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  • 1
    Electronic Resource
    Electronic Resource
    The Structure of Type VII Collagen (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 460 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb51156.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Tetrodotoxin: anesthetic activity in the de-epithelialized cornea (1998)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 236 (1998), S. 790-794 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  · Background: Tetrodotoxin (TTX) binds with high affinity to sodium channels and produces local anesthesia. We investigated whether TTX is an effective, long-acting corneal anesthetic in rabbits. · Methods: After mechanical debridement of the central corneal epithelium, topical TTX (1 mM, 0.1 mM, or 0.01 mM) was applied to one eye each of 18 New Zealand White rabbits. The fellow eye of each rabbit was treated with control vehicle. Blink response to a mechanical stimulus was assessed. Blink response was also assessed every 3 h for 30 h in 6 rabbits treated with 1 mM TTX administered every 6 h. In a separate group of 12 rabbits with central epithelial debridement, the rate of epithelial healing was compared between animals treated with topical 1.0 mM TTX and animals receiving no treatment. · Results: After 4 h, eyes treated with 1.0 mM and 0.1 mM TTX were anesthetic. At 6 h, five of six rabbit eyes treated with 1.0 mM TTX were still partially anesthetic. By 8 h, the mean anesthesia score for 1.0 mM TTX was approaching normal. With multiple dosing, all six rabbit eyes remained anesthetic for the duration of the experiment. There was no significant difference in the rate of re-epithelialization between eyes treated with TTX and untreated controls. There was no evidence of systemic or local toxicity from topical TTX. · Conclusion: In a rabbit model, TTX is a long-acting topical anesthetic that retains its effectiveness when administered repeatedly over 24 h and does not inhibit epithelial healing. It may have application in management of pain after photorefractive keratectomy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004170050160
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  • 3
    Electronic Resource
    Electronic Resource
    Human trabecular meshwork cells as a thyroid hormone target tissue: presence of functional thyroid hormone receptors (1999)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 237 (1999), S. 231-240 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract.  · Purpose: To deter- mine whether human trabecular meshwork cells (HTM) are a po- tential target tissue for thyroid hormone (3,3′,5-triiodothyronine, T3). · Methods: Cultured HTM were assayed for the presence of thyroid hormone receptors (TRs) and retinoid X receptors (RXRs) by reverse-transcriptase polymerase chain reaction (RT-PCR) to detected TR and RXR mRNA, and by immunohistochemistry to detect nuclear TR and RXR proteins. Functionality of the TR was determined by analysis of 125I-T3 binding affinity and capacity in HTM nuclear extracts. Effects of T3 on modulation of hyaluronic acid (HA) levels in HTM were measured as a function of dose and duration of T3 administration. · Results: Analysis of RT-PCR and immunohistochemistry demonstrated that cultured HTM expressed TRα1, TRα2, and TRβ1 but not TRβ2; and RXRα but not RXRβ and RXRγ isoforms. Saturation binding and analysis of 125I-T3 to HTM nuclear extracts revealed Kd of 57 pM. The number of T3 binding sites extrapolated from a Scatchard plot was 7.3×1010/μg of HTM nuclear protein extract. T3 supplementation reduced the concentration of HA in the cell medium by 32–43% compared to cells grown in the absence of T3. · Conclusions: Cultured HTM express three TR isoforms and one RXR isoform, bind T3 with an affinity similar to that of TR in responsive cells, and modulate their HA production in response to T3. These findings indicate that the human trabecular meshwork tissue has the capacity to respond to thyroid hormones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004170050224
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  • 4
    Electronic Resource
    Electronic Resource
    Biosynthesis of collagen (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 31-37 
    Details
    ISSN: 0730-2312
    Keywords: assembly ; biosynthesis ; protein folding ; disulfide links ; collagen ; procollapen I, III, IV, V ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: During the biosynthesis and assembly of collagen structures, disulfide links can serve several functions. During biosynthesis they successively stabilize intra-peptide folding and associations of three chains into one molecule. Studies on the refolding and reassociation of reduced and denatured carboxyl propeptides of procollagen I showed that successive interactions of folding and assembly are successively weaker. Disulfide bridges were reestablished within correctly refolded carboxyl propeptides. Rearrangements of disulfide bridges may occur during the processing of type V procollagen molecules as these collagens become incorporated into extracellular matrix. The basement membrane procollagen IV molecules become disulfide linked at each end into networks, and there are indications that further rearrangements of disulfide links may allow additional modulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280106
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    Paper (German National Licenses)
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