The Experts below are selected from a list of 1785 Experts worldwide ranked by ideXlab platform
Akira Ishibashi - One of the best experts on this subject based on the ideXlab platform.
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immunohistochemical detection of lipid peroxidation products protein bound acrolein and 4 hydroxynonenal protein adducts in actinic Elastosis of photodamaged skin
2001Co-Authors: Nobuhiko Tanaka, Shingo Tajima, Akira Ishibashi, Koji Uchida, Takeshi ShigematsuAbstract:Acrolein and 4-hydroxy-2-nonenal (HNE) are both byproducts of a lipid peroxidation reaction. Actinic Elastosis in photodamaged skin of aged individuals is characterized by the accumulation of fragmented elastic fibers in the sun-exposed areas. To study whether a lipid peroxidation reaction is involved in the accumulation of altered elastic fibers in actinic Elastosis, skin specimens obtained from sun-damaged areas were immunohistochemically examined using the antibodies against acrolein and HNE. Both antibodies were found to react with the accumulations of elastic material. Double immunofluorescence labeling demonstrated that acrolein/elastin and HNE/elastin were colocalized in the actinic Elastosis. Western blot analysis showed that the polypeptide with a molecular weight of 62 kDa reacted with anti-acrolein, anti-HNE and anti-elastin antibodies. The results suggest that acrolein and HNE may be associated with actinic Elastosis.
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elastin peptides induce migration and terminal differentiation of cultured keratinocytes via 67 kda elastin receptor in vitro 67 kda elastin receptor is expressed in the keratinocytes eliminating elastic materials in Elastosis perforans serpiginosa
2000Co-Authors: Norihiro Fujimoto, Shingo Tajima, Akira IshibashiAbstract:To delineate the molecular mechanism of transepidermal elimination of dermal elastic materials in Elastosis perforans serpiginosa, the interaction between elastin and cultured keratinocytes was studied in vitro . Synthetic elastin peptide VGVAPG elicited chemotactic responses to the cultured keratinocytes at the dose of 10 −9 M. Treatment of keratinocytes with 10 −6 or 10 −5 M elastin peptides resulted in the suppression of cell growth and the increased expression of involucrin and transglutaminase-1, markers of terminal differentiation. When cultured keratinocytes were treated with the elastin peptides, the expression of 67 kDa elastin receptor was increased. The induction of terminal differentiation by elastin peptides was attenuated by the treatment with the combination of anti-67 kDa elastin receptor antibody. The results indicate that elastin is a potent inducer of migration and terminal differentiation of cultured keratinocytes, which is mediated by the 67 kDa elastin receptor. In the lesional skins of patients with Elastosis perforans serpiginosa, the 67 kDa elastin receptor was specifically expressed in the epidermis immediately surrounding the elastic materials that were being eliminated. The elastin receptor may be involved in the interaction between keratinocytes and elastin in Elastosis perforans serpiginosa.
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expression of elastin related proteins and matrix metalloproteinases in actinic Elastosis of sun damaged skin
2000Co-Authors: Y Ohnishi, Shingo Tajima, Akira Ishibashi, Minoru Akiyama, Ryoji Kobayashi, I HoriiAbstract:Actinic Elastosis is characterized by an accumulation of elastotic material in the upper dermis and is considered to be a manifestation of ultraviolet-induced skin aging. To compare the structural components of the elastotic material in actinic Elastosis with those in normal skin, skin specimens were stained with antibodies raised against various elastin-related proteins. Elastotic materials exhibited a strong reaction to the antibodies for elastin, microfibril-associated glycoprotein-1 (MAGP-1), MAGP-4, matrix metalloproteinase 1 (MMP-1), MMP-2 and MMP-3, but a diminished reaction to anti-MMP-9 antibody. Fibroblast cell lines from the upper dermis of affected and unaffected skin were established, and the mRNA levels of MMPs were determined. MMP-1 and -2 mRNA levels were found to be elevated approximately twofold in the fibroblasts from actinic Elastosis. Since MMP-1 and -2 are considered to be major enzymes involved in the degradation of matrix components, the accumulation of elastotic materials in actinic Elastosis may be related to the degradation process.
Mary Seabury Stone - One of the best experts on this subject based on the ideXlab platform.
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penicillamine induced Elastosis of the mucosal lip
2009Co-Authors: Bethany K H Lewis, Peggy L Chern, Mary Seabury StoneAbstract:Long-term penicillamine therapy has been associated with alterations in dermal elastic tissue. Well-described associated dermatoses include pseudo-pseudoxanthoma elasticum, acquired cutis laxa, Elastosis perforans serpiginosa, and anetoderma. Histologically, "lumpy-bumpy"" or "bramble-bush"" morphologic changes of elastic fibers in the dermis are characteristic. Previous reports of these findings in normal-appearing skin and internal organs suggest a systemic elastolytic process. Here we report an unusual case of penicillamine-induced Elastosis affecting the mucosa of the lip with characteristic histologic features.
