factors in the human and mouse genes for type II procollagen (COL2A1)

Biochemical Journal, Jun 15, 1995

Research paper thumbnail of The mouse collagen X gene: complete nucleotide sequence, exon structure and expression pattern

Biochemical Journal, 1993

Research paper thumbnail of Construction and Partial Characterization of Recombinant cDNA Clones for Chicken Type I Collagen Messenger RNAs

Acta Chemica Scandinavica, 1984

Research paper thumbnail of Construction and identification of a cDNA clone for human type II procollagen mRNA

Biochemical Journal, Jul 1, 1985

Research paper thumbnail of Mice With a Deletion in the First Intron of the <i>Col1a1</i> Gene Develop Age-Dependent Aortic Dissection and Rupture

Circulation Research, Jan 9, 2004

Research paper thumbnail of Expression of mRNAs coding for the alpha 1 chain of type XIII collagen in human fetal tissues: comparison with expression of mRNAs for collagen types I, II, and III

Journal of Cell Biology, Sep 1, 1989

Research paper thumbnail of Tissue inhibitor of metalloproteinases 4 (TIMP4) is involved in inflammatory processes of human cardiovascular pathology

Histochemistry and Cell Biology, Mar 7, 2006

Research paper thumbnail of Abnormal Mitochondria in Cultured Synovial Fibroblasts in Rheumatoid and Reactive Arthritis?

Rheumatology, Aug 18, 1988

This paper summarizes our recent studies on synovial fibroblast cultures started from patients wi... more This paper summarizes our recent studies on synovial fibroblast cultures started from patients with rheumatoid or reactive arthritis and from healthy controls. Analysis of these cultures by flow cytometry, spectroscopy and electron microscopy revealed consistent differences between arthritic and normal fibroblasts. Increased autofluorescence, exceptional light scatter properties, rhodamine-123 staining and electron microscopic findings of fibroblasts from arthritis patients suggest involvement of mitochondria in the disease process. Conditioned media of activated monocytes induced in the mitochondria of normal synovial fibroblasts changes similar to those observed in the fibroblasts originating from patients with rheumatoid or reactive arthritis.

Research paper thumbnail of Plasma membranes from experimental granulation tissue

Biochemical Journal, Mar 1, 1975

Research paper thumbnail of O3122 Combined Effect of Bone Morphogenetic PROTEIN-2 Gene Therapy and Bioactive Glass Microspheres in Enhancement of New Bone Formation

Orthopaedic Proceedings, Mar 1, 2004

Aims: The present study examined the effect of ade-novirus-mediated recombinant human BMP-2 (RAd-... more Aims: The present study examined the effect of ade-novirus-mediated recombinant human BMP-2 (RAd-BMP-2) gene therapy combined with bioactive glass (BG) microspheres in promotion of new bone formation. Methods: Harlan Dawley female rats (n=72) underwent unilateral surgery of right or left tibia in a random order. A round cortical window ( − 2.8 mm) was drilled into the anteromedial cortex of the proximal tibia. A smaller unicortical hole ( − 1.0 mm) was drilled 5 mm distally. Bone marrow was removed and the medullary space between the cortical holes was þlled with BG microspheres. Adenoviral vectors RAdBMP-2 carrying the BMP-2 gene or RAdLacZ harbouring the E. coli LacZ reporter gene were injected locally into the medullary spaces. The control defects were þlled with BG microspheres only. Empty control defects were left to heal without any þlling. The rats were killed 4 days, 2 and 8 weeks after surgery and the tibias were harvested for analyses. At each time point, six animals were used for pQCT, radiography, BEI-SEM and histomorphometric analyses. Results: All BG-þlled defects showed a time-related increase of intramedullary new bone. At 8 weeks, there was signiþcantly more new bone in defects treated with BG and RAdBMP-2 gene than in defects left to heal without þlling (p=0.003) (BG + RAdBMP-2: 25.0 ± 6.0% and empty control defects: 12.3 ± 3.8%). Also defects þlled with BG only showed higher new bone formation than empty control defects, but this was not statistically signiþcant (p=0.10) (BG: 19.9 ± 7.3%). Conclusions: The current study showed that local BMP-2 gene therapy enhances new bone formation on bioactive glass microspheres.

