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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 760 (1995), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The resilience and strength of bone is due to the orderly mineralization of a specialized extracellular matrix (ECM) composed of type I collagen (90%) and a host of non-collagenous proteins that are, in general, also found in other tissues. Biglycan (encoded by the gene Bgn) is an ECM proteoglycan ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of orthopaedic science 1 (1996), S. 349-350 
    ISSN: 1436-2023
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 2 (1996), S. 353-364 
    ISSN: 1075-4261
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: Two-dimensional (2D) infrared (IR) correlation spectroscopy was used to monitor the ν1, ν3 phosphate contour (900-1200 cm-1) of maturing poorly crystalline hydroxyapatite in synthetic (synthesized at constant and variable pH) and biological (calcified turkey leg tendon) systems. The 2D IR plots of the mineral prepared at variable pH exhibit peaks at 961, 999, 1018, 1036, 1095, 1126, and 1150 cm-1. The peaks at 961, 999, and 1095 cm-1 represent vibrations of PO3-4 in an apatitic/stoichiometric environment of poorly crystalline HA, while those at 1018, 1036, and 1126 cm-1 arise from PO3-4 in a nonstoichiometric/acid phosphate environment of poorly crystalline HA. The 2D IR analysis suggests that the intensities of peaks associated with PO3-4 in a nonstoichiometric/acid phosphate environment decrease as the reaction progresses. The 2D IR plots of the mineral formed at constant pH showed only bands characteristic of PO3-4 in a stoichiometric/acid phosphate environment. Analysis of the 2D IR plots of the mineral from calcified turkey leg tendon reveals peaks at 1019, 1039, 1075, 1126, and 1147 cm-1. The peaks at 1019, 1039, and 1126 cm-1 are characteristic of PO3-4 in a nonstoichiometric/acid phosphate environment of poorly crystalline HA, while the band at 1075 cm-1 is characteristic of PO3-4 in an apatitic/stoichiometric environment of poorly crystalline HA. Thus, the in vitro experiment in which the mineral is formed at variable pH is a better model of the mineral phase in calcified turkey leg tendon. In addition, the asynchronous plots from both the synthetic and biological minerals revealed those peaks which were noncorrelated. Also, this method of data analysis provided enhanced resolution of the highly overlapped ν1, ν3 phosphate contour commonly seen in Fourier transform-IR spectra of calcified tissue. © 1996 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 64 (1997), S. 632-643 
    ISSN: 0730-2312
    Keywords: calcification ; proteoglycans ; chondrocyte culture ; micro-mass culture ; cartilage calcification ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: In the presence of 4 mM inorganic phosphate, differentiating chick limb-bud mesenchymal cells plated in micromass cultures form a mineralized matrix resembling that of chick calcified cartilage. To test the hypothesis that cartilage proteoglycans are inhibitors of cell mediated mineralization, the synthesis, content, and turnover of proteoglycans were altered in this system, and the extent of mineralization and properties of the mineral crystals examined. In all cases where the proteoglycan synthesis or proteoglycans present were modified to provide fewer or smaller molecules, mineralization was enhanced. Specifically, when proteoglycan synthesis was blocked by treatment with 10-10 M retinoic acid, extensive mineral deposition occurred on a matrix devoid of both proteoglycans and cartilage nodules. The crystals, which formed rapidly, were relatively large in size based on analysis by X-ray diffraction or FT-IR microspectroscopy, and were more abundant than in controls. When 2.5 or 5 mM xylosides were used to cause the synthesis of smaller proteoglycans, the extent of mineral accretion was also increased relative to controls; however, the matrix was less affected, and the extent of mineral deposition and the size of the crystals were not as markedly altered as in the case of retinoic acid. Modification of existing proteoglycans by either chondroinase ABC or hyaluronidase treatment similarly resulted in increased mineral accretion (based on 45Ca uptake or total Ca uptake) relative to cultures in which the proteoglycan content was not manipulated. Crystals were more abundant and larger than in control mineralizing cultures. In contrast, when proteoglycan degradation by metalloproteases was inhibited by metal chelation with o-phenanthroline, the Ca accretion at early time points was increased, but as mineralization progressed, Ca accumulation decreased. These data provide evidence that in this culture system, proteoglycans are inhibitors of mineralization. J. Cell. Biochem. 64:632-643. © 1997 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 72 (1998), S. 83-91 
    ISSN: 0730-2312
    Keywords: biomineralization ; calcification ; bone ; dentin ; matrix proteins ; matrix vesicles ; collagen ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Biomineralization is the process by which mineral crystals are deposited in an organized fashion in the matrix (either cellular or extracellular) of living organisms. Over the past 25 years, new insights into the mechanisms that control these processes have been obtained, yet questions asked then still persist, especially in terms of vertebrate mineralization. Specifically, there are still debates concerning the chemical nature of the first mineral crystals formed in bone, dentin, and cementum; the factors leading to the initial deposition of these crystals; and the functions of macromolecules found associated with these crystals. In this review, emphasis is placed on the currently accepted answers to these questions, drawing insight from nonvertebrate systems. It is suggested that there are redundant calcification mechanisms and that, by taking advantage of our current knowledge of these mechanisms, opportunities will be provided for therapeutic manipulation of diseases in which biomineralization is impaired. J. Cell. Biochem. Suppls. 30/31:83-91, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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