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  • 1
    Electronic Resource
    Electronic Resource
    Taurine Inhibits Development Of Atherosclerotic Lesions In apolipoprotein E-Deficient Mice (2001)
    Melbourne, Australia : Blackwell Science Pty
    Clinical and experimental pharmacology and physiology 28 (2001), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. The effects of taurine on the development of atherosclerotic lesions were investigated in apolipoprotein (apo) E-deficient mice, an animal model with severe hypercholesterolaemia and extensive atherosclerosis. These mice were fed a normal laboratory chow containing 2% taurine for 12 weeks.2. Serum total cholesterol was significantly elevated after 12 weeks treatment with taurine. This elevation was due to increases in very low-density lipoprotein- and low-density lipoprotein–cholesterol.3. Despite such effects on serum lipoproteins, analysis using en face oil red O staining revealed that taurine reduced the area of arterial lipid accumulation by 28%, as measured quantitatively as an index of atherosclerosis. Histological examination also demonstrated a decrease in the size of aortic lesions in taurine-treated mice.4. Serum levels of thiobarbituric acid reactive substances (TBARS) in apoE-deficent mice were higher than in normolipidaemic C57BL/6J mice. Serum TBARS levels were significantly decreased by 12 weeks treatment of apoE-deficient mice with taurine.5. Thus, taurine prevents the formation of atherosclerotic lesions, independently of serum cholesterol levels, and the results suggest that the anti-oxidative effects of tauirne are related to its anti-atherosclerotic actions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1440-1681.2001.03527.x
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  • 2
    Electronic Resource
    Electronic Resource
    Ultrastructural cytochemistry of complex carbohydrates in osteoblasts, osteoid, and bone matrix (1983)
    Springer
    Calcified tissue international 35 (1983), S. 309-319 
    Details
    ISSN: 1432-0827
    Keywords: Calcification ; Glycosaminoglycan ; Glycoprotein ; Collagen ; Acid phosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Glycosaminoglycans (GAGs) and glycoproteins are essential components for osteogenesis. We have examined rat osteoblasts, osteoid, transitional zone, and fully calcified bone matrix, utilizing Spicer's high-iron diaminethiocarbohydrazide-silver protein (HID-TCH-SP) method for sulfated glycoconjugates and Thiéry's periodate-TCH-SP (PA-TCH-SP) method for vicinal glycol-containing glycoconjugates. HID-TCH-SP stained cytoplasmic granules of osteoblasts. Stain deposits in the extracellular matrix were observed in decreasing amounts in osteoid, the transitional zone, and fully calcified bone matrix. Enzyme digestion with testicular hyaluronidase removed most HID-TCH-SP stain deposits. PA-TCH-SP staining was observed with increasing intensity in rough endoplasmic reticulum, Golgi saccules, and cytoplasmic granules. Collagen fibrils in osteoid were weakly stained with PA-TCH-SP, and their staining appeared even weaker in fully calcified bone matrix. In contrast, collagen fibrils in calcified cartilage stained intensely with the PA-TCH-SP method. Focal circular profiles (0.1–0.5µm in diameter), which lacked collagen fibrils but reacted moderately with PA-TCH-SP, were frequently seen in the transitional zone and fully calcified bone matrix, but were only occasionally present in osteoid. The presence of testicular hyaluronidase-resistant GAG and acid phosphatase in these focal areas suggests that they represent sites of GAG degradation. The eventual loss of HID-TCH-SP staining in the bone matrix suggests that removal of sulfated glycoconjugates may be a requisite for expansion of initial calcification sites and/or complete calcification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405052
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  • 3
    Electronic Resource
    Electronic Resource
    Ultrastructural visualization of elastic fibres with a tannate-metal salt method (1985)
    Springer
    Journal of molecular histology 17 (1985), S. 93-103 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A modification of the tannic acid-metal salt method was applied as an ultrastructural stain for elastin. Thin sections of glutaraldehyde-fixed, embedded rat aorta and rabbit elastic cartilage, with and without osmication, were examined. Raising the pH of the tannic acid solution from 2.7 to 9.0 progressively increased the electron-density of elastic fibres and collagen fibrils in osmicated and unosmicated specimens. The maximum tannic acid staining of elastic fibres was observed in the pH range 7.0–9.0. Collagen staining, although less intense than that of elastic fibres, was also greatest in this pH range. Elastic fibres in osmicated specimens demonstrated the strongest tannic acid staining with a minimal increase in density of collagen and cell nuclei when compared to the unosmicated specimens. Sequential treatments of osmicated specimens with tannic acid pH 7.0–9.0, and uranyl acetate, pH 4.1, enhanced the density of the elastin intensely, increased collagen staining moderately, but hardly increased the density of nuclei and microfibrils. In elastase-digested osmicated specimens, all tannic acid (pH 7.0)-uranyl acetate-reactive elastin was selectively removed. These results demonstrate that all the neutral and alkaline tannic acid-uranyl acetate methods can be used as a postembedment stain for elastin specimens fixed in glutaraldehyde and osmium tetroxide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003406
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  • 4
    Electronic Resource
    Electronic Resource
    Ultrastructural cytochemistry of oxytalan fibres in monkey periodontal ligaments with the high iron diamine method (1987)
    Springer