Research paper thumbnail of Progress in Studies on Experimental Silicosis and in the Characterization of the Fibrogenic Factor

We have suggested that the development of silicosis is based on an increased amount of RNA in mul... more We have suggested that the development of silicosis is based on an increased amount of RNA in multiplied fibroblasts with consequently enhanced synthesis of several proteins including collagen (Kulonen et al. 1983 b, 1984). The increase of mRNA (Lehtinen et al. 1983) may depend either on transcriptional control regulated by the fibrogenic factor or on a decreased breakdown and lengthened life of the mRNA molecules (Kulonen et al. 1983 a). The specific target of the fibrogenic factor, whether transcriptional or translational, is not known.

Research paper thumbnail of Identification of messenger RNA for human type II collagen

FEBS Letters, Sep 3, 1984

Research paper thumbnail of Localizing, ordering and orienting mouse collagen genes by high resolution FISH

Research paper thumbnail of Mouse type II collagen gene. Complete nucleotide sequence, exon structure, and alternative splicing

Journal of Biological Chemistry, 1991

Several overlapping clones covering the entire mouse type II collagen gene including 10 kilobases... more Several overlapping clones covering the entire mouse type II collagen gene including 10 kilobases (kb) of 5&#39;- and 15 kb of 3&#39;-flanking sequences were isolated from a cosmid library. The overall gene structure was determined by restriction mapping and sequencing. The gene spans 28.9 kb from the start of transcription to the polyadenylation site and contains 54 exons. It codes for a major mRNA species of 4910 bases which translates into a polypeptide of 1419 amino acids. A less abundant RNA species of 5110 bases contains additional sequences corresponding to an alternatively spliced exon 2. Except for the amino-terminal propeptide (N-propeptide) domain the exon-intron organization of the mouse pro alpha 1(II) collagen gene is remarkably similar to genes for other fibrillar collagen types. The overall identity of the coding sequences of the mouse and human type II collagen genes is 89% at the nucleotide level, but only 37 amino acid changes occur within the mature alpha 1(II) collagen chains between mouse and man. Intron sizes are also conserved between the mouse and human genes but not with the chick alpha 1(II) gene. The promoter of the mouse type II collagen gene is similar to those of the rat and human genes containing a TATA box and several G + C-rich elements but no CCAAT box. The 3&#39;-untranslated sequence contains two regions of high homology between chick, mouse, bovine, and human genes preceding the major polyadenylation site. Additional size variation in the mRNA arises from the use of a minor polyadenylation signal. Information on conserved noncoding sequences will help in studies on the regulation of the pro alpha 1(II) collagen gene. Detailed knowledge of the gene is also necessary for site-directed mutagenesis and work with transgenic mice.

Research paper thumbnail of Roadmap for a precision-medicine initiative in the Nordic region

Research paper thumbnail of Biobanks: Balancing Benefits and Risks

Advancing Global Bioethics, 2016

Since its creation in 1993, the International Bioethics Committee (IBC) of UNESCO has been active... more Since its creation in 1993, the International Bioethics Committee (IBC) of UNESCO has been actively involved both in analysing bioethical problems and in proposing related guidelines. Currently IBC is focusing on a number of bioethical problems in the rapidly changing world of biomedical research. The purpose of this chapter is to review the progress in biobanking of human specimens and their high-throughput analysis into data. Biobanks are becoming repositories of human genetic material and data and thereby play an important role in the advancement of human health and in research and development in life sciences and biomedicine. More importantly, systematic collection of human samples and data provides the basis for better stratification of diseases, for development of personalized medicine and for development of health policies throughout the world. However, availability of biobanked samples and derived genetic data may also create problems concerning informed consent, incidental (unsolicited) findings and privacy, which have also been discussed by IBC.