Shingo Tajima - One of the best experts on this subject based on the ideXlab platform.
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ne carboxymethyl lysine modification of elastin alters its biological properties implications for the accumulation of abnormal elastic fibers in actinic Elastosis
2012Co-Authors: Elastosis Yoshinaga, Akira Kawada, Koji Ono, Eita Fujimoto, Hiroshi Wachi, Satoru Harumiya, Ryoji Nagai, Shingo TajimaAbstract:Accumulation of degenerated elastic fibers in the sun-exposed skin designated as actinic Elastosis is a histological hallmark of photodamaged skin. Previous studies have indicated that the elastic fibers of actinic Elastosis interact with lysozyme and are modified by Ne-(carboxymethyl)lysine (CML), one of the major advanced glycation end products (AGEs). We studied here how CML modification of elastin is involved in the pathogenesis of actinic Elastosis. The CML-modified insoluble elastin became resistant to neutrophil elastase digestion, which was reversed by treatment with aminoguanidine, a potent inhibitor of AGE formation. In a temperature-dependent aggregation assay, CML-modified elastin rapidly formed self-aggregates, the size of which was larger than unmodified elastin. The elastic fiber sheets prepared from CML-modified α-elastin showed 3D wider diameter, tortuous appearance, and decreased elasticity on tensile tests. The CML-modified α-elastin, but not unmodified α-elastin, was found to bind to lysozyme in vitro, supporting the immunohistochemical findings that the antibodies for lysozyme and CML reacted simultaneously with the elastic fibers of actinic Elastosis and UV-irradiated skin. The glycated elastin is likely to cause the accumulation of abnormally aggregated elastic fibers and unusual interaction with lysozyme in actinic Elastosis.
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immunohistochemical detection of lipid peroxidation products protein bound acrolein and 4 hydroxynonenal protein adducts in actinic Elastosis of photodamaged skin
2001Co-Authors: Nobuhiko Tanaka, Shingo Tajima, Akira Ishibashi, Koji Uchida, Takeshi ShigematsuAbstract:Acrolein and 4-hydroxy-2-nonenal (HNE) are both byproducts of a lipid peroxidation reaction. Actinic Elastosis in photodamaged skin of aged individuals is characterized by the accumulation of fragmented elastic fibers in the sun-exposed areas. To study whether a lipid peroxidation reaction is involved in the accumulation of altered elastic fibers in actinic Elastosis, skin specimens obtained from sun-damaged areas were immunohistochemically examined using the antibodies against acrolein and HNE. Both antibodies were found to react with the accumulations of elastic material. Double immunofluorescence labeling demonstrated that acrolein/elastin and HNE/elastin were colocalized in the actinic Elastosis. Western blot analysis showed that the polypeptide with a molecular weight of 62 kDa reacted with anti-acrolein, anti-HNE and anti-elastin antibodies. The results suggest that acrolein and HNE may be associated with actinic Elastosis.
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elastin peptides induce migration and terminal differentiation of cultured keratinocytes via 67 kda elastin receptor in vitro 67 kda elastin receptor is expressed in the keratinocytes eliminating elastic materials in Elastosis perforans serpiginosa
2000Co-Authors: Norihiro Fujimoto, Shingo Tajima, Akira IshibashiAbstract:To delineate the molecular mechanism of transepidermal elimination of dermal elastic materials in Elastosis perforans serpiginosa, the interaction between elastin and cultured keratinocytes was studied in vitro . Synthetic elastin peptide VGVAPG elicited chemotactic responses to the cultured keratinocytes at the dose of 10 −9 M. Treatment of keratinocytes with 10 −6 or 10 −5 M elastin peptides resulted in the suppression of cell growth and the increased expression of involucrin and transglutaminase-1, markers of terminal differentiation. When cultured keratinocytes were treated with the elastin peptides, the expression of 67 kDa elastin receptor was increased. The induction of terminal differentiation by elastin peptides was attenuated by the treatment with the combination of anti-67 kDa elastin receptor antibody. The results indicate that elastin is a potent inducer of migration and terminal differentiation of cultured keratinocytes, which is mediated by the 67 kDa elastin receptor. In the lesional skins of patients with Elastosis perforans serpiginosa, the 67 kDa elastin receptor was specifically expressed in the epidermis immediately surrounding the elastic materials that were being eliminated. The elastin receptor may be involved in the interaction between keratinocytes and elastin in Elastosis perforans serpiginosa.
