The Experts below are selected from a list of 21 Experts worldwide ranked by ideXlab platform
Shintaro T. Suzuki - One of the best experts on this subject based on the ideXlab platform.
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ProtoCadherin Pcdh2 shows properties similar to, but distinct from, those of classical Cadherins
Journal of Cell Science, 1995Co-Authors: Shuichi Obata, Haruhiko Sago, Nozomu Mori, Shigeru Taketani, Julie M. Rochelle, Michael F. Seldin, Mari K. Davidson, Tom St. John, Shintaro T. SuzukiAbstract:Cell adhesion and several other properties of a recently identified Cadherin-Related Protein, protoCadherin Pcdh2, were characterized. A chimeric Pcdh2 in which the original cytoplasmic domain was replaced with the cytoplasmic domain of E-Cadherin was expressed in mouse L cells. The expressed Protein had a molecular mass of about 150 kDa and was localized predominantly at the cell periphery, as was the wild-type Pcdh2. In a conventional cell aggregation assay, the transfectants showed cell aggregation activity comparable to that of classical Cadherins. This activity was Ca(2+)-dependent and was inhibited by the addition of anti-Pcdh2 antibody, indicating that the chimeric Pcdh2, and probably the wild-type Pcdh2, has Ca(2+)-dependent cell aggregation activity. Mixed cell aggregation assay using L cells and different types of transfectants showed that the activity of Pcdh2 was homophilic and molecular type specific and that Pcdh2 was transfectants did not aggregate with other types of transfectants or with L cells. In immunoprecipitation, the chimeric Pcdh2 co-precipitated with a 105 kDa and a 95 kDa Protein, whereas wild-type Pcdh2 co-precipitated with no major Protein. Pcdh2 was easily solubilized with non-ionic detergent, in contrast to the case of classical Cadherins. On immunofluorescence microscopy, the somas of Purkinje cells were diffusely stained with anti-human Pcdh2 antibody. Mouse Pcdh1 and Pcdh2 were mapped to a small segment of chromosome 18, suggesting that various protoCadherins form a gene cluster at this region. The present results suggest that Pcdh2, and possibly other protoCadherins as well as protoCadherin-Related Proteins such as Drosophila fat, mediate Ca(2+)-dependent and specific homophilic cell-cell interaction in vivo and play an important role in cell adhesion, cell recognition, and/or some other basic cell processes.
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Cloning, expression, and chromosomal localization of a novel Cadherin-Related Protein, protoCadherin-3.
Genomics, 1995Co-Authors: Haruhiko Sago, Michihiro Kitagawa, Shuichi Obata, Nozomu Mori, Shigeru Taketani, Julie M. Rochelle, Michael F. Seldin, Mari K. Davidson, Tom St. John, Shintaro T. SuzukiAbstract:To study the diversity of the protoCadherin family, the cDNA clones for a novel protoCadherin were isolated by screening rat brain cDNA libraries with a cDNA fragment obtained by PCR, and some of the properties were then characterized. The overall structure of the Protein defined by the clone is similar to that of previously identified protoCadherins; however, the cytoplasmic domain is distinct from those of previously cloned protoCadherins or any other Protein sequences in the data bank. We named this protocad herin-3 (Pcdh3) since this is the third protoCadherin of which the entire coding sequence has been determined. Most of the deduced amino acid sequences of other cDNA clones obtained by the screening show high homology with but are distinct from that of Pcdh3, indicating that most of these sequences correspond to homologous but different protoCadherins. These results demonstrate that Pcdh3 and the protoCadherins defined by these clones constitute a protoCadherin subfamily. Chromosome mapping indicates that mouse Pcdh3 is located in a specific region of mouse chromosome 18, close to the location of previously cloned protoCadherins, suggesting that various protoCadherins form a cluster in this region. In situ hybridization results showed that Pcdh3 and its Related Proteins were expressed at various areas in brain. The expressed Pcdh3 Protein from the cDNA in mouse L cells was about 100 kDa in molecular weight and was localized at cell-cell contact sites. In contrast to the classical Cadherins, however, the expressed Pcdh3 was sensitive to trypsin even in the presence of Ca2+, and the transfectants did not show strong Ca(2+)-dependent cell aggregation activity. These results indicate the structural and possibly functional diversity of the protoCadherin family and suggest a distinctive biological role for Pcdh3.
