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Biomedical subjects

R Matsuda

Publications and source records attributed to R Matsuda.

At least 73 records · Page 4Linked to original sources
PubMed1984

There is selective accumulation of a growth factor in chicken skeletal muscle. I. Transferrin accumulation in adult anterior latissimus dorsi.

Chick embryo myoblasts in culture will respond to extracts of adult anterior latissimus dorsi muscle with an increase in cell number and an increase in total protein and in myosin heavy chain in fused myotubes. Extracts of adult pectoralis major and of posterior latissimus muscles are only marginally active. The active adult muscle extracts are fractionated by DEAE-cellulose column chromatography and transferrin is identified as the active component based on the following findings: (1) the active fractions are shown to contain an 80K protein that comigrates with chicken transferrin on SDS-PAGE, (2) the active extract from the anterior latissimus dorsi completely replaced embryo extract in the culture medium and supported normal myogenesis, (3) the active extract requires iron for its ability to support myogenesis, (4) the peptide map of the 80K protein is identical to a peptide map of transferrin. Under conditions where the 80K protein is detected in adult anterior latissimus dorsi muscles it is shown that the protein is nevertheless not synthesized in the muscle. These results support the idea that tissues of selective muscles in the adult chicken accumulate transferrin. An accompanying paper shows that transferrin also accumulates in early developmental stages of fast muscle tissue but that accumulation ceases after hatching in these muscles in normal chickens but not in animals of congenic strains with inherited muscular dystrophy.

Aging↗
PubMed1984

There is selective accumulation of a growth factor in chicken skeletal muscle. II. Transferrin accumulation in dystrophic fast muscle.

Transferrin or a transferrin-like protein, with ability to stimulate myogenesis and terminal differentiation in vitro, is found in fast chicken muscle during embryonic development. After hatching, however, transferrin is no longer accumulated or is only weakly accumulated by fast muscles like the pectoralis major and the posterior latissimus dorsi but continues to be accumulated by slow muscles like the anterior latissimus dorsi. In congenic lines of chickens bearing the gene for muscular dystrophy, however, adult fast muscles do not lose the ability to accumulate transferrin. While transferrin is found selectively in adult normal and dystrophic muscle it does not appear to be synthesized by muscle cells. Immunocytochemical localization shows that transferrin is accumulated not so much by muscle fibers as it is by single cells in the muscle interstitial space. The relationship between transferrin presence and growth patterns in adult skeletal muscle is not currently understood but evidence suggests that transferrin stimulation of myogenesis observed in vitro may be mediated in vivo by non-muscle cells dwelling within the muscle interstitial space. These cells may act as transferrin-uptake sources for subsequent satellite cell stimulation.

Animals↗
PubMed1984

Denervated skeletal muscle displays discoordinate regulation for the synthesis of several myofibrillar proteins.

Synthesis patterns of myosin heavy- and light-chain isoforms, tropomyosin and troponin, have been studied in chicken fast muscle denervated at both neonatal and adult stages. Denervated neonatal muscle does not synthesize the adult myosin heavy-chain isoform at the time of denervation, but it does synthesize the adult isoform several months after denervation. Thus, innervation does not appear to be necessary for the normal sequential replacement of embryonic and neonatal myosin heavy chain by the adult variant. Nerve is required, however, for the regulation of tropomyosin and troponin expression. Normally the pectoralis major muscle represses synthesis of both beta-tropomyosin and leg-type troponin T during late embryonic development. After denervation, however, the muscle relaxes its ongoing repression of these proteins and significant amounts of both beta-tropomyosin and leg-type troponin T are synthesized by the muscle. Denervation also results in an altered pattern of myosin light-chain synthesis so that the ratio of fast light-chain 3/fast light-chain 1 decreases. Similar results are found in muscle denervated at the adult stage. In denervated muscle, therefore, synthesis of these myofibrillar proteins is not coordinated: ongoing isoform shifts proceed to express an adult pattern of myosin heavy chain while tropomyosin, troponin, and myosin light-chain patterns appear to revert to embryonic configurations.

Aging↗
PubMed1983

Human fetal muscle and cultured myotubes derived from it contain a fetal-specific myosin light chain.

