15 results on '"Cong, Yi"'
Search Results
2. Fluvoxamine inhibits Th1 and Th17 polarization and function by repressing glycolysis to attenuate autoimmune progression in type 1 diabetes
- Author
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Zou, Yuan, Zhang, Jing, Sun, Fei, Xu, Qianqian, Chen, Longmin, Luo, Xi, Wang, Ting, Zhou, Qing, Zhang, Shu, Xiong, Fei, Kong, Wen, Yang, Ping, Yu, Qilin, Liu, Shiwei, and Wang, Cong-Yi
- Published
- 2024
- Full Text
- View/download PDF
3. Cigarette smoke extract stimulates bronchial epithelial cells to undergo a SUMOylation turnover
- Author
-
Zhou, Haifeng, Zhang, Lei, Li, Yang, Wu, Guorao, Zhu, He, Zhang, Huilan, Su, Jia-Kun, Guo, Lei, Zhou, Qing, Xiong, Fei, Yu, Qilin, Yang, Ping, Zhang, Shu, Cai, Jibao, and Wang, Cong-Yi
- Published
- 2020
- Full Text
- View/download PDF
4. Macrophages: friend or foe in idiopathic pulmonary fibrosis?
- Author
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Zhang, Lei, Wang, Yi, Wu, Guorao, Xiong, Weining, Gu, Weikuan, and Wang, Cong-Yi
- Published
- 2018
- Full Text
- View/download PDF
5. Aloperine Protects Mice against Ischemia-Reperfusion (IR)-Induced Renal Injury by Regulating PI3K/AKT/mTOR Signaling and AP-1 Activity
- Author
-
Hu, Shuang, Zhang, Yuxing, Zhang, Meng, Guo, Yanchao, Yang, Ping, Zhang, Shu, Simsekyilmaz, Sakine, Xu, Jun-Fa, Li, Jinxiu, Xiang, Xudong, Yu, Qilin, and Wang, Cong-Yi
- Published
- 2015
- Full Text
- View/download PDF
6. Macrophages: friend or foe in idiopathic pulmonary fibrosis?
- Author
-
Yi Wang, Weikuan Gu, Weining Xiong, Cong-Yi Wang, Guorao Wu, and Lei Zhang
- Subjects
0301 basic medicine ,Macrophage polarization ,Review ,Alternatively activated (M2) macrophages ,Lung injury ,03 medical and health sciences ,Idiopathic pulmonary fibrosis ,0302 clinical medicine ,Pulmonary fibrosis ,medicine ,Macrophage ,Animals ,Humans ,Classically activated (M1) macrophages ,lcsh:RC705-779 ,Lung ,business.industry ,Macrophages ,Interstitial lung disease ,lcsh:Diseases of the respiratory system ,respiratory system ,Macrophage Activation ,medicine.disease ,Idiopathic Pulmonary Fibrosis ,respiratory tract diseases ,030104 developmental biology ,medicine.anatomical_structure ,IPF ,030220 oncology & carcinogenesis ,Immunology ,Therapeutic strategies ,Wound healing ,business - Abstract
Idiopathic pulmonary fibrosis (IPF) is a prototype of lethal, chronic, progressive interstitial lung disease of unknown etiology. Over the past decade, macrophage has been recognized to play a significant role in IPF pathogenesis. Depending on the local microenvironments, macrophages can be polarized to either classically activated (M1) or alternatively activated (M2) phenotypes. In general, M1 macrophages are responsible for wound healing after alveolar epithelial injury, while M2 macrophages are designated to resolve wound healing processes or terminate inflammatory responses in the lung. IPF is a pathological consequence resulted from altered wound healing in response to persistent lung injury. In this review, we intend to summarize the current state of knowledge regarding the process of macrophage polarization and its mediators in the pathogenesis of pulmonary fibrosis. Our goal is to update the understanding of the mechanisms underlying the initiation and progression of IPF, and by which, we expect to provide help for developing effective therapeutic strategies in clinical settings.
