The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Kuniyoshi Shimakura - One of the best experts on this subject based on the ideXlab platform.
-
sarcoplasmic calcium binding Protein identification as a new allergen of the black tiger shrimp penaeus monodon
International Archives of Allergy and Immunology, 2008Co-Authors: Kazuo Shiomi, Yuichiro Sato, Shohei Hamamoto, Hajime Mita, Kuniyoshi ShimakuraAbstract:Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic Calcium-Binding Protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa Protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa Protein, suggesting the 20-kDa Protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.
-
sarcoplasmic calcium binding Protein identification as a new allergen of the black tiger shrimp penaeus monodon
International Archives of Allergy and Immunology, 2008Co-Authors: Kazuo Shiomi, Yuichiro Sato, Shohei Hamamoto, Hajime Mita, Kuniyoshi ShimakuraAbstract:Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic Calcium-Binding Protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa Protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa Protein, suggesting the 20-kDa Protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.
Kazuo Shiomi - One of the best experts on this subject based on the ideXlab platform.
-
sarcoplasmic calcium binding Protein identification as a new allergen of the black tiger shrimp penaeus monodon
International Archives of Allergy and Immunology, 2008Co-Authors: Kazuo Shiomi, Yuichiro Sato, Shohei Hamamoto, Hajime Mita, Kuniyoshi ShimakuraAbstract:Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic Calcium-Binding Protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa Protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa Protein, suggesting the 20-kDa Protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.
-
sarcoplasmic calcium binding Protein identification as a new allergen of the black tiger shrimp penaeus monodon
International Archives of Allergy and Immunology, 2008Co-Authors: Kazuo Shiomi, Yuichiro Sato, Shohei Hamamoto, Hajime Mita, Kuniyoshi ShimakuraAbstract:Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic Calcium-Binding Protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa Protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa Protein, suggesting the 20-kDa Protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.
Wen Guo Jiang - One of the best experts on this subject based on the ideXlab platform.
-
Calcium-Binding Protein S100P Promotes Tumor Progression but Enhances Chemosensitivity in Breast Cancer.
Frontiers in oncology, 2020Co-Authors: Yizi Cong, Yuxin Cui, Suxia Wang, Lei Jiang, Jianqiao Cao, Shiguang Zhu, Emily Birkin, Jane Lane, Fiona Ruge, Wen Guo JiangAbstract:Background: Chemoresistance remains one of the obstacles to overcome in the treatment of breast cancer. S100 Calcium-Binding Protein P (S100P) has been observed to be overexpressed in several cancers and has been associated with drug resistance, metastasis, and prognosis. However, the role of S100P in chemoresistance in breast cancer has not been thoroughly determined. Methods: Immunohistochemistry was used to evaluate the expression level of S100P Protein in 22 pairs (pre-chemo and post-chemo) of breast cancer tissue from patients who underwent neoadjuvant chemotherapy. The influence of S100P on the biological behavior and chemosensitivity of breast cancer cells was then investigated. Results: The Protein level of S100P in breast cancer tissue was significantly higher than in benign fibroadenoma (p
-
calcium binding Protein s100p promotes tumor progression but enhances chemosensitivity in breast cancer
Frontiers in Oncology, 2020Co-Authors: Yizi Cong, Yuxin Cui, Suxia Wang, Lei Jiang, Jianqiao Cao, Shiguang Zhu, Emily Birkin, Jane Lane, Fiona Ruge, Wen Guo JiangAbstract:Background: Chemoresistance remains one of the obstacles to overcome in the treatment of breast cancer. S100 Calcium-Binding Protein P (S100P) has been observed to be overexpressed in several cancers and has been associated with drug resistance, metastasis, and prognosis. However, the role of S100P in chemoresistance in breast cancer has not been thoroughly determined. Methods: Immunohistochemistry was used to evaluate the expression level of S100P Protein in 22 pairs (pre-chemo and post-chemo) of breast cancer tissue from patients who underwent neoadjuvant chemotherapy. The influence of S100P on the biological behavior and chemosensitivity of breast cancer cells was then investigated. Results: The Protein level of S100P in breast cancer tissue was significantly higher than in benign fibroadenoma (p<0.001). The S100P expression level was shown to be decreased by 46.55% after neoadjuvant chemotherapy (p=0.015). Subgroup analysis revealed that S100P reduction (57.58%) was mainly observed in the HER2+ tumors (p=0.027). Our in-vitro experiments showed that the knockdown of S100P suppressed the proliferation, adhesion, migration and invasion abilities of T47D and SK-BR-3 breast cancer cells. We further demonstrated that this knockdown increased the chemoresistance to paclitaxel and cisplatin in SK-BR-3 cells. We found that S100P exerted its function by activating NF-κB, CCND1 and Vimentin, but downregulating E-cadherin. Conclusions: S100P promotes the aggressive properties of breast cancer cells and may be considered as a promising therapeutic target. Moreover, S100P can be used to predict the therapeutic effect of chemotherapy in HER2+ breast cancer patients.