Research paper thumbnail of Construction and partial characterization of two recombinant cDNA clones for procollagen from chicken cartilage

Nucleic Acids Research, 1982

Research paper thumbnail of Co-expression of collagens II and XI and alternative splicing of exon 2 of collagen II in several developing human tissues

Biochemical Journal, Sep 1, 1993

Research paper thumbnail of Epidermal growth factor increases collagen production in granulation tissue by stimulation of fibroblast proliferation and not by activation of procollagen genes

Biochemical Journal, Oct 15, 1987

Research paper thumbnail of Localization of types I, II, and III collagen mRNAs in developing human skeletal tissues by in situ hybridization

Journal of Cell Biology, Apr 1, 1987

Research paper thumbnail of Conservation of the sizes of 53 introns and over 100 intronic sequences for the binding of common transcription factors in the human and mouse genes for type II procollagen (COL2A1)

Biochemical Journal, Jun 15, 1995

Research paper thumbnail of The mouse collagen X gene: complete nucleotide sequence, exon structure and expression pattern

Biochemical Journal, 1993

Research paper thumbnail of Construction and Partial Characterization of Recombinant cDNA Clones for Chicken Type I Collagen Messenger RNAs

Acta Chemica Scandinavica, 1984

Research paper thumbnail of Construction and identification of a cDNA clone for human type II procollagen mRNA

Biochemical Journal, Jul 1, 1985

Research paper thumbnail of Mice With a Deletion in the First Intron of the <i>Col1a1</i> Gene Develop Age-Dependent Aortic Dissection and Rupture

Circulation Research, Jan 9, 2004

Research paper thumbnail of Expression of mRNAs coding for the alpha 1 chain of type XIII collagen in human fetal tissues: comparison with expression of mRNAs for collagen types I, II, and III

Journal of Cell Biology, Sep 1, 1989

Research paper thumbnail of Tissue inhibitor of metalloproteinases 4 (TIMP4) is involved in inflammatory processes of human cardiovascular pathology

Histochemistry and Cell Biology, Mar 7, 2006

Research paper thumbnail of Abnormal Mitochondria in Cultured Synovial Fibroblasts in Rheumatoid and Reactive Arthritis?

Rheumatology, Aug 18, 1988

This paper summarizes our recent studies on synovial fibroblast cultures started from patients wi... more This paper summarizes our recent studies on synovial fibroblast cultures started from patients with rheumatoid or reactive arthritis and from healthy controls. Analysis of these cultures by flow cytometry, spectroscopy and electron microscopy revealed consistent differences between arthritic and normal fibroblasts. Increased autofluorescence, exceptional light scatter properties, rhodamine-123 staining and electron microscopic findings of fibroblasts from arthritis patients suggest involvement of mitochondria in the disease process. Conditioned media of activated monocytes induced in the mitochondria of normal synovial fibroblasts changes similar to those observed in the fibroblasts originating from patients with rheumatoid or reactive arthritis.

Research paper thumbnail of Plasma membranes from experimental granulation tissue

Biochemical Journal, Mar 1, 1975

Research paper thumbnail of O3122 Combined Effect of Bone Morphogenetic PROTEIN-2 Gene Therapy and Bioactive Glass Microspheres in Enhancement of New Bone Formation

Orthopaedic Proceedings, Mar 1, 2004

Aims: The present study examined the effect of ade-novirus-mediated recombinant human BMP-2 (RAd-... more Aims: The present study examined the effect of ade-novirus-mediated recombinant human BMP-2 (RAd-BMP-2) gene therapy combined with bioactive glass (BG) microspheres in promotion of new bone formation. Methods: Harlan Dawley female rats (n=72) underwent unilateral surgery of right or left tibia in a random order. A round cortical window ( − 2.8 mm) was drilled into the anteromedial cortex of the proximal tibia. A smaller unicortical hole ( − 1.0 mm) was drilled 5 mm distally. Bone marrow was removed and the medullary space between the cortical holes was þlled with BG microspheres. Adenoviral vectors RAdBMP-2 carrying the BMP-2 gene or RAdLacZ harbouring the E. coli LacZ reporter gene were injected locally into the medullary spaces. The control defects were þlled with BG microspheres only. Empty control defects were left to heal without any þlling. The rats were killed 4 days, 2 and 8 weeks after surgery and the tibias were harvested for analyses. At each time point, six animals were used for pQCT, radiography, BEI-SEM and histomorphometric analyses. Results: All BG-þlled defects showed a time-related increase of intramedullary new bone. At 8 weeks, there was signiþcantly more new bone in defects treated with BG and RAdBMP-2 gene than in defects left to heal without þlling (p=0.003) (BG + RAdBMP-2: 25.0 ± 6.0% and empty control defects: 12.3 ± 3.8%). Also defects þlled with BG only showed higher new bone formation than empty control defects, but this was not statistically signiþcant (p=0.10) (BG: 19.9 ± 7.3%). Conclusions: The current study showed that local BMP-2 gene therapy enhances new bone formation on bioactive glass microspheres.

