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Biomedical subjects

M Takeichi

Publications and source records attributed to M Takeichi.

At least 199 records · Page 11Linked to original sources
PubMed1987

Quantitative electron microscopic investigation on changes of mitochondria in long-term CPZ administration in rat brain, liver and heart.

The effect of chronic administration of chlorpromazine (CPZ) on mitochondria (MT) in the rat brain (striatum), liver and heart was quantitatively examined with both the electron microscope and computer-assisted PICTURE ANALYSIS OA-1. The specimens were taken from six female rats, three controls and three experimentals to which 20 mg/kg body weight of CPZ was administered orally for 15 months from 5 weeks after birth. Thus the quantitative electron microscopic study was made on the mitochondrial sizes (cross-sectional areas) and cristal densities and the following results were obtained: 1) The sizes of MT from the striatal nerve cells and axo-dendritic spine postsynapses and liver parenchymal cells were larger in the CPZ-administered rats than in the controls, whereas there were no statistically significant changes in the sizes of MT from the striatal axo-dendritic spine presynapses and heart papillary muscle cells to which the influence of long-term CPZ administration could be well expected. 2) In contrast, with the mitochondrial sizes, the cristal densities represented by the number of cristae per unit area (mu2) of MT have decreased in the striatal nerve cells and axo-dendritic spine pre- and postsynapses, liver parenchymal cells and heart papillary muscle cells of the CPZ-administered rats than in those of the controls.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1986

Cadherin cell adhesion molecules with distinct binding specificities share a common structure.

Ca2+-dependent cell--cell adhesion molecules, termed cadherins, are divided into subclasses with distinct tissue distributions and distinct cell-binding specificities. To elucidate the biochemical relationship of these subclasses, we compared the pattern of tryptic cleavage and the partial amino acid sequence of mouse liver E-cadherin with those of chicken brain N-cadherin. Although these two cadherins are distinct in their cell-binding and immunological specificities, they showed an identical mol. wt and a similar tryptic cleavage pattern. We isolated tryptic fragments of E- and N-cadherin, and determined the sequences of nine amino acid residues of their amino terminus. The results showed that sequences of amino acids from the amino terminus to the 7th residues are identical in these two cadherins. We thus suggest that cadherins with distinct specificities have a common genic origin.

Animals↗
PubMed1986

A novel cadherin cell adhesion molecule: its expression patterns associated with implantation and organogenesis of mouse embryos.

The Ca2+-dependent cell adhesion molecules, termed cadherins, were previously divided into two subclasses, E- and N-types, with different adhesive specificity. In this study, we identified a novel class of cadherin, termed P-cadherin, using a visceral endoderm cell line PSA5-E. This cadherin was a 118,000-D glycoprotein and distinct from E- and N-cadherins in immunological specificity and molecular mass. In accord with these findings, cells with P-cadherin did not cross-adhere with cells with E-cadherin. P-Cadherin first appeared in developing mouse embryos in the extraembryonic ectoderm and the visceral endoderm at the egg cylinder stage and later was expressed in various tissues. The placenta and the uterine decidua most abundantly expressed this cadherin. The expression of P-cadherin was transient in many tissues, and its permanent expression was limited to certain tissues such as the epidermis, the mesothelium, and the corneal endothelium. When the tissue distribution of P-cadherin was compared with that of E-cadherin, we found that: each cadherin displayed a unique spatio-temporal pattern of expression; P-cadherin was co-expressed with E-cadherin in local regions of various tissues; and onset or termination of expression of P-cadherin was closely associated with connection or segregation of cell layers, as found with other cadherins. These results suggested that differential expression of multiple classes of cadherins play a role in implantation and morphogenesis of embryos by providing cells with heterogenous adhesive specificity.

Animals↗
PubMed1986

N-linked oligosaccharides are not involved in the function of a cell-cell binding glycoprotein E-cadherin.

E-cadherin is a Ca2+-dependent cell-cell adhesion molecule identified as a glycoprotein with a molecular weight (MW) of 124,000. To study the role of the sugar moieties of this adhesion molecule, we tested the effect of tunicamycin on aggregation mediated by E-cadherin of teratocarcinoma cells. Immunoblot analysis using a monoclonal antibody to E-cadherin showed that in cells treated with tunicamycin this adhesion molecule is converted into two forms with MW of 118,000 and 131,000. The smaller one was exposed on the cell surface and showed a trypsin sensitivity characteristic to E-cadherin, suggesting that this is the peptide moiety of E-cadherin whose glycosylation with N-linked oligosaccharides was blocked by tunicamycin. The larger one was not removed by trypsin treatment of cells, suggesting an intracellular location. These tunicamycin-treated cells aggregated in a Ca2+-dependent manner, and the aggregation was inhibited by a monoclonal antibody to E-cadherin. These results suggested that N-linked oligosaccharides are not involved in the functional sites of this adhesion molecule.

Antibodies, Monoclonal↗
PubMed1986

The role of cell adhesion in the synchronization and orientation of polarization in 8-cell mouse blastomeres.