- Published
- 2018
7. Generation and functional characterization of the anti-transferrin receptor single-chain antibody-GAL4 (TfRscFv-GAL4) fusion protein
- Author
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Shu Zhang, Heyu Hu, Zhi-Quan Hu, Jing Liu, Guanxin Shen, Tong Lu, Ping Lei, Zhang-Qun Ye, Xing Zeng, Cong-Yi Wang, Zhihua Wang, and Qing Ye
- Subjects
Protein Folding ,Saccharomyces cerevisiae Proteins ,lcsh:Biotechnology ,Recombinant Fusion Proteins ,Genetic Vectors ,Green Fluorescent Proteins ,Protein Renaturation ,Transferrin receptor ,Breast Neoplasms ,HL-60 Cells ,Saccharomyces cerevisiae ,Gene delivery ,Biology ,Inclusion bodies ,Green fluorescent protein ,Mice ,Stomach Neoplasms ,lcsh:TP248.13-248.65 ,Cell Line, Tumor ,Receptors, Transferrin ,Escherichia coli ,Animals ,Humans ,Transfection ,Hep G2 Cells ,Flow Cytometry ,Fusion protein ,Molecular biology ,DNA-Binding Proteins ,Tissue Array Analysis ,Cancer cell ,biology.protein ,MCF-7 Cells ,Female ,Antibody ,Biotechnology ,Research Article ,HeLa Cells ,Plasmids ,Single-Chain Antibodies ,Transcription Factors - Abstract
Background The development of vectors for cell-specific gene delivery is a major goal of gene therapeutic strategies. Transferrin receptor (TfR) is an endocytic receptor and identified as tumor relative specific due to its overexpression on most tumor cells or tissues, and TfR binds and intakes of transferrin-iron complex. We have previously generated an anti-TfR single-chain variable fragments of immunoglobulin (scFv) which were cloned from hybridoma cell line producing antibody against TfR linked with a 20 aa-long linker sequence (G4S)4. In the present study, the anti-TfR single-chain antibody (TfRscFv) was fused to DNA-binding domain of the yeast transcription factor GAL4. The recombinant fusion protein, designated as TfRscFv-GAL4, is expected to mediate the entry of DNA-protein complex into targeted tumor cells. Results Fusion protein TfRscFv-GAL4 was expressed in an E. coli bacterial expression system and was recovered from inclusion bodies with subsequent purification by metal-chelate chromatography. The resulting proteins were predominantly monomeric and, upon refolding, became a soluble biologically active bifunctional protein. In biological assays, the antigen-binding activity of the re-natured protein, TfRscFv-GAL4, was confirmed by specific binding to different cancer cells and tumor tissues. The cell binding rates, as indicated by flow cytometry (FCM) analysis, ranged from 54.11% to 8.23% in seven different human carcinoma cell lines. It showed similar affinity and binding potency as those of parent full-length mouse anti-TfR antibody. The positive binding rates to tumor tissues by tissue microarrays (TMA) assays were 75.32% and 63.25%, but it showed weakly binding with hepatic tissue in 5 cases, and normal tissues such as heart, spleen, adrenal cortex blood vessel and stomach. In addition, the re-natured fusion protein TfRscFv-GAL4 was used in an ELISA with rabbit anti-GAL4 antibody. The GAL4-DNA functional assay through the GAL4 complementary conjugation with the GAL4rec-GFP-pGes plasmid to verify the GLA4 activity and GAL4rec-recognized specificity functions. It also shows the complex, TfRscFv-GAL4-GAL4rec-GFP-pGes, could be taken into endochylema to express the green fluorescent protein (GFP) with 8 to 10-fold transfection efficiency. Conclusions Results of our study demonstrated that the biofunctianality of genetically engineered fusion protein, TfRscFv-GAL4, was retained, as the fusion protein could both carry the plasmid of GAL4rec-pGes and bind TfR on tumour cells. This product was able to transfect target cells effectively in an immuno-specific manner, resulting in transient gene expression. This protein that can be applied as an effective therapeutic and diagnostic delivery to the tumor using endogenous membrane transport system with potential widespread utility.
