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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 6 (1970), S. 225-228 
    ISSN: 0014-5793
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Archives of Biochemistry and Biophysics 226 (1983), S. 506-516 
    ISSN: 0003-9861
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2307
    Keywords: Limb bud cultures (mouse) ; Electron microscopy ; Effect of highly sulfated GAG (SP54® and Arteparon®) ; Collagen structure ; Cartilage pattern
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Addition of 1 mg/ml or higher doses of the highly sulfated pentosanpolysulfoester SP54® or the mucopolysaccharidepolysulfoester Arteparon® to limb bud cultures from 11-day-old mouse embryos caused a marked reduction in the growth of the distal parts of the cartilage anlagen. The most striking effect, however, was the change in the collagen structure of the cartilaginous intercellular substance. After more than 0.05 mg/ml SP54® or Arteparon® no collagen filaments were seen but collagen aggregates with an altered cross-striation occurred. They were produced by an antiparallel arrangement of collagen molecules caused by the highly sulfated substances. By immunofluorescence microscopy it was shown that SP54® and Arteparon® did not influence the distribution of the collagen types but only affected the aggregation of collagen type II. From the morphological point of view the production of endogenous PG seemed to be uneffected by SP54® and Arteparon®. The effect of SP54® and Arteparon® was reversible. After removal of these substances characteristic collagen filaments re-formed. The collagen aggregates were decomposed extracellularly or phagocytosed by chondroblasts and decomposed intracellularly.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 268 (1971), S. 235-241 
    ISSN: 1432-1912
    Keywords: Aerobic Glycolysis ; Embryonic Metabolism ; Glucose Metabolism ; Aerobe Glykolyse ; Stoffwechsel embryonalen Gewebes ; Glucose-Stoffwechsel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Analytical Biochemistry 94 (1979), S. 253-258 
    ISSN: 0003-2697
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0568
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Formation and morphology of the thickened basement membrane-like layer around the persisting maternal vessels of the Callithrix jacchus placenta were investigated from day 45 until term (day 142) using light, electron and immunofluorescence microscopy. Thickening occurs with the establishment of contacts between the vessels and the syncytiotrophoblast (day 48). Final thickness is reached at about day 100. The course of the vessels shows wide gaps where the maternal blood flows freely into the intertrabecular spaces. As revealed by electron microscopy, the extracellular sheath around the maternal vessels consists of an inner subendothelial basement membrane (3–6 μm) and an outer fibril-containing layer (2–4 μm). Cell debris is seen between the two layers and in the basement membrane. Plaques of granular and fine-filamentous material are incorporated into the fibril-containing layer. The synthesis of the basement membrane material is localized in the endothelial cells. Immunofluorescence microscopy reveals collagen types IV and V, laminin and heparan sulfate proteoglycan (BM-1) in the sheath around the persisting vessels. Fibronectin occurs only in certain areas or in the form of dots. Collagen types I and III are not seen in the region of the vascular wall. It can, therefore, be assumed that the subendothelial layer represents a genuine basement membrane; the fibrils consist of collagen type V and the plaques contain fibronectin. The existence of the thick perivascular sheath is attributed to the persistence and stability of the maternal vessels.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0568
    Keywords: Chondrogenesis ; Brachypod mouse ; Mutant ; Limb development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Brachypod (bpH/bpH), an autosomal mutation in mice, is characterized by a shortening of the long bones and paws, and a delay or absence of ossification in some of the distal limb elements. The present study represents a detailed description of the brachypod phenotype in day 12 hindlimb buds maintained for 6 days in a submerged, serum-free organ culture system. Using this in vitro system, the proximal-to-distal effect on the severity of cartilage reduction was intensified in the brachypod explants with an intermediate expression in the heterozygotes. Immunofluorescent staining of the brachypod cartilage revealed a deficiency in and an abnormal distribution of the proteoglycans. Although there was no recognizable difference in the immunofluorescent staining for type II collagen between the mutant and wild-type, electron micrographs showed the presence of thick fibrils in the matrix. Other atypical structures in the brachypod cartilage included pleomorphic nuclei, reduced intracellular glycogen granules and profuse intercellular contacts. It is proposed that with the use of this in vitro system which supports the autonomous development of the individual limb elements, experiments concerning the pathogenesis of skeletal mutations such as brachypod should be more feasible.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1420-908X
    Keywords: Immunoassay ; Chondrocytes ; Collagen type II ; Antiarthritic therapy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cartilage destruction is a characteristic feature of osteoarthritis. Treatment with certain nonsteroidal anti-inflammatory drugs could exacerbate cartilage destruction by impairing the synthesis of cartilage matrix proteins, type II collagen and proteoglycan. In order to monitor the changes occurring in cartilage collagen synthesis, we developed a type II collagen specific ELISA. The effects of antiarthritic agents on type II collagen and glycosaminoglycan synthesis were examined in rat chondrosarcoma cultures. Drugs were added to the monolayer cultures and 4 days later the total type II collagen, as determined by the type II collagen ELISA, and glycosaminoglycan content, as measured by dimethylmethylene blue dye binding assay, was measured. All drugs except tiaprofenic acid decreased type II collagen synthesis by at least 40% at 100 μg/ml. Tiaprofenic acid at 1 μg/ml increased type II collagen content by 54% of the controls. Glycosaminoglycan synthesis was decreased by acetylsalicylic acid, diclofenac and tiaprofenac acid, at 50 μg/ml or above. Indomethacin, naproxen and dexamethasone had no effect. Interestingly, tenidap stimulated the glycoaminoglycan synthesis by 32% at 100 μg/ml. We show that the combination of chondrosarcoma cultures, type II collagen specific ELISA and dimethylmethylene blue dye binding assay serves as a useful model for screening the effects of agents capable of modulating type II collagen and glycosaminoglycan synthesis.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Graefe's archive for clinical and experimental ophthalmology 212 (1980), S. 143-148 
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Isolated collagen fibrils treated with type-specific antibodies can be stained using a peroxidase-antibody complex. The staining pattern of the fibrils with this peroxidase-antibody complex is demonstrated and compared with the normal negative staining pattern of the fibrils. The possible binding sites of the anticollagen antibodies on the fibrils is also discussed.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Graefe's archive for clinical and experimental ophthalmology 215 (1981), S. 273-278 
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have used the indirect immunperoxidase technique to examine the exfoliation syndrome and can demonstrate that the fibrils so typically found in this disease certainly contain basement membrane proteoglycans. This finding is interesting for two reasons: 1. For the first time, an electron-microscopical technique is described that is able to identify one protein component of the exfoliation material. 2. The fact that the basement membrane proteoglycans are present in the exfoliation material supports the hypothesis that this disease is caused by a disturbance in the biosynthesis of the basement membrane.
    Type of Medium: Electronic Resource
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