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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 39 (1996), S. 946-951 
    ISSN: 1432-0428
    Keywords: Diabetes mellitus ; glycation ; cross-links ; vascular stiffening
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Previous studies have shown that biomechanical analysis of aorta from diabetic subjects reveals a marked increase in stiffness compared to aorta from age-matched control subjects. In the present paper we have proposed that this increased stiffness can be attributed to glycation-induced inter-molecular cross-links based on a direct analysis of the two known glycation cross-links, the fluorescent pentosidine and the non-fluorescent NFC-1. There was a significant difference in the increase in concentration of both cross-links with increasing age for both the intima (p〈0.0025) and the media (p〈0.0005) from the diabetic compared to the control subjects, but no correlation with the mature enzymic cross-link hydroxylysyl-pyridinoline. Finally, we have obtained a significant correlation of stiffness with both glycation cross-links (NFC-1, r=0.86; p〈0.005 and pentosidine r=0.75, p〈0.05), but the concentration of NFC-1 is about 50 times greater than that of pentosidine, indicating that it is the major glycation cross-link responsible for the stiffening of the aorta.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 39 (1996), S. 946-951 
    ISSN: 1432-0428
    Keywords: Keywords Diabetes mellitus ; glycation ; cross-links ; vascular stiffening.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Previous studies have shown that biomechanical analysis of aorta from diabetic subjects reveals a marked increase in stiffness compared to aorta from age-matched control subjects. In the present paper we have proposed that this increased stiffness can be attributed to glycation-induced inter-molecular cross-links based on a direct analysis of the two known glycation cross-links, the fluorescent pentosidine and the non-fluorescent NFC-1. There was a significant difference in the increase in concentration of both cross-links with increasing age for both the intima (p 〈 0.0025) and the media (p 〈 0.0005) from the diabetic compared to the control subjects, but no correlation with the mature enzymic cross-link hydroxylysyl-pyridinoline. Finally, we have obtained a significant correlation of stiffness with both glycation cross-links (NFC-1, r = 0.86; p 〈 0.005 and pentosidine r = 0.75, p 〈 0.05), but the concentration of NFC-1 is about 50 times greater than that of pentosidine, indicating that it is the major glycation cross-link responsible for the stiffening of the aorta. [Diabetologia (1996) 39: 946–951]
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 43 (2000), S. 550-557 
    ISSN: 1432-0428
    Keywords: Keywords Malondialdehyde ; cross-linking ; diabetes ; atherosclerosis.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Malondialdehyde (MDA) is a highly toxic by-product formed in part by lipid oxidation derived free radicals. Many studies have shown that its concentration is increased considerably in diabetes mellitus. Malondialdehyde reacts both irreversibly and reversibly with proteins and phospholipids with profound effects. In particular, the collagen of the cardiovascular system is not only stiffened by cross-links mediated by malondialdehyde but then becomes increasingly resistant to remodelling. It is important in diabetes mellitus because the initial modification of collagen by sugar adducts forms a series of glycation products which then stimulate breakdown of the lipids to malondialdehyde and hence further cross-linking by malondialdehyde of the already modified collagen. Some progress is being made into the mechanisms of formation and the nature of the intermolecular cross-links induced by malondialdehyde which result in the stiffening of the collagenous tissues. Our recent studies indicate the formation of pyridyl cross-links. Malondialdehyde has been shown to react several orders of magnitude faster with the pre-existing collagen enzymic cross-links than the amino acid side-chains. Malondialdehyde modification of basic amino-acid side-chains also results in a change in properties, for example, in the charge profile of the molecule resulting in modified cell-matrix interactions. Although aspects of the biochemistry of malondialdehyde are still not fully understood its complex chemistry is being unravelled and this should lead to ways of preventing its damaging reactions, for example, through antioxidant therapy. [Diabetologia (2000) 43: 550–557]
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Experimental brain research 118 (1998), S. 501-510 
    ISSN: 1432-1106
    Keywords: Key words Face processing ; Magnetoencephalography ; Evoked responses ; Human subjects
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  This is a whole head magnetoencephalographic (MEG) study of the neural processing of briefly presented images of human faces in 14 normal subjects. The experiments involved three tasks of increasing complexity, involving image categorisation, image comparison and the identification of emotion. The analyses were based on average responses to repeated stimuli in the different image categories. These averages were processed to give numerical measures of the power within defined regions and latency spans. The only statistically significant difference in these data between the response to faces and other images is in the right occipito-temporal channels at a latency of 140 ms. The face-specific response is largely independent of the task. Source modelling suggests an extended source in the ventral occipito-temporal region. The analysis supports the notions of both face-specificity and right hemisphere dominance for all image types at early latencies.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 37 (1972), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 190 (1961), S. 259-260 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The polycrystalline carbohydrate and oc-hydroxy acid samples were sealed off in evacuated glass phials (5 mm. x 20 cm.) and irradiated from a 180 c. cobalt-60 y-radiation source for 15 hr. at room temperature. The samples could be kept at liquid-air temperature, until their spectra were recorded at ...
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Scandinavian journal of medicine & science in sports 15 (2005), S. 0 
    ISSN: 1600-0838
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine , Sports Science
    Notes: The molecular mechanisms involved in the aging of collagen and consequent increase in mechanical strength and stiffness occur in a series of enzymic and non-enzymic intermolecular cross-links. The enzymic mechanism involves divalent aldimine intermolecular cross-links derived from the reaction of aldehydes which then mature to trivalent cross-links and further stabilize the collagen fiber and is now well known. Recent studies have demonstrated that the rate of turnover and level of telopeptide lysyl hydroxylation modifies the nature of the cross-link and hence the mechanical strength of the fiber.The slow turnover of mature collagen subsequently allows accumulation of the products of the adventitious non-enzymic reaction of glucose with the lysines in the triple helix to form glucosyl lysine and its Amadori product, that is, the Maillard reaction. These products are subsequently oxidized to a complex series of advanced glycation end-products, some of which are intermolecular cross-links between the triple helices rendering the fiber too stiff for optimal functioning of the collagen fibers, and consequently of the particular tissue involved. The glycation reactions following maturation are true aging processes, and attempts at their specific inhibition involve competitive inhibition of the Maillard reaction and chemical cleavage of the glycation cross-links.It is clear that the nature of the age-related cross-links and hence tissue strength depends on the rate of turnover of the collagen. An examination of the particular effect of strenuous exercise on the rate of turnover of collagen and hence cross-linking in different tissues could lead to a better understanding of optimal sports training regimes.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial and engineering chemistry 9 (1937), S. 490-491 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial and engineering chemistry 12 (1940), S. 52-52 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Industrial and engineering chemistry 8 (1936), S. 52-55 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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