Hajime Mita - One of the best experts on this subject based on the ideXlab platform.
-
sarcoplasmic calcium binding Protein identification as a new allergen of the black tiger shrimp penaeus monodon
International Archives of Allergy and Immunology, 2008Co-Authors: Kazuo Shiomi, Yuichiro Sato, Shohei Hamamoto, Hajime Mita, Kuniyoshi ShimakuraAbstract:Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic Calcium-Binding Protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa Protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa Protein, suggesting the 20-kDa Protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.
-
sarcoplasmic calcium binding Protein identification as a new allergen of the black tiger shrimp penaeus monodon
International Archives of Allergy and Immunology, 2008Co-Authors: Kazuo Shiomi, Yuichiro Sato, Shohei Hamamoto, Hajime Mita, Kuniyoshi ShimakuraAbstract:Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic Calcium-Binding Protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa Protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa Protein, suggesting the 20-kDa Protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.
Shohei Hamamoto - One of the best experts on this subject based on the ideXlab platform.
-
sarcoplasmic calcium binding Protein identification as a new allergen of the black tiger shrimp penaeus monodon
International Archives of Allergy and Immunology, 2008Co-Authors: Kazuo Shiomi, Yuichiro Sato, Shohei Hamamoto, Hajime Mita, Kuniyoshi ShimakuraAbstract:Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic Calcium-Binding Protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa Protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa Protein, suggesting the 20-kDa Protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.
-
sarcoplasmic calcium binding Protein identification as a new allergen of the black tiger shrimp penaeus monodon
International Archives of Allergy and Immunology, 2008Co-Authors: Kazuo Shiomi, Yuichiro Sato, Shohei Hamamoto, Hajime Mita, Kuniyoshi ShimakuraAbstract:Background: Tropomyosin and arginine kinase have been identified as crustacean allergens. During purification of arginine kinase from black tiger shrimp Penaeus monodon, we found a new allergen of 20-kDa. Methods: A 20-kDa allergen was purified from the abdominal muscle of black tiger shrimp by salting-out, anion-exchange HPLC and reverse-phase HPLC. Following digestion of the 20-kDa allergen with lysyl endopeptidase, peptide fragments were isolated by reverse-phase HPLC, and 2 of them were sequenced. The 20-kDa allergen, together with tropomyosin and arginine kinase purified from black tiger shrimp, was evaluated for IgE reactivity by ELISA. Five species of crustaceans (kuruma shrimp, American lobster, pink shrimp, king crab and snow crab) were surveyed for the 20-kDa allergen by immunoblotting. Results: The 20-kDa allergen was purified from black tiger shrimp and identified as a sarcoplasmic Calcium-Binding Protein (SCP) based on the determined amino acid sequences of 2 enzymatic fragments. Of 16 sera from crustacean-allergic patients, 8 and 13 reacted to SCP and tropomyosin, respectively; the reactivity to arginine kinase was weakly recognized with 10 sera. In immunoblotting, an IgE-reactive 20-kDa Protein was also detected in kuruma shrimp, American lobster and pink shrimp but not in 2 species of crab. Preadsorption of the sera with black tiger shrimp SCP abolished the IgE reactivity of the 20-kDa Protein, suggesting the 20-kDa Protein to be an SCP. Conclusions: SCP is a new crustacean allergen, and distribution of IgE-reactive SCP is probably limited to shrimp and crayfish.