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expression of elastin related proteins and matrix metalloproteinases in actinic Elastosis of sun damaged skin
2000Co-Authors: Y Ohnishi, Shingo Tajima, Akira Ishibashi, Minoru Akiyama, Ryoji Kobayashi, I HoriiAbstract:Actinic Elastosis is characterized by an accumulation of elastotic material in the upper dermis and is considered to be a manifestation of ultraviolet-induced skin aging. To compare the structural components of the elastotic material in actinic Elastosis with those in normal skin, skin specimens were stained with antibodies raised against various elastin-related proteins. Elastotic materials exhibited a strong reaction to the antibodies for elastin, microfibril-associated glycoprotein-1 (MAGP-1), MAGP-4, matrix metalloproteinase 1 (MMP-1), MMP-2 and MMP-3, but a diminished reaction to anti-MMP-9 antibody. Fibroblast cell lines from the upper dermis of affected and unaffected skin were established, and the mRNA levels of MMPs were determined. MMP-1 and -2 mRNA levels were found to be elevated approximately twofold in the fibroblasts from actinic Elastosis. Since MMP-1 and -2 are considered to be major enzymes involved in the degradation of matrix components, the accumulation of elastotic materials in actinic Elastosis may be related to the degradation process.
Bethany K H Lewis - One of the best experts on this subject based on the ideXlab platform.
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penicillamine induced Elastosis of the mucosal lip
2009Co-Authors: Bethany K H Lewis, Peggy L Chern, Mary Seabury StoneAbstract:Long-term penicillamine therapy has been associated with alterations in dermal elastic tissue. Well-described associated dermatoses include pseudo-pseudoxanthoma elasticum, acquired cutis laxa, Elastosis perforans serpiginosa, and anetoderma. Histologically, "lumpy-bumpy"" or "bramble-bush"" morphologic changes of elastic fibers in the dermis are characteristic. Previous reports of these findings in normal-appearing skin and internal organs suggest a systemic elastolytic process. Here we report an unusual case of penicillamine-induced Elastosis affecting the mucosa of the lip with characteristic histologic features.
Seikoh Horiuchi - One of the best experts on this subject based on the ideXlab platform.
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photo enhanced modification of human skin elastin in actinic Elastosis by n carboxymethyl lysine one of the glycoxidation products of the maillard reaction
1997Co-Authors: Kumiko Mizutari, Kazuyoshi Ikeda, Kenichi Kayashima, Seikoh HoriuchiAbstract:Long-term incubation of proteins with glucose leads to the formation of advanced glycation end products (AGEs), which are characterized by fluorescence, brown color, and cross-linking. Formation of AGEs in vitro requires oxygen and is dependent on transition metal-catalyzed oxidation of glucose or Amadori products. AGEs are thought to be involved in aging and age-enhanced diseases such as diabetic complications, atherosclerosis, dialysis-related amyloidosis, and Alzheimer's disease. Chronic exposure of the skin to sunlight induces hyperplasia of the elastic tissue in the upper dermis known as actinic Elastosis. Herein we used a monoclonal anti-AGE antibody (6D12) whose epitope is N ∈ -(carboxymethyl)lysine (CML), one of the glycoxidation products of AGEs, and demonstrated that the lesions of actinic Elastosis were modified by CML. Further immunohistochenilcal and immunoelectron microscopic examination with 6D12 demonstrated CML accumulates predominantly in elastic fibers especially in the amorphous electron-dense materials corresponding to photo-induced degenerated area rather than the electron-lucent region. Immunochemical analyses with enzyme-linked immunosorbent assay (ELISA) of elastase-soluble fractions demonstrated that the CML levels of the sun-exposed area were significantly higher than those of the sun-unexposed area. We conclude that ultraviolet-induced oxidation may accelerate CML formation in actinic Elastosis of photoaged skin.
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photo enhanced modification of human skin elastin in actinic Elastosis by n epsilon carboxymethyl lysine one of the glycoxidation products of the maillard reaction
1997Co-Authors: Kumiko Mizutari, Kazuyoshi Ikeda, Kenichi Kayashima, Tomomichi Ono, Seikoh HoriuchiAbstract:Long-term incubation of proteins with glucose leads to the formation of advanced glycation end products (AGEs), which are characterized by fluorescence, brown color, and cross-linking. Formation of AGEs in vitro requires oxygen and is dependent on transition metal-catalyzed oxidation of glucose or Amadori products. AGEs are thought to be involved in aging and age-enhanced diseases such as diabetic complications, atherosclerosis, dialysis-related amyloidosis, and Alzheimer's disease. Chronic exposure of the skin to sunlight induces hyperplasia of the elastic tissue in the upper dermis known as actinic Elastosis. Herein we used a monoclonal anti-AGE antibody (6D12) whose epitope is N ∈ -(carboxymethyl)lysine (CML), one of the glycoxidation products of AGEs, and demonstrated that the lesions of actinic Elastosis were modified by CML. Further immunohistochenilcal and immunoelectron microscopic examination with 6D12 demonstrated CML accumulates predominantly in elastic fibers especially in the amorphous electron-dense materials corresponding to photo-induced degenerated area rather than the electron-lucent region. Immunochemical analyses with enzyme-linked immunosorbent assay (ELISA) of elastase-soluble fractions demonstrated that the CML levels of the sun-exposed area were significantly higher than those of the sun-unexposed area. We conclude that ultraviolet-induced oxidation may accelerate CML formation in actinic Elastosis of photoaged skin.