- Published
- 2012
8. Molecular cloning and characterization of the mouse Acdp gene family
- Author
-
Haiqian An, Ping Yang, Jianguo G. Gu, Jennifer Ling, Dehuang Guo, Jin-Xiong She, Jing Da Shi, Zheng Dong, Sharad Purohit, and Cong-Yi Wang
- Subjects
Male ,DNA, Complementary ,lcsh:QH426-470 ,Sequence analysis ,lcsh:Biotechnology ,Protein domain ,Blotting, Western ,Molecular Sequence Data ,Sequence alignment ,Biology ,PC12 Cells ,Homology (biology) ,Cell Line ,Mice ,Complementary DNA ,lcsh:TP248.13-248.65 ,Genetics ,Gene family ,Animals ,Humans ,Amino Acid Sequence ,Cloning, Molecular ,Gene ,Phylogeny ,Microscopy, Confocal ,Sequence Homology, Amino Acid ,Gene Expression Profiling ,Cell Membrane ,Brain ,Chromosome Mapping ,Membrane Proteins ,3T3 Cells ,Sequence Analysis, DNA ,Blotting, Northern ,Chromosomes, Mammalian ,Rats ,lcsh:Genetics ,Essential gene ,Multigene Family ,Carrier Proteins ,Sequence Alignment ,Biotechnology ,Research Article - Abstract
Background We have recently cloned and characterized a novel gene family named ancient conserved domain protein (ACDP) in humans. To facilitate the functional study of this novel gene family, we have cloned and characterized Acdp, the mouse homologue of the human ACDP gene family. Results The four Acdp genes (Acdp1, Acdp2, Acdp3 and Acdp4) contain 3,631 bp, 3,244 bp, 2,684 bp and 2,743 bp of cDNA sequences, and encode deduced proteins of 951, 874, 713 and 771 amino acids, respectively. The mouse Acdp genes showed very strong homologies (>90%) in both nucleotide and amino acid sequences to their human counterparts. In addition, both nucleotide and amino acid sequences within the Ancient Conserved Domain (ACD) are highly conserved in many different taxonomic species. Particularly, Acdp proteins showed very strong AA homologies to the bacteria CorC protein (35% AA identity with 55% homology), which is involved in magnesium and cobalt efflux. The Acdp genes are widely expressed in all tissues tested except for Acdp1, which is only highly expressed in the brain with low levels of expression in kidney and testis. Immunostaining of Acdp1 in hippocampus neurons revealed a predominant localization on the plasma membrane. Conclusion The Acdp genes are evolutionarily conserved in diverse species and ubiquitously expressed throughout development and adult tissues suggesting that Acdp may be an essential gene. Acdp showed strong homology to bacteria CorC protein and predominantly localized on the plasma membrane. These results suggest that Acdp is probably a family of proteins involved in ion transport in mammalian cells
- Published
- 2004
9. Comparative analysis of the alveolar macrophage proteome in ALI/ARDS patients between the exudative phase and recovery phase.
- Author
-
Haiyun Dong, Jinxiu Li, Youdi Lv, Yanyan Zhou, Guyi Wang, Shuang Hu, Xiaoyu He, Ping Yang, Zhiguang Zhou, Xudong Xiang, and Cong-Yi Wang
- Subjects
MACROPHAGES ,ANTIGEN presenting cells ,CONNECTIVE tissue cells ,KILLER cells ,PHAGOCYTES - Abstract
Background: Despite decades of extensive studies, the morbidity and mortality for acute lung injury/acute respiratory distress syndrome (ALI/ARDS) remained high. Particularly, biomarkers essential for its early diagnosis and prognosis are lacking. Methods: Recent studies suggest that alveolar macrophages (AMs) at the exudative phase of ALI/ARDS initiate, amplify and perpetuate inflammatory responses, while they resolve inflammation in the recovery phase to prevent further tissue injury and perpetuated inflammation in the lung. Therefore, proteins relevant to this functional switch could be valuable biomarkers for ALI/ARDS diagnosis and prognosis. We thus conducted comparative analysis of the AM proteome to assess its dynamic proteomic changes during ALI/ARDS progression and recovery. Results: 135 proteins were characterized to be differentially expressed between AMs at the exudative and recovery phase. MALDI-TOF-MS and peptide mass fingerprint (PMF) analysis characterized 27 informative proteins, in which 17 proteins were found with a marked increase at the recovery phase, while the rest of 10 proteins were manifested by the significantly higher levels of expression at the exudative phase. Conclusions: Given the role of above identified proteins played in the regulation of inflammatory responses, cell skeleton organization, oxidative stress, apoptosis and metabolism, they have the potential to serve as biomarkers for early diagnosis and prognosis in the setting of patients with ALI/ARDS. [ABSTRACT FROM AUTHOR]
- Published
- 2013
- Full Text
- View/download PDF
10. Generation and functional characterization of the anti-transferrin receptor single-chain antibody-GAL4 (TfRscFv-GAL4) fusion protein.
