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Biomedical subjects

M Kawashima

Publications and source records attributed to M Kawashima.

At least 307 records · Page 17Linked to original sources

The earliest form of C-protein expressed during striated muscle development is immunologically the same as cardiac-type C-protein.

A monoclonal antibody (C-315) specific for cardiac-type C-protein was prepared and, in combination with other antibodies specific for fast and slow skeletal muscle C-proteins, it was used to investigate the expression of C-protein isoforms in developing striated muscle cells in vivo and in vitro. During embryonic development of skeletal muscles, a C-protein recognized by C-315 appeared first but only transiently, it being replaced subsequently by two other isoforms recognized by the antibodies to slow and fast skeletal muscle C-proteins in a fiber-type specific manner as previously demonstrated (Obinata et al. (1984) Develop. Biol. 101, 116-124). In contrast, only cardiac-type C-protein was detected in cardiac muscle throughout the developmental stages. When myogenesis in vitro was monitored using the same antibodies, C-315 binding appeared first in multinucleated myotubes as in vivo which was followed by the sequential expression of two other C-protein variants. The reactivity of C-315 as well as that of anti-slow and anti-fast skeletal C-protein antibodies persisted during muscle development in culture. Thus, this study demonstrates that the earliest form of C-protein expressed in striated muscles may either be a cardiac-type isoform or a unique embryonic protein containing an epitope in common with the adult cardiac-type protein, and that transitions of C-protein isoform expression characteristic of each fiber-type occur during muscle development in vivo but not in vitro.

Animals↗

Characterization of a new type of human papillomavirus found in a lesion of Bowen's disease of the skin.

The genome of a human papillomavirus (HPV) found in a patient with Bowen's disease of the skin was molecularly cloned. Blot hybridization experiments, performed under stringent conditions, revealed no cross-hybridization between this HPV DNA and the other known HPV DNAs, showing that this HPV represents a new type, tentatively named HPV34. In relaxed hybridization conditions, the highest cross-hybridization was observed with HPV16 DNA. The physical map of HPV34 DNA was aligned with the genetic map of HPV16 DNA by heteroduplex mapping. HPV34 was not detected in 12 additional patients with Bowen's disease of the skin, but a closely related HPV DNA was found in one patient with penile Bowenoid papulosis.

Bowen's Disease↗

Endogenous sugar acid control of hypothalamic neuron activity and gastric acid secretion in rats.

The feeding related endogenous sugar acids, 2-deoxytetronic acid, 2-DTA and 3-deoxypentonic acid, 3-DPA, were investigated for their peripheral and central (hypothalamic) control of gastric acid secretion, and effects on activity of lateral hypothalamic (LHA) neurons in rats. Peripheral gastric acid secretion was not affected by either 2-DTA or 3-DPA. Slight gastric acid secretion was elicited by 3-DPA only when it was applied directly into the gastric related site of the LHA. Gastric acid secretion induced by 2-deoxy-D-glucose (2DG) was suppressed by application of 2-DTA in the LHA. 3-DPA had no effect on 2DG induced secretion. Electrophoretic application of 2-DTA significantly inhibited the activity of both gastric and non-gastric type glucose-sensitive neurons in the LHA, and 3-DPA significantly excited both types of glucose-sensitive neurons. The results agree with previous reports that 2-DTA and 3-DPA are endogenous satiety and hunger factors, respectively, and act by modulating hypothalamic control of gastric acid secretion which is mediated through gastric type and non-gastric type glucose-sensitive neurons.

Animals↗

Embryonic chicken skeletal, cardiac, and smooth muscles express a common embryo-specific myosin light chain.

It has been demonstrated that embryonic chicken gizzard smooth muscle contains a unique embryonic myosin light chain of 23,000 mol wt, called L23 (Katoh, N., and S. Kubo, 1978, Biochem. Biophys. Acta, 535:401-411; Takano-Ohmuro, H., T. Obinata, T. Mikawa, and T. Masaki, 1983, J. Biochem. (Tokyo), 93:903-908). When we examined myosins in developing chicken ventricular and pectoralis muscles by two-dimensional gel electrophoresis, the myosin light chain (Le) that completely comigrates with L23 was detected in both striated muscles at early developmental stages. Two monoclonal antibodies, MT-53f and MT-185d, were applied to characterize the embryonic light chain Le of striated muscles. Both monoclonal antibodies were raised to fast skeletal muscle myosin light chains; the former antibody is specific to fast muscle myosin light chains 1 and 3, whereas the latter recognizes not only fast muscle myosin light chains but also the embryonic smooth muscle light chain L23. The immunoblots combined with both one- and two-dimensional gel electrophoresis showed that Le reacts with MT-185d but not with MT-53f. These results strongly indicate that Le is identical to L23 and that embryonic chicken skeletal, cardiac, and smooth muscles express a common embryo-specific myosin light chain.

Animals↗