Research paper thumbnail of Progress in Studies on Experimental Silicosis and in the Characterization of the Fibrogenic Factor

We have suggested that the development of silicosis is based on an increased amount of RNA in mul... more We have suggested that the development of silicosis is based on an increased amount of RNA in multiplied fibroblasts with consequently enhanced synthesis of several proteins including collagen (Kulonen et al. 1983 b, 1984). The increase of mRNA (Lehtinen et al. 1983) may depend either on transcriptional control regulated by the fibrogenic factor or on a decreased breakdown and lengthened life of the mRNA molecules (Kulonen et al. 1983 a). The specific target of the fibrogenic factor, whether transcriptional or translational, is not known.

Research paper thumbnail of Identification of messenger RNA for human type II collagen

FEBS Letters, Sep 3, 1984

Research paper thumbnail of Localizing, ordering and orienting mouse collagen genes by high resolution FISH

Research paper thumbnail of Mouse type II collagen gene. Complete nucleotide sequence, exon structure, and alternative splicing

Journal of Biological Chemistry, 1991

Several overlapping clones covering the entire mouse type II collagen gene including 10 kilobases... more Several overlapping clones covering the entire mouse type II collagen gene including 10 kilobases (kb) of 5&#39;- and 15 kb of 3&#39;-flanking sequences were isolated from a cosmid library. The overall gene structure was determined by restriction mapping and sequencing. The gene spans 28.9 kb from the start of transcription to the polyadenylation site and contains 54 exons. It codes for a major mRNA species of 4910 bases which translates into a polypeptide of 1419 amino acids. A less abundant RNA species of 5110 bases contains additional sequences corresponding to an alternatively spliced exon 2. Except for the amino-terminal propeptide (N-propeptide) domain the exon-intron organization of the mouse pro alpha 1(II) collagen gene is remarkably similar to genes for other fibrillar collagen types. The overall identity of the coding sequences of the mouse and human type II collagen genes is 89% at the nucleotide level, but only 37 amino acid changes occur within the mature alpha 1(II) collagen chains between mouse and man. Intron sizes are also conserved between the mouse and human genes but not with the chick alpha 1(II) gene. The promoter of the mouse type II collagen gene is similar to those of the rat and human genes containing a TATA box and several G + C-rich elements but no CCAAT box. The 3&#39;-untranslated sequence contains two regions of high homology between chick, mouse, bovine, and human genes preceding the major polyadenylation site. Additional size variation in the mRNA arises from the use of a minor polyadenylation signal. Information on conserved noncoding sequences will help in studies on the regulation of the pro alpha 1(II) collagen gene. Detailed knowledge of the gene is also necessary for site-directed mutagenesis and work with transgenic mice.

Research paper thumbnail of Roadmap for a precision-medicine initiative in the Nordic region

Research paper thumbnail of Biobanks: Balancing Benefits and Risks

Advancing Global Bioethics, 2016

Since its creation in 1993, the International Bioethics Committee (IBC) of UNESCO has been active... more Since its creation in 1993, the International Bioethics Committee (IBC) of UNESCO has been actively involved both in analysing bioethical problems and in proposing related guidelines. Currently IBC is focusing on a number of bioethical problems in the rapidly changing world of biomedical research. The purpose of this chapter is to review the progress in biobanking of human specimens and their high-throughput analysis into data. Biobanks are becoming repositories of human genetic material and data and thereby play an important role in the advancement of human health and in research and development in life sciences and biomedicine. More importantly, systematic collection of human samples and data provides the basis for better stratification of diseases, for development of personalized medicine and for development of health policies throughout the world. However, availability of biobanked samples and derived genetic data may also create problems concerning informed consent, incidental (unsolicited) findings and privacy, which have also been discussed by IBC.