    Journal of molecular histology 19 (1987), S. 75-84 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Monkey periodontal ligaments have been examined at the ultrastructural level to demonstrate the nature of reactive sites in oxytalan fibres. The high iron diamine (HID) and HID-thiocarbohydrazide-silver proteinate methods specific for sulphate groups, with and without prior oxidation with monopersulphate, were used. Oxytalan fibres were composed of bundles of microfibrils with a diameter of 11.5 ± 1.7 nm (mean ±s.d.,n = 50). In cross section the microfibrils were found to have a denser periphery, giving them a ‘tubular’ appearance. The oxytalan microfibrils of non-oxidized specimens showed little reactivity with either HID method, except that the extracellular matrix material in close association with collagen fibrils stained weakly; in oxidized specimens, both HID methods strongly stained oxytalan microfibrils and weakly stained the extracellular matrix material. Such reactivity of oxytalan microfibrils was not altered by digestion with testicular hyaluronidase or chondroitinase ABC, performed prior to or after persulphate oxidation. Further, the sequential thiosulphation and HID method for the demonstration of disulphide and sulphhydryl groups stained oxytalan fibres moderately. These results indicate that the oxidative generation of sulphate groups in oxytalan fibres may occur from either disulphide or sulphhydryl groups, or both, rather than the result of unmasking of sulphated glycosaminoglycans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01682751
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  • 5
    Electronic Resource
    Electronic Resource
    Immunoelectron microscopic studies of glycosaminoglycans in the metaphyseal bone trabeculae of growing rats (1992)
    Springer
    Journal of molecular histology 24 (1992), S. 747-755 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The types and distribution of glycosaminoglycans (GAGs) were studied immunocytochemically in osteoid, mineralized bone matrix, and cartilage matrix of growing rat metaphyseal bone after aldehyde fixation and EDTA demineralization, using four monoclonal antibodies (mAbs 1-B-5, 2-B-6, 3-B-3 and 5-D-4). These mAbs specifically recognize epitopes in non-sulphated chondroitin (C0-S); chondroitin 4-sulphate (C4-S) and dermatan sulphate (DS); chondroitin 6-sulphate (C6-S) and C0-S; and keratan sulphate (KS) respectively. In osteoid, all mAbs except 1-B-5 weakly stained matrix material on and between collagen fibrils, and moderately stained organic material corresponding to bone nodules, which are known sites of mineralization. However, the staining of osteoid abruptly decreased at the mineralization front; weak staining was confined mostly to the organic material of bone nodules in mineralized bone matrix, with very weak or no staining of the rest of the bone matrix. This staining progressively decreased toward the mineralized cartilage matrix and became negative. The mineralized cartilage matrix and lamina limitans reacted strongly with all mAbs except 5-D-4. These results indicate that osteoid contains sulphated proteoglycans containing C4-S and/or DS, C6-S and KS, and subsequent bone matrix mineralization appears to require accumulation of these macromolecules within bone nodules and eventual loss of these substances for complete mineralization, whereas proteoglycans containing C0-S, C4-S and/or DS, and C6-S, still exist in mineralized cartilage matrix and lamina limitants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01460827
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  • 6
    Electronic Resource
    Electronic Resource
    Ultrastructural cytochemistry of proteoglycans associated with calcification of shark cartilage (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 208 (1984), S. 149-158 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Proteoglycans (PGs) as well as sulfated glycosaminoglycans (GAGs) are closely associated with cartilage calcification. An inner zone of endoskeletal tesserae of sharks is composed of a unique calcified hyaline cartilage. Initial calcification can be seen in the cartilage close to the inner zone. We have ultrastructurally examined shark, Triakis scyllia, noncalcifying, calcifying, and calcified cartilage using the tannic acid-ferric chloride (TA-Fe), the high iron diamine (HID), and the HID-thiocarbohydrazide-silver proteinate (HID-TCH-SP) methods for localization of sulfated complex carbohydrates. In noncalcifying cartilage, TA-Fe and HID strongly stained matrix granules which were round, ovoid, elongated, or irregularly shaped and presumably represented PG monomers. The size and staining intensity of the reactive matrix granules progressively decreased in calcifying cartilage toward the calcification front of the calcified cartilage. Similarly, a progressive decrease in the size of the HID-TCH-SP stain deposits in the matrix granules was observed in the calcifying cartilage close to the calcification front and was interpreted as a decrease in length of sulfate containing GAG chains. In the calcified cartilage, the highly calcified areas were often localized in the calcification front and contained few or no small HID-TCH-SP stain deposits, whereas the weakly calcified regions contained more stain deposits. These results indicate that partial and complete degradation of sulfated GAGs and/or PGs may be a requisite for calcification of shark cartilage.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092080202
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  • 7
    Electronic Resource
    Electronic Resource
