Biomedical subjects

D Rhee

Publications and source records attributed to D Rhee.

5 recordsLinked to original sources

PubMed1998

Inhibition of calcium-dependent motility of cochlear outer hair cells by the protein kinase inhibitor, ML-9.

The calcium ionophore ionomycin has been shown to induce length increases of guinea pig outer hair cells (Dulon et al., 1990). We have demonstrated that these length increases can be inhibited by a 30 min preincubation of the cells with the protein kinase inhibitor ML-9. At either 30 or 60 s after ionomycin application, the effect of ML-9 was dose-dependent with a half maximal response at approximately 0.3 microM. No effect on cell length was detected after 30 min incubation with 0.5 and 5 microM ML-9 alone. However, with 50 and 500 microM ML-9, significant contraction in cell length was observed. 50 microM ML-9 did not interfere with the ability of ionomycin to elevate fluorescence of the calcium indicator Fluo-3, nor did it alter the ability of cells to exclude propidium iodide from their nuclei. Treatment with 500 microM ML-9 resulted in impaired cell morphology. The data support the hypothesis that protein kinase activity regulates calcium-dependent processes that affect shape changes of outer hair cells. They are consistent with the involvement of the calcium/calmodulin-dependent enzyme, myosin light chain kinase, a known target of ML-9, but do not preclude the possibility of another intracellular target for ML-9.

Aniline Compounds↗

PubMed1997

Premyofibrils in spreading adult cardiomyocytes in tissue culture: evidence for reexpression of the embryonic program for myofibrillogenesis in adult cells.

Do adult cardiomyocytes use the same pathways hypothesized for the formation of myofibrils in embryonic cardiomyocytes in tissue culture. [Rhee, et al., Cell Motil. Cytoskeleton 28:1-24, 1994]? Premyofibrils in embryonic cardiomyocytes are composed of short sarcomeric units of alpha-actinin (Z-bodies) and actin filaments held together by short nonmuscle myosin IIB filaments. Premyofibrils are believed to be transformed into nascent myofibrils by their capture of muscle-specific myosin II filaments aligned in aperiodic arrays. Nascent myofibrils are thought to transform into mature myofibrils by the loss of nonmuscle myosin IIB, the fusion of the Z-bodies into Z-bands, and the periodic alignment of muscle myosin II filaments into A-bands. Freshly isolated cat and rat adult cardiomyocytes placed in tissue culture lack premyofibrils and nascent myofibrils. Adult cardiomyocytes spreading in culture reinitiate the synthesis of nonmuscle myosin IIB. Moreover, patterns similar to the proposed embryonic myofibrillar program first detected in spreading chick embryonic hearts were also detected in these spreading adult mammalian cardiomyocytes. The isolated adult cardiomyocytes begin to spread after 1 day in culture by sending out lamellipodia. When these cells are injected with fluorescently labeled alpha-actinin, linear arrays of short spacings of beaded alpha-actinin bodies are detected in the spreading edges of the adult cardiomyocytes. These dense bodies (Z-bodies) stain positively for the same sarcomeric-specific isoform of alpha-actinin that is in the Z-bands of mature sarcomeres. These linear arrays of alpha-actinin-containing Z-bodies have other characteristics of premyofibrils and are detected only in the spreading regions of the cells. Thus, these premyofibrils at the edges of the spreading adult cardiomyocytes stain positively for nonmuscle myosin IIB but negatively for muscle-specific myosin II. Initially, no vinculin is associated with any parts of the premyofibrils in the spreading regions of the early spreading cardiomyocytes. However, later, vinculin is found to be associated with the ends of the premyofibrils. Fibers that stain solidly for muscle-specific myosin II (i.e., nascent myofibrils) are localized between the peripheral premyofibrils and the centrally positioned, mature myofibrils. It is suggested that the puzzling ability of cardiomyocytes in hypertrophic hearts to reinitiate the synthesis of fetal sarcomeric proteins may be related to the reinitiation of the embryonic premyofibril program for myofibrillogenesis.

Animals↗

PubMed1994

Phospholipid immobilization on solid surfaces.