- Author
-
Ye, Qing, Hu, Heyu, Wang, Zhihua, Lu, Tong, Hu, Zhiquan, Zeng, Xing, Zhang, Shu, Liu, Jing, Lei, Ping, Wang, Cong-Yi, Ye, Zhangqun, and Shen, Guanxin
- Subjects
TRANSFERRIN receptors ,IMMUNOGLOBULINS ,HYBRIDOMAS ,TRANSCRIPTION factors ,FLOW cytometry ,CANCER cells - Abstract
Background: The development of vectors for cell-specific gene delivery is a major goal of gene therapeutic strategies. Transferrin receptor (TfR) is an endocytic receptor and identified as tumor relative specific due to its overexpression on most tumor cells or tissues, and TfR binds and intakes of transferrin-iron complex. We have previously generated an anti-TfR single-chain variable fragments of immunoglobulin (scFv) which were cloned from hybridoma cell line producing antibody against TfR linked with a 20 aa-long linker sequence (G4S)
4 . In the present study, the anti-TfR single-chain antibody (TfRscFv) was fused to DNA-binding domain of the yeast transcription factor GAL4. The recombinant fusion protein, designated as TfRscFv-GAL4, is expected to mediate the entry of DNA-protein complex into targeted tumor cells.Results: Fusion protein TfRscFv-GAL4 was expressed in an E. coli bacterial expression system and was recovered from inclusion bodies with subsequent purification by metal-chelate chromatography. The resulting proteins were predominantly monomeric and, upon refolding, became a soluble biologically active bifunctional protein. In biological assays, the antigen-binding activity of the re-natured protein, TfRscFv-GAL4, was confirmed by specific binding to different cancer cells and tumor tissues. The cell binding rates, as indicated by flow cytometry (FCM) analysis, ranged from 54.11% to 8.23% in seven different human carcinoma cell lines. It showed similar affinity and binding potency as those of parent full-length mouse anti-TfR antibody. The positive binding rates to tumor tissues by tissue microarrays (TMA) assays were 75.32% and 63.25%, but it showed weakly binding with hepatic tissue in 5 cases, and normal tissues such as heart, spleen, adrenal cortex blood vessel and stomach. In addition, there-natured fusion protein TfRscFv-GAL4 was used in an ELISA with rabbit anti-GAL4 antibody. The GAL4-DNA functional assay through the GAL4 complementary conjugation with the GAL4rec-GFP-pGes plasmid to verify the GLA4 activity and GAL4rec-recognized specificity functions. It also shows the complex, TfRscFv-GAL4-GAL4rec-GFPpGes, could be taken into endochylema to express the green fluorescent protein (GFP) with 8 to 10-fold transfection efficiency.Conclusions: Results of our study demonstrated that the biofunctianality of genetically engineered fusion protein,TfRscFv-GAL4, was retained, as the fusion protein could both carry the plasmid of GAL4rec-pGes and bind TfR on tumour cells. This product was able to transfect target cells effectively in an immuno-specific manner, resulting in transient gene expression. This protein that can be applied as an effective therapeutic and diagnostic delivery to the tumor using endogenous membrane transport system with potential widespread utility. [ABSTRACT FROM AUTHOR]- Published
- 2012
- Full Text
- View/download PDF
11. Molecular cloning and characterization of the mouse Acdp gene family.
- Author
-
Cong-Yi Wang, Ping Yang, Jing-Da Shi, Purohit, Sharad, Dehuang Guo, Haiqian An, Jian-Guo Gu, Ling, Jennifer, Zheng Dong, and Jin-Xiong She
- Subjects
- *
MOLECULAR cloning , *CHROMOSOMAL proteins , *GENES , *NUCLEOTIDE sequence , *CIRCULAR DNA , *LABORATORY mice - Abstract
Background: We have recently cloned and characterized a novel gene family named ancient conserved domain protein (ACDP) in humans. To facilitate the functional study of this novel gene family, we have cloned and characterized Acdp, the mouse homologue of the human ACDP gene family. Results: The four Acdp genes (Acdp1, Acdp2, Acdp3 and Acdp4) contain 3,631 bp, 3,244 bp, 2,684 bp and 2,743 bp of cDNA sequences, and encode deduced proteins of 951, 874, 713 and 771 amino acids, respectively. The mouse Acdp genes showed very strong homologies (>90%) in both nucleotide and amino acid sequences to their human counterparts. In addition, both nucleotide and amino acid sequences within the Ancient Conserved Domain (ACD) are highly conserved in many different taxonomic species. Particularly, Acdp proteins showed very strong AA homologies to the bacteria CorC protein (35% AA identity with 55% homology), which is involved in magnesium and cobalt efflux. The Acdp genes are widely expressed in all tissues tested except for Acdp1, which is only highly expressed in the brain with low levels of expression in kidney and testis. Immunostaining of Acdp1 in hippocampus neurons revealed a predominant localization on the plasma membrane. Conclusion: The Acdp genes are evolutionarily conserved in diverse species and ubiquitously expressed throughout development and adult tissues suggesting that Acdp may be an essential gene. Acdp showed strong homology to bacteria CorC protein and predominantly localized on the plasma membrane. These results suggest that Acdp is probably a family of proteins involved in ion transport in mammalian cells. [ABSTRACT FROM AUTHOR]
- Published
- 2004
12. Aloperine Protects Mice against Ischemia-Reperfusion (IR)-Induced Renal Injury by Regulating PI3K/AKT/mTOR Signaling and AP-1 Activity.
