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ABSTRACT: Chalcedony, a microcrystalline form of silica (SiO(2)), has been found in the human brains of elderly patients by using a standard optical petrographic microscope. We document here our visualization of chalcedony using a Leica TCS - SP2 confocal laser scanning microscope. Sections of human brain were collected after autopsy from elderly patients. The autofluorescent character of chalcedony allowed us to obtain three-dimensional images of the crystals and mature prismatic quartz (chalcedony) was observed. Chalcedony occurred as rhombohedral (trigonal) crystals approximately 30 microm in size distributed in patches or aggregates. A less mature silica polymorph of about 1- 2 microm in size was detected near the crystals. This is the first time that biogenically-produced crystalline mineral as autofluorescent crystal aggregates has been observed in the human central nervous system of elderly patients using confocal laser scanning microscopy.
Biotechnic & Histochemistry 10/2009; 85(3):171-6. · 0.67 Impact Factor
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ABSTRACT: Electric organs of Psammobatis extenta (Rajiformes) electric fish derive from myoblasts of the caudal region (16). Here we study the presence of muscle proteins, actin and the actin-binding proteins, alpha-actinin and tropomyosin, in the electrocytes by means of biochemical approaches, scanning electron microscopy and immunocytochemical methods. NBD-phallacidin is employed to detect the filamentous form of actin (F-actin). Immunoblots of actin and alpha-actinin from P. extenta skeletal and smooth muscle show that the electric organ forms of actin and alpha-actinin correspond to muscle types. Scanning electron microscopy shows that P. extenta electrocytes are highly polarized cells, semicircular in shape, with an anterior, concave innervated face and a posterior, convex, non-innervated face. The immunofluorescence patterns of alpha-actinin and tropomyosin distribution are similar to those of actin, in that these epitopes appear to occur throughout the entire electrocyte cytoplasm. F-actin, as revealed by NBD-phallacidin fluorescence, was also found throughout the cytoplasm. This is the first time that evidence is presented to demonstrate the existence of muscle actin in this weak electric fish species electrocyte. The close evolutionary connection to that of muscle cells is discussed.
Comparative biochemistry and physiology. Part A, Physiology 03/1997; 116(2):113-8.
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ABSTRACT: 1. The electrocytes from the electric organ of the Patagonian ray P. extenta are very unusual cells: semicircular in shape, multinucleated and highly polarized. They have an anterior, concave, innervated face, which exhibits positive histochemical reactions for acetylcholinesterase and for the nicotinic acetylcholine receptor. Multiple nerve-endings are covered with Schwann cell projections, similar to those present in skeletal muscle. Their posterior face is convex, non-innervated and is in contact with collagen fibres. 2. The cytoplasm of these electrocytes possesses abundant filamentous actin (F-actin), orderly distributed in the cell and exhibiting intense fluorescence with NBD-phallacidin. The F-actin is in contact with Z-lines as in muscle, and in contrast with Torpedo (Kordeli et al., 1986, 1987) and Discopyge (Vidal et al., 1986, 1989a) electrocytes, where it is confined to the non-innervated face. 3. Electrocytes of this Rajidae are an ideal model for the study of F-actin because of the similar embryological origin with skeletal muscle tissue and also because of the peculiar characteristics of their cytoplasm, packed full with F-actin. In addition, electric organs could constitute an alternative biological source for the study of the cholinergic synapse.
Biocell: official journal of the Sociedades Latinoamericanas de Microscopía Electronica ... et. al 09/1995; 19(2):113-23. · 0.63 Impact Factor
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ABSTRACT: The glycosylphosphatidylinositol membrane anchor of variant surface glycoprotein of the African trypanosome Trypanosoma brucei contains several mannosyl residues for which dolichol phosphoryl mannose is supposed to be the precursor; this itself is probably synthesised by a dolichol-dependent mannosyltransferase. We have characterised and localised a mannosyltransferase activity of T. brucei which transfers mannose from GDP-[14C]mannose to exogenously added dolichyl phosphate. The enzyme was saturable for both its substrates and had a Km of 7.8 microM and 3.3 microM, respectively, for dolichyl phosphate and GDP-mannose. Mannosyltransferase was labile at 37 degrees C in the presence of Triton X-100, but its activity remained constant for at least 60 min at temperatures between 10-15 degrees C. The enzyme was inhibited by amphomycin and this inhibition was potentiated by the presence of 10 mM CaCl2. After subcellular fractionation of cell homogenates by differential centrifugation, mannosyltransferase was recovered mainly in the microsomal fraction and its distribution was very similar to that of RNA, a marker for the rough endoplasmic reticulum. After isopycnic centrifugation in a linear sucrose gradient the distribution of mannosyltransferase also resembled that of RNA. Both constituents exhibited a shift towards lower densities after pre-treatment of microsomal membranes with inorganic pyrophosphate, while other membrane markers such as acid phosphatase and nucleoside diphosphatase did not. It is concluded that the formation of dolichol phosphoryl mannose from GDP-mannose and dolichyl phosphate in T. brucei occurs mainly in the rough endoplasmic reticulum.
Molecular and Biochemical Parasitology 03/1994; 63(2):255-64. · 2.55 Impact Factor
