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  • 1
    Electronic Resource
    Electronic Resource
    Cellular control of collagen breakdown in rheumatoid arthritis (1978)
    Springer
    Inflammation research 8 (1978), S. 36-42 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Remodelling of connective tissue and its destruction in rheumatoid arthritis is related to collagenolysis. Study of collagenase released by rheumatoid synovial cells has indicated that the enzyme is released in latent form from adherent synovial cells in culture. As a latent enzyme it is protected from complexing with α2 macroglobulin, the principal proteinase inhibitor. Activation in vivo is very likely caused by proteases which destroy or complex with a portion of collagenase responsible for its latency. Recent data suggest that the latent collagenase is an enzyme-inhibitor complex and not a true zymogen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01972399
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Sequence of a Menkes-type Cu-transporting ATPase from Rat C6 Glioma Cells: Comparison of the rat protein with other mammalian Cu-transporting ATPases (1998)
    Springer
    Molecular and cellular biochemistry 181 (1998), S. 49-61 
    Details
    ISSN: 1573-4919
    Keywords: Menkes gene ; Menkes transcript ; Cu-ATPase ; heavy metal binding domain ; rat brain ATPase ; copper homeostasis ; C6 rat glioma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Rat Atp7a occupied a single open reading frame (27-4502) which coded for a protein of 1492 residues. Rat Atp7a was 98% and 95% identical to published sequences for the mouse and Chinese hamster, respectively, and 94% homologous to human ATP7A. Compared to ATP7A, the rat transcript coded for an additional alanine (A446) in the heavy metal binding (Hmb) domain and showed a 34 bp gap in the 3′ UTR. Based on published sequence data, hydropathic profiles for rat, mouse, Chinese hamster, and human Cu-ATPases were practically identical with the exception of 8 additional amino acid residues between the 4th and 5th Hmb sites in the human. As deduced from amino acid sequence data, Hmb was predicted to have regions with helical and beta structures. All four species had five of the six metal binding sites centered within hydrophobic regions. The comparative analyses suggested that the Hmb region of the molecule could experience numerous amino acid substitutions with no apparent disruption to the ATPase transport function whereas variations to the ATPase domain would be more critical.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006896612272
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Genes regulating copper metabolism (1998)
    Springer
    Molecular and cellular biochemistry 188 (1998), S. 57-62 
    Details
    ISSN: 1573-4919
    Keywords: copper transport ; Menkes disease ; Wilson disease ; copper absorption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The metabolism of Cu is intimately linked with its nutrition. From gut to enzymes, Cu bioavailability to key enzymes and other components operates through a complex mechanism that uses transport proteins as well as small molecular weight ligands. Steps in Cu transport through the blood, absorption by cells, and incorporation into enzymes are slowly being understood. Cloning and sequencing of the genes for Menkes disease and Wilson disease has shown that membrane-bound enzymes analogous to Cu-ATPases in prokaryotes are equally important to Cu transport and homeostasis in mammalian cells. The primary structure of the mammalian Cu-ATPases has been deduced from cDNAs from tissues and organs. It now appears that mammalian Cu-ATPase have tissue and developmental specificity. In this review, we will focus on the Cu-ATPase that has been identified with Menkes disease. An emphasis will be placed on the existence of multiple forms of the ATPase and some indication as to how the different isoforms befit their role in the normal physiology of copper, specifically transmembrane transport and maintenance of a favorable internal cellular environment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006816321679
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    Paper (German National Licenses)
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