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[The so-called cardiac myxoma. Histological, electron microscopical, immunofluorescence, and biochemical investigations in 3 cases (author's transl)].

Three cardiac Myxomas were studied by light-, immuno-fluorescence and electron microscopy. Acid mucopolysaccharides of the tumour were isolated chromatographically. The surfaces of the "myxomas" were papillary in two cases and smooth in one. The smooth surfaced tumour recurred six months after primary resection; histological specimens were more cellular than those of the papillary tumors and showed nuclear polymorphism and mitoses. The cells of two papillary tumours were identified as endocardial by electron microscopy, however, the cells of the smooth surfaced tumour were typical myofibroblasts. In both types of "myxomas" the cells were rich on cytoplasmic filament that contained acto-myosin. Biochemical investigation failed to reveal any difference between the acid mucopolysaccharide pattern of the two tumour types; isolated mucopolysaccharides being typical for embryonal mesenchymal tissue. The authors agree with Albertini (1963), that "cardiac myxoma" is a misnomer for two different typical endocardial tumours: a true endothelioma and a "special fibroma" (myofibroma or myofibrosarcoma).

Adult

Cross bridge slippage induced by the ATP analogue AMP-PNP and stretch in glycerol-extracted fibrillar muscle fibres.

Glycerol-extracted insect fibillar muscle fibers in rigor exhibited both an elastic and a plastic phase in the length-tension diagram. The transition between these phases took place at a critical tension, the "yield point" or elastic limit. In the plastic phase the apparent static elastic modulus became zero, whereas the immediate elastic modulus (measured by rapid length changes completed within 4 ms) exhibited no abrupt change at the yield point. The tension value of the yield point (but not immediate stiffness) was lowered by addition of AMP-PNP and was partially restored by washing out AMP-PNP. The dependence of the critical tension at which plastic flow begins on cooperative cross bridge behaviour is discussed in terms of breaking and reforming acto-myosin linkages. Evidence is presented that addition of AMP-PNP induces slippage of cross bridges on the actin filament by affecting the interaction between myosin and actin.

Actins

The Myo2 adaptor Ldm1 and its receptor Ldo16 mediate actin-dependent lipid droplet motility.

Organelle motility enables strategic cellular reorganizations. In yeast, this process depends on the actin cytoskeleton, type V myosin motor proteins, and organelle-specific myosin adaptor proteins. While the myosin adaptors for most organelles are known, the coupling of myosin to lipid droplets (LDs), the cellular lipid storage organelles, remained enigmatic. Using genome-wide screening, we identified Ldm1 (lipid droplet motility 1/Yer085c) as a myosin adaptor. Ldm1 binds to the globular tail domain of the myosin Myo2 and to the LD surface protein Ldo16 to enable actin-dependent LD motility. Ldo16 has additional roles in LD contact sites to the vacuole and the endoplasmic reticulum, suggesting a coordination of LD motility and organelle tethering. Ldm1 has a second role in mitochondrial transport, and elevated Ldm1 levels rescue defects of the mitochondrial Myo2-adaptors Mmr1/Ypt11. Our work identifies the molecular machinery for LD motility and contributes to a comprehensive understanding of acto-myosin-based cellular reorganization.

Lipid Droplets