Human fetal muscles at ages 110, 125, and 132 days contain a fetal-specific myosin light chain. This light chain is absent in adult human muscle, copurifies with myosin, and is identified as a slow light chain because it reacts with purified antibody to chicken slow muscle light chains and does not react strongly with antibody to fast myosin light chains. This light chain is synthesized in cultures of fetal muscle along with normal myosin light chains. The presence of a fetal light chain in culture provides a marker for studies of human muscle disease in which it is important to know when or if the muscle makes a transition from embryonic or fetal expression to true adult phenotype.

Fetus↗
PubMed1983

Regional differences in the expression of myosin light chains and tropomyosin subunits during development of chicken breast muscle.

Types of myosin light chains and tropomyosins present in various regions and at different developmental stages of embryonic and posthatched chicken breast muscle (pectoralis major) have been characterized by two-dimensional gel electrophoresis. In the embryonic muscle all areas appear to accumulate both slow and fast forms of myosin light chains in addition to alpha and beta forms of tropomyosin. During development regional differences in myosin and tropomyosin expression become apparent. Slow myosin subunits become gradually restricted to areas of the anterior region of the muscle and finally become localized to a small red strip found on its anterior deep surface. This red region is characterized by the presence of slow and fast myosin light chains, alpha-fast, alpha-slow, and beta-tropomyosin. In all other areas of the muscle examined only fast myosin light chains, beta-tropomyosin and the alpha-fast form of tropomyosin, are found. In addition, beta-tropomyosin also gradually becomes lost in the posterior regions of the developing breast muscle. In the adult, the red strip area represents less than 1% of the total pectoralis major mass and of the myosin extracted from this area approximately 15% was present as an isozyme that comigrated on nondenaturing gels with myosin from a slow muscle (anterior latissimus dorsi). The red region accumulates therefore fast as well as slow muscle myosin. Thus while the adult chicken pectoralis major is over 99% fast white muscle, the embryonic muscle displays a significant and changing capacity to accumulate both fast and slow muscle peptides.

Animals↗
PubMed1983

Regenerating adult chicken skeletal muscle and satellite cell cultures express embryonic patterns of myosin and tropomyosin isoforms.

Regenerating areas of adult chicken fast muscle (pectoralis major) and slow muscle (anterior latissimus dorsi) were examined in order to determine synthesis patterns of myosin light chains, heavy chains and tropomyosin. In addition, these patterns were also examined in muscle cultures derived from satellite cells of adult fast and slow muscle. One week after cold-injury the regenerating fast muscle showed a pattern of synthesis that was predominately embryonic. These muscles synthesized the embryonic myosin heavy chain, beta-tropomyosin and reduced amounts of myosin fast light chain-3 which are characteristic of embryonic fast muscle but synthesized very little myosin slow light chains. The regenerating slow muscle, however, showed a nearly complete array of embryonic peptides including embryonic myosin heavy chain, fast and slow myosin light chains and both alpha-fast and slow tropomyosins. Peptide map analysis of the embryonic myosin heavy chains synthesized by regenerating fast and slow muscles showed them to be identical. Thus, in both muscles there is a return to embryonic patterns during regeneration but this return appears to be incomplete in the pectoralis major. By 4 weeks postinjury both regenerating fast and slow muscles had stopped synthesizing embryonic isoforms of myosin and tropomyosin and had returned to a normal adult pattern of synthesis. Adult fast and slow muscles yielded a satellite cell population that formed muscle fibers in culture. Fibers derived from either population synthesized the embryonic myosin heavy chain in addition to alpha-fast and beta-tropomyosin. Thus, muscle fibers derived in culture from satellite cells of fast and slow muscles synthesized a predominately embryonic pattern of myosin heavy chains and tropomyosin. In addition, however, the satellite cell-derived myotubes from fast muscle synthesized only fast myosin light chains while the myotubes derived from slow muscle satellite cells synthesized both fast and slow myosin light chains. Thus, while both kinds of satellite cells produced embryonic type myotubes in culture the overall patterns were not identical. Satellite cells of fast and slow muscle appear therefore to have diverged from each other in their commitment during maturation in vivo.

Animals↗
PubMed1983

The interaction of selenium with various metals in vitro and in vivo.