Hassan Y. Naim - One of the best experts on this subject based on the ideXlab platform.
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Cadherin-Related Protein 24 induces morphological changes and partial cell polarization by facilitating direct cell-cell interactions.
Biological chemistry, 2012Co-Authors: Marc Behrendt, Michael P. Krahn, Hiam Al-bayati, Amiri, Sandra Rizk, Hassan Y. NaimAbstract:Cadherin-Related Protein 24 (CDHR24) is a potential tumor suppressor located apically as well as laterally in polarized cells. Here, the role of CDHR24 in contributing to cell morphology and polarity is examined. CDHR24 was predominantly localized at the nonattached part of nonpolarizing cells while another apically sorted Protein, aminopeptidase N, was equally distributed over the plasma membrane. Furthermore, CDHR24 expression induced cell aggregation capacity, indicating direct cell-cell interaction. The transepithelial resistance, however, was elevated in polarized MDCK cells, but not in nonpolarizing CHO cells. Our data propose a model in which CDHR24 is directly involved in cell and tissue morphogenesis.
Ann C. Palmenberg - One of the best experts on this subject based on the ideXlab platform.
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Cryo-EM structure of rhinovirus C15a bound to its Cadherin-Related Protein 3 receptor
Proceedings of the National Academy of Sciences of the United States of America, 2020Co-Authors: Yingyuan Sun, Kelly Watters, Marchel G. Hill, Qianglin Fang, Yue Liu, Richard J. Kuhn, Thomas Klose, Michael G. Rossmann, Ann C. PalmenbergAbstract:Infection by Rhinovirus-C (RV-C), a species of Picornaviridae Enterovirus, is strongly associated with childhood asthma exacerbations. Cellular binding and entry by all RV-C, which trigger these episodes, is mediated by the first extracellular domain (EC1) of Cadherin-Related Protein 3 (CDHR3), a surface Cadherin-like Protein expressed primarily on the apical surfaces of ciliated airway epithelial cells. Although recombinant EC1 is a potent inhibitor of viral infection, there is no molecular description of this Protein or its binding site on RV-C. Here we present cryo-electron microscopy (EM) data resolving the EC1 and EC1+2 domains of human CDHR3 complexed with viral isolate C15a. Structure-suggested residues contributing to required interfaces on both EC1 and C15a were probed and identified by mutagenesis studies with four different RV-C genotypes. In contrast to most other rhinoviruses, which bind intercellular adhesion molecule 1 receptors via a capsid Protein VP1-specific fivefold canyon feature, the CDHR3 EC1 contacts C15a, and presumably all RV-Cs, in a unique cohesive footprint near the threefold vertex, encompassing residues primarily from viral Protein VP3, but also from VP1 and VP2. The EC1+2 footprint on C15a is similar to that of EC1 alone but shows that steric hindrance imposed by EC2 would likely prevent multiProtein binding by the native receptor at any singular threefold vertex. Definition of the molecular interface between the RV-Cs and their receptors provides new avenues that can be explored for potential antiviral therapies.
Marc Behrendt - One of the best experts on this subject based on the ideXlab platform.
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Cadherin-Related Protein 24 induces morphological changes and partial cell polarization by facilitating direct cell-cell interactions.
Biological chemistry, 2012Co-Authors: Marc Behrendt, Michael P. Krahn, Hiam Al-bayati, Amiri, Sandra Rizk, Hassan Y. NaimAbstract:Cadherin-Related Protein 24 (CDHR24) is a potential tumor suppressor located apically as well as laterally in polarized cells. Here, the role of CDHR24 in contributing to cell morphology and polarity is examined. CDHR24 was predominantly localized at the nonattached part of nonpolarizing cells while another apically sorted Protein, aminopeptidase N, was equally distributed over the plasma membrane. Furthermore, CDHR24 expression induced cell aggregation capacity, indicating direct cell-cell interaction. The transepithelial resistance, however, was elevated in polarized MDCK cells, but not in nonpolarizing CHO cells. Our data propose a model in which CDHR24 is directly involved in cell and tissue morphogenesis.
