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  • 1
    ISSN: 1432-0428
    Keywords: Keywords Leptin ; leptin receptor ; Ob-R ; obesity ; sequence variant.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Leptin is an adipocyte-derived blood-borne satiety factor that acts on its cognate leptin receptor (Ob-R) in the hypothalamus, thereby regulating food intake and energy expenditure. To explore whether mutations in the Ob-R gene cause obesity in humans, we have searched for mutations in the gene for Ob-Rb, a biologically active receptor isoform, in obese Japanese subjects. We have also examined associations between such mutants and obesity in the Japanese. Genomic DNAs were used as templates in polymerase chain reaction (PCR) with primers selected to amplify exons 2 to 20 of the human Ob-Rb gene. Direct sequence analysis of the PCR products revealed 7 nucleotide sequence variants (Lys109Arg, Gln223Arg, Ser343Ser, Ser492Thr, Lys656Asn, Ala976Asp, and Pro1019Pro) in the Ob-Rb coding region from 17 obese Japanese subjects with a family history of obesity (BMI 39.3 ± 8.4 kg/m2). No missense and nonsense mutations were found such as those in Zucker fatty (fa/fa) rats and Koletsky (fa k /fa k) rats. Nucleotide substitutions occurred at relatively high frequencies at codons 109, 223, 976, and 1019 (79, 91, 100, and 85 %, respectively). Allele frequency of each variant determined by PCR-RFLP and PCR-single strand conformation polymorphism analyses showed no significant differences between 47 obese (BMI 35.1 ± 6.5 kg/m2) and 68 non-obese (BMI 21.6 ± 2.2 kg/m2) subjects. The present study represents the first report of sequence variants of the Ob-Rb gene in the Japanese and provides evidence against either obesity-causing mutations or association of sequence variants with obesity in obese Japanese subjects. [Diabetologia (1997) 40: 1204–1210]
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Juveniles of Leiognathus nuchalis were raised from fertilized eggs for up to 60 d and examined for luminescence activity. Almost all juveniles raised separately from adults failed to produce detectable light. In contrast, a significant percentage (33 to 100%) of the juveniles became luminescent in less than 48 h when they were either kept with adults or inoculated with a homogenate of the adult light organs. The luminescence tended to increase with time after the treatments. These findings suggest that: (1) most of L. nuchalis offspring typically hatch and develop apo-symbiotically and (2) at least 45 d after hatching, juveniles can be infected with symbiotic luminous bacteria from the light organ of adult fish, and thereby gain the ability to produce light.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1041
    Keywords: Key words Pirfenidone; peritoneal sclerosis ; haemo‐dialysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 719-722 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1267-1270 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 451-456 
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The molecular and crystal structure of, cobalt(II) complex prepared by the reaction of 1,3,5-triphenylformazan with cobalt dichloride, 2,3,5-triphenyltetrazolium dichloro(1,3,5-triphenylformazanato)cobaltate(II), has been determined by means of X-ray diffraction. The complex crystallized in a triclinic space group P\overline 1, with Mr = 728.55, a = 10.214 (3), b = 18.208 (7), c = 9.985 (2) Å, \alpha = 96.44 (3), \beta = 107.92 (2), \gamma = 81.79 (3)°, Z = 2, Dx = 1.387 Mg m−3, \mu = 0.683 mm−1, F(000) = 750, R = 0.041, wR = 0.040 and S = 1.40. The complex is composed of a pair of ions, the 2,3,5-triphenyltetrazolium cation and the dichloro(1,3,5-triphenylformazanato)cobaltate(II) anion. The cobalt(II) ion is tetrahedrally coordinated by two N atoms and two chloride ions. One of the chloride ions of the anion has electrostatic intermolecular contacts with the tetrazolium ring of the cation. The conductivity of the complex in nitromethane solution showed complete dissociation of a pair of ions to separate ions.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Graefe's archive for clinical and experimental ophthalmology 233 (1995), S. 58-62 