A detailed investigation into the activity of the homotypic, Ca2+-dependent cell-cell adhesion system (CDS) in the early mouse embryo has revealed its involvement in the synchronizing of the time of polarization of 8-cell blastomeres, and the orienting of the axis of polarization. Since polarization marks an important and early event in the process of cell diversification in the mouse embryo, it is concluded that the CDS provides an important component of the system by which the temporal and spatial elements of normal development are integrated.

Animals↗
PubMed1985

A monoclonal antibody disrupting calcium-dependent cell-cell adhesion of brain tissues: possible role of its target antigen in animal pattern formation.

The Ca2+-dependent cell-cell adhesion system (CDS) is thought to be essential for the formation and maintenance of cell adhesion in a wide variety of tissues. Previous studies suggested that CDS has some cell-type specificity; for example, the monoclonal antibody ECCD-1 selectively recognizes CDS of certain epithelial tissues in mouse embryos but not nervous tissues. In the present study, we have obtained a monoclonal antibody, designated NCD-1, that disrupts connections between brain cells of mouse embryos. A series of experiments suggested that NCD-1 specifically recognizes CDS. We then determined the distribution of the NCD-1 antigen in various mouse tissues. NCD-1 reacted with cells of the following tissues and cell lines: nervous tissues from various sources, lens, striated muscle, cardiac muscle, glioma G26-20, adrenocortical tumor Y1, and melanoma B16. None of these cells reacted with ECCD-1, and the cells reactive with ECCD-1 did not react with NCD-1. There was also a class of cells that did not react with either ECCD-1 or NCD-1. These results suggest that cells in the body can be classified into at least three groups containing CDS of differing specificities. A map of the tissue localization of these different classes of CDS also suggests that the expression of cell-type-specific cell adhesion molecules in each tissue plays a crucial role in adhesion between the same cell types and segregation of different cell types in processes essential for animal morphogenesis.

Animals↗
PubMed1985

Morphometry of cytoarchitecture of the lateral hypothalamic area in the rat.

The cytoarchitecture of the lateral hypothalamic area (LHA) in rats was studied with cresyl violet-stained coronal celloidin sections and with sections of the brain impregnated by a Golgi method. Unimodality was established in the frequency distribution histogram of both the somatic cross-sectional area of the LHA neurons and somatic shape (elongation and circularity). The predominant somatic orientation was in the dorsomedial-ventrolateral direction: bimodality of the frequency distribution of somatic orientation was denied. These findings suggest that the LHA neurons examined in the present study are not subdivisible on the basis of the somatic area, shape or orientation. Although the neurons were classified into eight types based upon the dendritic pattern, those in the LHA largely consisted of only three of them; Type III (dendrites extending in two directions along the long axis of soma), Type IV (three directions) and Type VIII (four directions) jointly accounted for 97.1 percent of the total neurons examined. This finding suggests that the parameter of dendritic pattern serves an important purpose in the typing of the rat LHA neurons. The orientation of intrinsic dendrites and intrinsic axons in the LHA has also been described.

Animals↗
PubMed1985

Electron microscopic morphometric studies on synaptic vesicles of long-term CPZ-administered rat striatum.

The effect of chronic administration of chlorpromazine (CPZ) on the striatal synaptic vesicles was quantitatively investigated with an electron microscope. Six rats, three controls and three experimentals, which received 20 mg/kg b.wt. of CPZ daily for 15 months, were sacrificed and a total of 300 axo-dendritic spine synapses (50 synapses per animal) were randomly taken and divided into three zones with a width of 160-467 nm on electron micrographs (final magnification 60,000). The first zone was adjacent to the presynaptic membrane in the region of the synaptic cleft. The second and third were farther away from the first zone. In these zones we measured the vesicle density, vesicle size and vesicle elongation ratio (the shortest diameter/the longest diameter) with the following results: In both the CPZ-administered rats and the controls the vesicle number per unit area of axoplasm (vesicle density) was smaller in Zone III than in Zones I and II, while those in the latter two zones did not differ from each other. However, there was no significant difference in the vesicle number in any zone between the control and experimental animals. The vesicles in every zone were significantly larger in the CPZ-administered animals than in the controls. There were no conclusive findings on the vesicle elongation ratio (vesicle shape).

Animals↗
PubMed1984

Molecular nature of the calcium-dependent cell-cell adhesion system in mouse teratocarcinoma and embryonic cells studied with a monoclonal antibody.