- Author
-
Shuang Hu, Yuxing Zhang, Meng Zhang, Yanchao Guo, Ping Yang, Shu Zhang, Simsekyilmaz, Sakine, Jun-Fa Xu, Jinxiu Li, Xudong Xiang, Qilin Yu, and Cong-Yi Wang
- Abstract
Aloperine is a quinolizidine alkaloid extracted from the leaves of Sophora plants. It has been recognized with the potential to treat inflammatory and allergic diseases as well as tumors. In this report, we demonstrate that pretreatment with aloperine provided protection for mice against ischemia-reperfusion (IR)-induced acute renal injury as manifested by the attenuated inflammatory infiltration, reduced tubular apoptosis, and well-preserved renal function. Mechanistic studies revealed that aloperine selectively repressed IL-1β and IFN-γ expression by regulating PI3K/Akt/mTOR signaling and NF-κB transcriptional activity. However, aloperine did not show a perceptible impact on IL-6 and TGF-β expression and the related Jak2/Stat3 signaling. It was also noted that aloperine regulates AP-1 activity, through which it not only enhances SOD expression to increase reactive oxygen species (ROS) detoxification but also promotes the expression of antiapoptotic Bcl-2, thereby preventing tubular cells from IR-induced apoptosis. Collectively, our data suggest that administration of aloperine prior to IR insults, such as renal transplantation, could be a viable approach to prevent IR-induced injuries. [ABSTRACT FROM AUTHOR]
- Published
- 2015
- Full Text
- View/download PDF
13. Aloperine Protects Mice against Ischemia-Reperfusion (IR)-Induced Renal Injury by Regulating PI3K/AKT/mTOR Signaling and AP-1 Activity.
- Author
-
Hu S, Zhang Y, Zhang M, Guo Y, Yang P, Zhang S, Simsekyilmaz S, Xu JF, Li J, Xiang X, Yu Q, and Wang CY
- Abstract
Aloperine is a quinolizidine alkaloid extracted from the leaves of Sophora plants. It has been recognized with the potential to treat inflammatory and allergic diseases as well as tumors. In this report, we demonstrate that pretreatment with aloperine provided protection for mice against ischemia-reperfusion (IR)-induced acute renal injury as manifested by the attenuated inflammatory infiltration, reduced tubular apoptosis, and well-preserved renal function. Mechanistic studies revealed that aloperine selectively repressed IL-1β and IFN-γ expression by regulating PI3K/Akt/mTOR signaling and NF-κB transcriptional activity. However, aloperine did not show a perceptible impact on IL-6 and TGF-β expression and the related Jak2/Stat3 signaling. It was also noted that aloperine regulates AP-1 activity, through which it not only enhances SOD expression to increase reactive oxygen species (ROS) detoxification but also promotes the expression of antiapoptotic Bcl-2, thereby preventing tubular cells from IR-induced apoptosis. Collectively, our data suggest that administration of aloperine prior to IR insults, such as renal transplantation, could be a viable approach to prevent IR-induced injuries.
- Published
- 2016
- Full Text
- View/download PDF
14. Comparative analysis of the alveolar macrophage proteome in ALI/ARDS patients between the exudative phase and recovery phase.