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract • Background: Since Brockhurst reported the connection between uveal effusion in nanophthalmic eyes and their scleral alterations and treated them with vortex vein decompression or sclerectomy, many observers have found abnormal accumulation of glycosaminoglycans (GAGS) in nanophthalmic sclera. These GAG abnormalities were thought to effect the collagen changes, though it was not clear which GAGs were changed. • Methods: GAGs were isolated and their contents were determined in scleral specimens from three nanophthalmic patients and five age-matched controls, using electrophoresis and the cetylpyridinium method. • Results: Hyaluronic acid, dermatan sulfate and chondroitin sulfate were the major GAGs in both nanophthalmic and control samples. Nanophthalmic sclera showed 2.4-fold, 10-fold and 5.5-fold increases in hyaluronic acid, dermatan sulfate and chondroitin sulfate, respectively, compared with the controls. • Conclusion: The results suggest that increased levels of GAGS, particularly of dermatan sulfate and chondroitin sulfate may contribute to the abnormalities of collagen fibrillogenesis and be closely involved with the pathogenesis of nanophthalmos.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Graefe's archive for clinical and experimental ophthalmology 236 (1998), S. 531-536 
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  · Background: We determined the types and distribution of glycosaminoglycans (GAGs) and collagens, in anterior capsular opacification after endocapsular phacoemulsification and aspiration (ECPEA) and intraocular lens implantation. · Methods: Opacified anterior capsules were removed from human eyes after ECPEA. Immunohistochemical staining was performed to determine GAGs with monoclonal antibodies to chondroitin, chondroitin-4-sulfate (C4S), chondroitin-6-sulfate (C6S), dermatan sulfate (DS), and keratan sulfate (KS); collagens with monoclonal antibodies to types I, II, and III collagens; and cellular characteristics with monoclonal antibodies to vimentin, desmin, α-smooth muscle actin, and cytokeratin. Decorin mRNA and type I collagen mRNA were detected by in situ hybridization. · Results: In the capsules, the C6S, DS, KS, and types I and III collagens were similar to the chemical components found at the adhesion site of the anterior and posterior capsules after extracapsular cataract extraction, and cellular components contained vimentin, desmin, α-smooth muscle actin, cytokeratin, decorin mRNA, and type I collagen mRNA. · Conclusions: The GAGs and collagens in opacified anterior capsule after ECPEA were similar to those found during wound healing, although KS is present in normal anterior segment tissue during development and only in the cornea postnatally. These chemical components may be produced by myofibroblast-like cells presumably transformed from lens epithelial cells.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Graefe's archive for clinical and experimental ophthalmology 236 (1998), S. 679-687 
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  · Background: We determined the distribution of glycosaminoglycans and collagens in the developing human vitreous. · Methods: Eighty human eyes from 5 gestational weeks to 2 postnatal years of age were used. Glycosaminoglycan components were determined by enzyme digestion with hyaluronidase or chondroitinase AC and ABC and immunohistochemistry for chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, and dermatan sulfate. Collagen distribution was determined by immunohistochemistry for types I, II, and III collagens. · Results: Enzyme digestion showed that throughout development hyaluronic acid is the main glycosaminoglycan in the vitreous and in the extraocular space at 5–7 gestational weeks. Both areas were filled with mesenchymal cells. Immunohistochemistry showed chondroitin-6-sulfate in the vitreous between 6 and 40 gestational weeks, and chondroitin-4-sulfate between 12 and 40 gestational weeks. Hyaluronic acid and chondroitin sulfate appeared in the retina and around the hyaloid vessels at 12–40 weeks. Immunohistochemistry showed type III collagen in the vitreous and around the mesenchymal cells at 5–7 weeks that was replaced by type II collagen after 8 weeks. · Conclusions: Hyaluronic acid is the major glycosaminoglycan in the vitreous throughout development, except for the transient appearance of chondroitin sulfate at 6–40 gestational weeks. Type III is the main collagen in the early developing vitreous that converts to type II collagen at 8 weeks. The primary and secondary vitreous has the same components as these macromolecules. These vitreous glycosaminoglycans and collagens seem to be produced by mesenchymal cells at an early stage and by the retina and hyaloid vessels during middle and late development.
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