    Ultrastructural cytochemistry of trout arterial fibrils as elastic components (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 220 (1988), S. 369-375 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The trout arterial wall contains numerous extracellular fibrils that are presumed to be elastic. However, the cytochemical properties of the arterial fibrils have not been studied. Thus, we have ultrastructurally and cytochemically examined these fibrils, utilizing routine uranyl acetate and lead (UA-Pb) double staining, the tannic acid (pH 7.0)-uranyl acetate (TA-UA) method as an electrondense staining for elastin, and Thiéry's periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) method to localize vicinal glycol-containing complex carbohydrates. The arterial fibrils, about 23 nm in thickness, were interwoven at random but frequently showed the circular alignment to the long axis of the aorta. Occasionally they appeared to coalesce side by side, and the coalesced portion tended to lose its affinity for UA-Pb stains. The TA-UA method stained the fibrils moderately to intensely and stained the coalesced parts of the fibrils more intensely. All of those TA-UA positive fibrils were completely removed after elastase en bloc digestion. The PA-TCH-SP method did not stain the arterial fibrils but stained another kind of much thinner interfibrillar filamentous structure. These results suggest that the fibrils in the wall of trout ventral aorta are elastin in nature and do not contain vicinal glycols, although the fibrils usually exist in a fibrillar form, which is unlike mammalian amorphous elastin.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092200405
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  • 8
    Electronic Resource
    Electronic Resource
    Ultrastructural and cytochemical study of elastic fibers in the ventral aorta of a teleost, Anguilla japonica (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 226 (1990), S. 18-26 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Previous studies have revealed that amorphous elastin and microfibrils are structural entities of mammalian elastic fibers. Elastin shows a wide phylogenetic distribution, but the presence of elastin-associated microfibrils has not been demonstrated in teleost aorta. Thus, we have ultrastructurally and cytochemically examined elastic fibers in the ventral aorta of eel, a teleost, by utilizing routine uranyl acetate and lead double staining, the tannic acid (pH 7.0) - uranyl acetate (TA-UA) method, elastase en bloc digestion, Thiéry's periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) method, and the horseradish-peroxidase-labeled concanavalin A (Con A) method. In the ventral aorta of eel, a little ultrastructural difference between elastic fibers in the intima and media and those in the adventitia was noticed, but in either tunic each elastic fiber was basically composed of a “fibrillar core” and surrounding microfibrils. The fibrillar core was a collection of fibrils which showed a tendency to coalesce with each other, and these constituent fibrils were TA-UA positive and elastase-sensitive, representing their nature of elastin. By contrast, microfibrils associated with the fibrillar core were TA-UA negative and elastase-resistant, and their glycoproteinaceous nature was demonstrated by PA-TCH-SP and Con A methods. Thus, this study provides evidence for the presence of elastin-associated microfibrils in teleost aorta. These results are discussed in relation to the topographical difference of elastic fibers in eel aortic wall.
    Additional Material: 20 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092260104
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  • 9
    Electronic Resource
    Electronic Resource
    Ultrastructural cytochemistry of aortic microfibrils in the arctic lamprey, Lampetra japonica (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 223 (1989), S. 158-164 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In the ventral aorta of lamprey, microfibrils are major components of the extracellilar matrix. With special refeence to these microfibrils, we have cytochemically exmined the ventral aorta, utilizaing the tannic acid (pH 7.0)-uranyl acetate (TA-UA) method, elastase en bloc digestion, Thiéry's periodis acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) method, and ferritin- or horseradish peroxidase-labeledd concanacalin A (Con A) methods. The lamprey microfirils were strongly stained with PA-TCH-SP and both Con A methods, but did not show TA-UA staining nor elastase sensitivity. These cytochemical properties of lamprey microfibrils are identical with those of mammalian elastin-associated microfibrils. On the other hand, in spite of extensive examination, TA-UA positive and elastase-sensitive extracellular components were not found, so that lamprey ventral aorta does not appear to contain elasin. These results indicate that lamprey lamprey aortic connective tissue contains microfibrils as elastic components, but deposition of amorphous elastin dose not occur.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092230207
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  • 10
    Electronic Resource
    Electronic Resource
    Thermal polymerization of dihydro-exo-dicyclopentadienyl acrylate (1979)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 180 (1979), S. 33-40 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The thermal polymerization of dihydro-exo-dicyclopentadienyl acrylate (DDA) (tricyclo[5.2.1.02.6]dec-3-en-9-yl acrylate) was carried out under nitrogen in the absence of any initiator to investigate the kinetics and mechanism for it. The polymerization rate was found to follow the equation: Rp=k[DDA]1.6. The rate was nearly the same as those obtained for the polymerization of other alkyl acrylates. The overall activation energy for the polymerization was determined to be 57,3 kJ/mol (13,7 kcal/mol). The kinetic data and the data obtained by spin trapping technique during the polymerization showed that the double bond of the acryl group was polymerized much faster than that of the cyclopentene ring to form the straight chain polymer and that the double bond of the cyclopentene ring began to polymerize to a small extent, at a stage where most of acryl groups were polymerized, to give some crosslinking structures.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1979.021800104
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