Single chain ether phospholipids (PLs) containing omega-carboxyl groups in the alkyl chain were immobilized on silica propylamine (SPA) to form IAM chromatography packing material. The PL ligands are analogs of phosphatidylglycerol (PG), phosphatidylserine (PS), phosphatidylethanolamine (PE), and phosphatidic acid (PA). All of these PLs contain polar functional groups in the lipid head group that require protection prior to PL immobilization and then deprotection after immobilization. The IAM surface was prepared in four steps: (i) the omega-carboxyl group was activated with carbonyldiimidazole, (ii) the activated PL-imidazolide ligand was bonded to SPA, (iii) the surface was end capped with a long chain anhydride and then end-capped with a short chain anhydride, and (iv) protecting groups were removed to form the IAM surface. The extent of deblocking the protecting groups was typically > or = 90%. This immobilization strategy generated a phospholipid surface that was stable when solvated with all organic solvents and aqueous buffers between pH 2 and 8. Both FT-IR spectroscopy and elemental analysis indicated that the bonding densities were 64-83 mg of PL/g of SPA, which corresponds to an area per molecule of 66-104 A2. These bonding densities for the immobilized PLs are very close to the area per molecule of mobile phospholipids comprising liposome membrane. The similar areas per molecule of immobilized PLs and mobile phospholipid in liposomes indicate that the lipid environments are similar.

Liposomes↗

PubMed1994

The premyofibril: evidence for its role in myofibrillogenesis.

When cardiac muscle cells are isolated from embryonic chicks and grown in culture they attach to the substrate as spherical cells with disrupted myofibrils, and over several days in culture, they spread and extend lamellae. Based on antibody localizations of various cytoskeletal proteins within the spreading cardiomyocyte, three types of myofibrils have been identified: 1) fully formed mature myofibrils that are centrally positioned in the cell, 2) premyofibrils that are closest to the cell periphery, and 3) nascent myofibrils located between the premyofibrils and the mature myofibrils. Muscle-specific myosin is localized in the A-bands in the mature, contractile myofibrils, and along the nascent myofibrils in a continuous pattern, but it is absent from the premyofibrils. Antibodies to non-muscle isoforms of myosin IIB react with the premyofibrils at the cell periphery and with the nascent myofibrils, revealing short bands of myosin between closely spaced bands of alpha-actinin. In the areas where the nascent myofibrils border on the mature myofibrils, the bands of non-muscle myosin II reach lengths matching the lengths of the mature A-bands. With the exception of a small transition zone consisting of one myofibril, or sometimes several sarcomeres, bordering the nascent myofibrils, there is no reaction of these non-muscle myosin IIB antibodies with the mature myofibrils in spreading myocytes. C-protein is found only in the mature myofibrils, and its presence there may prevent co-polymerization of non-muscle and muscle myosins. Antibodies directed against the non-muscle myosin isoforms, IIA, do not stain the cardiomyocytes. In contrast to the cardiomyocytes, the fibroblasts in these cultures stain with antibodies to both non-muscle myosin IIA and IIB. The premyofibrils near the leading edge of the lamellae show no reaction with antibodies to either titin or zeugmatin, whereas the nascent myofibrils and mature myofibrils do. The spacings of the banded alpha-actinin staining range from 0.3 to 1.4 microns in the pre- and nascent myofibrils and reach full spacings (1.8-2.5 microns) in the mature myofibrils. Based on these observations, we propose a premyofibril model in which non-muscle myosin IIB, titin, and zeugmatin play key roles in myofibrillogenesis. This model proposes that pre- and nascent myofibrils are composed of minisarcomeres that increase in length, presumably by the concurrent elongation of actin filaments, the loss of the non-muscle myosin II filaments, the fusion of dense bodies or Z-bodies to form wide Z-bands, and the capture and alignment of muscle myosin II filaments to form the full spacings of mature myofibrils.

Actinin↗

PubMed1990

The Tao, psychoanalysis and existential thought.

The purpose of this paper is to clarify some existing misunderstandings in the area of psychotherapy, existential approach and the Eastern Tao (Zen Buddhism, Confucianism, Lao-tzu, Chuang-tzu) by showing the common elements between Eastern Tao and psychoanalysis, and existential thought. The author compared the goal of Tao practice, namely, Zen Buddhism, Confucianism etc. with that of Western psychoanalysis, humanistic psychology and transpersonal psychotherapy. He concludes that these goals are the same and that the names are different. He also compared the procedures and processes of psychoanalysis and Zen practice. Sudden enlightenment and gradual training in Zen practice were compared with insight and 'working through' in psychoanalysis. Zen emphasis on relationship, ego strength and interpretation was linked with similar topics in psychoanalysis. The results of Zen practice and the central features of every psychoanalytic treatment were examined and found the same, that is, the resolution of, or transcending of, love (dependence) and hate (hostility). The description of a mature analyst and that of a Boddhisattva were compared and found the same. A trace of neurotic motivation remains but they are not influenced by it in helping others. The problem of theory and reality was discussed and strong emphasis on reality was described; in other words, the goal is directed at reality and theory is only a means pointing at reality. If you see the reality, you should forget the theory.

Buddhism↗