Shuichi Obata - One of the best experts on this subject based on the ideXlab platform.
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ProtoCadherin Pcdh2 shows properties similar to, but distinct from, those of classical Cadherins
Journal of Cell Science, 1995Co-Authors: Shuichi Obata, Haruhiko Sago, Nozomu Mori, Shigeru Taketani, Julie M. Rochelle, Michael F. Seldin, Mari K. Davidson, Tom St. John, Shintaro T. SuzukiAbstract:Cell adhesion and several other properties of a recently identified Cadherin-Related Protein, protoCadherin Pcdh2, were characterized. A chimeric Pcdh2 in which the original cytoplasmic domain was replaced with the cytoplasmic domain of E-Cadherin was expressed in mouse L cells. The expressed Protein had a molecular mass of about 150 kDa and was localized predominantly at the cell periphery, as was the wild-type Pcdh2. In a conventional cell aggregation assay, the transfectants showed cell aggregation activity comparable to that of classical Cadherins. This activity was Ca(2+)-dependent and was inhibited by the addition of anti-Pcdh2 antibody, indicating that the chimeric Pcdh2, and probably the wild-type Pcdh2, has Ca(2+)-dependent cell aggregation activity. Mixed cell aggregation assay using L cells and different types of transfectants showed that the activity of Pcdh2 was homophilic and molecular type specific and that Pcdh2 was transfectants did not aggregate with other types of transfectants or with L cells. In immunoprecipitation, the chimeric Pcdh2 co-precipitated with a 105 kDa and a 95 kDa Protein, whereas wild-type Pcdh2 co-precipitated with no major Protein. Pcdh2 was easily solubilized with non-ionic detergent, in contrast to the case of classical Cadherins. On immunofluorescence microscopy, the somas of Purkinje cells were diffusely stained with anti-human Pcdh2 antibody. Mouse Pcdh1 and Pcdh2 were mapped to a small segment of chromosome 18, suggesting that various protoCadherins form a gene cluster at this region. The present results suggest that Pcdh2, and possibly other protoCadherins as well as protoCadherin-Related Proteins such as Drosophila fat, mediate Ca(2+)-dependent and specific homophilic cell-cell interaction in vivo and play an important role in cell adhesion, cell recognition, and/or some other basic cell processes.
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Cloning, expression, and chromosomal localization of a novel Cadherin-Related Protein, protoCadherin-3.
Genomics, 1995Co-Authors: Haruhiko Sago, Michihiro Kitagawa, Shuichi Obata, Nozomu Mori, Shigeru Taketani, Julie M. Rochelle, Michael F. Seldin, Mari K. Davidson, Tom St. John, Shintaro T. SuzukiAbstract:To study the diversity of the protoCadherin family, the cDNA clones for a novel protoCadherin were isolated by screening rat brain cDNA libraries with a cDNA fragment obtained by PCR, and some of the properties were then characterized. The overall structure of the Protein defined by the clone is similar to that of previously identified protoCadherins; however, the cytoplasmic domain is distinct from those of previously cloned protoCadherins or any other Protein sequences in the data bank. We named this protocad herin-3 (Pcdh3) since this is the third protoCadherin of which the entire coding sequence has been determined. Most of the deduced amino acid sequences of other cDNA clones obtained by the screening show high homology with but are distinct from that of Pcdh3, indicating that most of these sequences correspond to homologous but different protoCadherins. These results demonstrate that Pcdh3 and the protoCadherins defined by these clones constitute a protoCadherin subfamily. Chromosome mapping indicates that mouse Pcdh3 is located in a specific region of mouse chromosome 18, close to the location of previously cloned protoCadherins, suggesting that various protoCadherins form a cluster in this region. In situ hybridization results showed that Pcdh3 and its Related Proteins were expressed at various areas in brain. The expressed Pcdh3 Protein from the cDNA in mouse L cells was about 100 kDa in molecular weight and was localized at cell-cell contact sites. In contrast to the classical Cadherins, however, the expressed Pcdh3 was sensitive to trypsin even in the presence of Ca2+, and the transfectants did not show strong Ca(2+)-dependent cell aggregation activity. These results indicate the structural and possibly functional diversity of the protoCadherin family and suggest a distinctive biological role for Pcdh3.