The molecular nature of the Ca2+-dependent cell-cell adhesion system in mouse teratocarcinoma (t-CDS) was studied using a monoclonal antibody recognizing t-CDS. We isolated a hybridoma clone producing a monoclonal antibody (ECCD-1) able to disrupt cell-cell adhesion when added to monolayer cultures of teratocarcinoma cells. This antibody bound to the cells with intact t-CDS, resulting in an inhibition of their aggregation, but did not bind to cells from which t-CDS was removed by trypsin treatment in the absence of Ca2+. The binding of ECCD-1 to cell surfaces required Ca2+ but not other ions. Western blot analysis showed that ECCD-1 recognizes multiple cell surface proteins, the major one of which is a component with a molecular weight of 124,000. The binding of ECCD-1 to these antigens was Ca2+-dependent even in cell-free systems, suggesting that the molecules involved in t-CDS undergo conformational changes by binding with Ca2+, leading to conversion of their molecular structure into an active form. ECCD-1 also reacted with 8-cell stage mouse embryos and with certain types of epithelial cells (excluding fibroblastic cells) in various differentiated tissues collected from mouse fetuses, again affecting their cell-cell adhesion. We also showed that a monoclonal antibody (DE1) raised against gp84 (F. Hyafil et al., 1981, Cell 26, 447-454) recognizes the same antigens as ECCD-1.

Animals↗
PubMed1984

Monoclonal antibody ECCD-1 inhibits intercellular communication in teratocarcinoma PCC3 cells.

The monoclonal antibody ECCD-1 recognizing a certain class of cell surface proteins inhibits the Ca2+-dependent cell-to-cell adhesion in teratocarcinoma stem cells. In this paper, we studied the effect of ECCD-1 on cell-to-cell communication in PCC3 cells by measuring the transfer of lucifer yellow between cells. To this aim, PCC3 cells were cultured in the presence of ECCD-1 for various periods, and then the fluorescent dye was injected into a cell located in the center of cell colonies, followed by counting number of cells to which the dye was transferred. The results showed that ECCD-1 inhibits the dye transfer between cells, suggesting that the Ca2+-dependent cell-to-cell adhesion system (CDS) is essential for the functions of gap junction.

Animals↗
PubMed1983

The calcium-dependent cell-cell adhesion system regulates inner cell mass formation and cell surface polarization in early mouse development.

The monoclonal antibody ECCD-1 inhibits Ca2+-dependent cell-cell adhesion in teratocarcinoma cells, recognizing a cell surface component of MW 124,000. When mouse embryos at various preimplantation stages were cultured in the presence of ECCD-1, the compacted morphology of the 8- to 16-cell-stage embryos was destroyed. In these embryos, cell proliferation normally occurred and development of blastocyst-like vesicles was attained. However, these embryos did not contain inner cell mass (ICM). We found that ECCD-1 affects the pattern of polarization of the cell surface in late 8- and 16-cell-stage blastomeres, as detected by staining with fluorescence-labeled concanavalin A. In normal blastomeres, the pole was always apart from the cell-cell contact plane. In those cultured in ECCD-1, formation of the pole tended to be inhibited, and if observed, the pole was close to the cell-cell contact plane. We discuss the possible mechanisms for inhibition of ICM formation caused by blocking Ca2+-dependent cell-cell adhesion between blastomeres.

Animals↗
PubMed1983

Calcium-dependent cell-cell adhesion molecules common to hepatocytes and teratocarcinoma stem cells.

The molecules involved in Ca2+-dependent cell-cell adhesion systems (CDS) in mouse hepatocytes were characterized and compared with those in teratocarcinoma cells. Fab fragments of antibody raised against liver tissues (anti-liver) inhibited Ca2+-dependent aggregation of both liver and teratocarcinoma cells. A monoclonal antibody raised against teratocarcinoma CDS (ECCD-1) also inhibited the Ca2+-dependent aggregation of these two cell types equally. These antibodies induced disruption of cell-cell adhesion in monolayers of hepatocytes. Thus, CDS in these two cell types are not immunologically distinctive. Immunochemical analyses with these antibodies showed that CDS in both hepatocytes and teratocarcinoma cells involved at least two classes of cell surface proteins with molecular weights of 124,000 and 104,000. ECCD-1 selectively bound to hepatocytes but not to fibroblastic cells in liver cell cultures. Thus, the molecular constitution of CDS in hepatocytes and teratocarcinoma stem cells is identical. As ECCD-1 reacts with other classes of embryonic and fetal cells, the molecules identified here could have a major role in cell-cell adhesion in various tissues at any developmental stage of animals.

Animals↗
PubMed1983

Selective expression of cell type specific cell-cell adhesion molecules in mouse hybrid cells.

Ca2+-dependent cell-cell adhesion systems (CDS) are present in a variety of cells which can be grouped into at least two qualitatively different types, the teratocarcinoma type (t-CDS) and the fibroblast type (f-CDS), where different classes of adhesion molecules operate, respectively. In order to study the regulatory mechanisms of expression of different CDS types, we made cell hybrids between teratocarcinoma OTF9 cells (t-CDS) and fibroblast L cells (f-CDS), and between OTF9 cells (t-CDS) and hepatoma MH cells (no CDS). We thus examined which type of CDS is expressed in hybrid clones using a probe, an antibody that recognizes t-CDS selectively. We isolated many hybrid clones with different phenotypes, all displaying CDS activity, and found that CDS functioning in each clone was either t-CDS or another type(s) of CDS. There were no clones in which both t-CDS and another type(s) of CDS are active. We therefore suggested that the expression or function of t-CDS and other types of CDS is mutually exclusive within a single cell.

Alkaline Phosphatase↗