The effects of many metal ions (Mn2+, Ag+, Cu+, Cu2+, Cd2+, Hg2+, Pb2+, Zn2+, As3+, Co2+, Bi3+, Ni2+, Sn2+, Sr2+, Fe2+, Fe3+, Ba2+, Mg2+, Cr3+, Cr6+, Pt2+, Au3+, Tl+, and Pd2+) on behavior of selenium in biological systems were examined in vitro and in vivo. In the in vitro studies using four different reaction systems, Mn2+, Ag+, Cu+, Cu2+, Cd2+, Hg2+, Pb2+, Zn2+, As3+, Co2+, Ni2+, Cr6+, Pt2+, Au3+, Tl+ and Pd2+ affected the behavior of selenium. Body distribution of selenium in mice was significantly altered by the i.v. coadministration of Ag+, Cu+, Cu2+, Cd2+, Hg2+, Pb2+, Zn2+, As3+, Bi3+, Ni2+, Cr3+, Pt2+, Au3+ or Pd2+. In the present study it was proved that the behavior of selenium in biological systems were influenced by many metals in vitro and in vivo. This observation is important in contemplating the biological roles of selenium as an essential element or as modifying factor for the toxicity of metal compounds.

Animals↗
PubMed1982

Myosin heavy chains from two different adult fast-twitch muscles have different peptide maps but identical mRNAs.

Myosin heavy chains prepared from the pectoralis major and from the posterior latissimus dorsi of the same adult chicken exhibit different peptide maps when cleaved with Staphylococcus aureus V8 protease. These differences were observed at five different enzyme concentrations and in chickens of various strains. The cleavage pattern of pectoralis major myosin heavy chain from different adult chickens was always identical, as was that of posterior latissimus dorsi myosin heavy chain, demonstrating the reproducibility of the technique. However, when RNAs extracted from the pectoralis major and from the posterior latissimus dorsi were translated in a cell-free reticulocyte lysate, the myosin heavy chain encoded by pectoralis major RNA and the myosin heavy chain encoded by posterior latissimus dorsi RNA exhibited identical peptide maps. These results suggest that the different peptide maps of myosin heavy chains from the pectoralis major and posterior latissimus dorsi may arise from posttranslational modifications.

Animals↗
PubMed1982

The two myosin isoenzymes of chicken anterior latissimus dorsi muscle contain different myosin heavy chains encoded by separate mRNAs.

The two myosin isozymes (SM1 and SM2) of the anterior latissimus dorsi muscle of the chicken change in relative concentration during development. As SM1 decreases from 13 days of embryonic growth through 1 year of adult maturation, SM2 increases. In the adult muscle SM2 accounts for over 95% of the total myosin. The myosin heavy chains of the two isozymes are distinctly different and may be separated from each other by 5% SDS polyacrylamide gel electrophoresis. The faster migrating myosin heavy chain is identified as originating from SM1 and the slower migrating myosin heavy chain from SM2 myosin isozymes. The myosin heavy chains change in relative concentration during development exactly parallel with changes in SM1 and SM2 isozyme levels. Peptide map analysis also reveals that SM1 myosin heavy chains and SM2 myosin heavy chains are distinctly different. When RNA from the ALD muscle is added to reticulocyte lysate protein synthesizing systems the translation products are shown to include both SM1 and SM2 myosin heavy chains. These comigrate exactly on 5% SDS polyacrylamide gels with authentic counterparts from ALD muscle. Finally, when peptide maps of SM1 and SM2 myosin heavy chains synthesized in the reticulocyte lysate are compared they are again found to be distinctly different and each is identical to a peptide map of respective authentic SM1 and SM2 myosin heavy chains. It is concluded that the myosin heavy chains of SM1 and SM2 myosin isozymes of ALD muscle have different primary structures and that they are encoded by two distinctly different mRNAs.

Age Factors↗
PubMed1982

Japanese encephalitis virus infection in fetal mice at different stages of pregnancy. II. Resistance to Japanese encephalitis virus infection.

The relationship between the stage of pregnancy of mice at the time of Japanese encephalitis (JE) virus inoculation and the resistance of JE virus infection of their offsprings was investigated. It was found that there was a stronger resistance to JE virus infection in offsprings born of mothers inoculated with JE virus at nine to sixteen days before parturition than in offsprings of mothers inoculated at one to eight days or at seventeen to twenty days before parturition. Resistance of the offsprings to JE virus infection lasted up to the age of 180 days after birth.

Animals↗