- Author
-
Dong H, Li J, Lv Y, Zhou Y, Wang G, Hu S, He X, Yang P, Zhou Z, Xiang X, and Wang CY
- Subjects
- Adolescent, Adult, Blotting, Western, Bronchoalveolar Lavage Fluid, Electrophoresis, Gel, Two-Dimensional, Female, Humans, Male, Middle Aged, Peptide Mapping, Proteome chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Young Adult, Acute Lung Injury metabolism, Acute Lung Injury pathology, Macrophages, Alveolar metabolism, Macrophages, Alveolar pathology, Proteome metabolism, Respiratory Distress Syndrome metabolism, Respiratory Distress Syndrome pathology
- Abstract
Background: Despite decades of extensive studies, the morbidity and mortality for acute lung injury/acute respiratory distress syndrome (ALI/ARDS) remained high. Particularly, biomarkers essential for its early diagnosis and prognosis are lacking., Methods: Recent studies suggest that alveolar macrophages (AMs) at the exudative phase of ALI/ARDS initiate, amplify and perpetuate inflammatory responses, while they resolve inflammation in the recovery phase to prevent further tissue injury and perpetuated inflammation in the lung. Therefore, proteins relevant to this functional switch could be valuable biomarkers for ALI/ARDS diagnosis and prognosis. We thus conducted comparative analysis of the AM proteome to assess its dynamic proteomic changes during ALI/ARDS progression and recovery., Results: 135 proteins were characterized to be differentially expressed between AMs at the exudative and recovery phase. MALDI-TOF-MS and peptide mass fingerprint (PMF) analysis characterized 27 informative proteins, in which 17 proteins were found with a marked increase at the recovery phase, while the rest of 10 proteins were manifested by the significantly higher levels of expression at the exudative phase., Conclusions: Given the role of above identified proteins played in the regulation of inflammatory responses, cell skeleton organization, oxidative stress, apoptosis and metabolism, they have the potential to serve as biomarkers for early diagnosis and prognosis in the setting of patients with ALI/ARDS.
- Published
- 2013
- Full Text
- View/download PDF
15. Molecular cloning and characterization of the mouse Acdp gene family.
- Author
-
Wang CY, Yang P, Shi JD, Purohit S, Guo D, An H, Gu JG, Ling J, Dong Z, and She JX
- Subjects
- 3T3 Cells, Amino Acid Sequence, Animals, Blotting, Northern, Blotting, Western, Brain metabolism, Carrier Proteins metabolism, Cell Line, Cell Membrane metabolism, Chromosome Mapping, Chromosomes, Mammalian genetics, Cloning, Molecular, DNA, Complementary chemistry, DNA, Complementary genetics, Gene Expression Profiling, Humans, Male, Membrane Proteins genetics, Membrane Proteins metabolism, Mice, Microscopy, Confocal, Molecular Sequence Data, PC12 Cells, Phylogeny, Rats, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Carrier Proteins genetics, Multigene Family genetics
- Abstract
Background: We have recently cloned and characterized a novel gene family named ancient conserved domain protein (ACDP) in humans. To facilitate the functional study of this novel gene family, we have cloned and characterized Acdp, the mouse homologue of the human ACDP gene family., Results: The four Acdp genes (Acdp1, Acdp2, Acdp3 and Acdp4) contain 3,631 bp, 3,244 bp, 2,684 bp and 2,743 bp of cDNA sequences, and encode deduced proteins of 951, 874, 713 and 771 amino acids, respectively. The mouse Acdp genes showed very strong homologies (>90%) in both nucleotide and amino acid sequences to their human counterparts. In addition, both nucleotide and amino acid sequences within the Ancient Conserved Domain (ACD) are highly conserved in many different taxonomic species. Particularly, Acdp proteins showed very strong AA homologies to the bacteria CorC protein (35% AA identity with 55% homology), which is involved in magnesium and cobalt efflux. The Acdp genes are widely expressed in all tissues tested except for Acdp1, which is only highly expressed in the brain with low levels of expression in kidney and testis. Immunostaining of Acdp1 in hippocampus neurons revealed a predominant localization on the plasma membrane., Conclusion: The Acdp genes are evolutionarily conserved in diverse species and ubiquitously expressed throughout development and adult tissues suggesting that Acdp may be an essential gene. Acdp showed strong homology to bacteria CorC protein and predominantly localized on the plasma membrane. These results suggest that Acdp is probably a family of proteins involved in ion transport in mammalian cells
- Published
- 2004
- Full Text
- View/download PDF
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