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  • 1990-1994  (4)
  • 1991  (4)
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  • 1990-1994  (4)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Anatomy and embryology 184 (1991), S. 345-353 
    ISSN: 1432-0568
    Keywords: Human embryo ; Lectins ; Spine ; Vertebral development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Paraffin sections from vertebral columns of ten human embryos and fetuses ranging from stage 16 to the 12th week were stained with the FITC-coupled lectins PNA, RCA I, Con A and WGA in order to investigate changes in carbohydrate-binding sites during vertebral development. PNA revealed a specific binding site in the vertebral body blastema in the precartilaginous stage of development. Beginning with the 25-mm CRL embryo, PNA-binding sites occurred in the developing fibrous annulus and the inner zone of the intervertebral discs. The first binding sites for RCA I were seen in the extracellular matrix of vertebral bodies during the cartilaginous stage of vertebral development. During early ossification of the vertebrae, staining for RCA I-binding sites in the cytoplasm of the chondrocytes and the area around the future cartilaginous end-plates was observed. Con A bound to the chondrocyte cytoplasm, and also very strongly to notochordal cells in all developmental stages examined. WGA-binding sites appeared simultaneously with cartilage formation. Connective tissue components, e.g. ligaments, were diffusely stained by WGA. Also this lectin showed an affinity for vertebral body chondrocytes. We discuss the biochemical aspects of these lectin-binding sites, and their possible roles in the differentiation process of the human vertebral column. The results of this first lectin histochemical study on human vertebral development are compared with related results in other species.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. ; Stafa-Zurich, Switzerland
    Materials science forum Vol. 65-66 (Jan. 1991), p. 175-180 
    ISSN: 1662-9752
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In the present work we compared the appearance of carbohydrate binding sites for mannose, maltose, sialic acid andN-acetyl-glucosamine in the 11 to 13-day-old mouse embryo with the appearance of BSA and lectin binding sites. The carbohydrate-binding sites were localized with FITC-coupled neoglycoproteins, synthesized by chemical glycosylation of bovine serum albumin (BSA). These localizations were compared with binding of the FITC-labelled unglycosylated BSA. Furthermore the localizations of neoglycoprotein and BSA binding sites were correlated with binding of the FITC-labelled lectins WGA, RCA I and Con A. Initial appearance of neoglycoprotein binding sites occurred in the lens capsule of the 13 day old mouse embryo. Binding sites for the unglycosylated BSA appeared earlier, i.e. already in the 12-day-old embryo, in the basement membranes of the choroid plexus and the lung bud and lectin binding sites were seen in these structures in the 11-day-old embryo. The staining of the basement membrane and the lens capsule for BSA binding sites in the 12-and 13-day-old embryos correspond to WGA binding to these membranes. From these results we concluded that 1) specific carbohydrates which are probably involved in embryonic development appear much earlier in the embryo than the endogenous lectins which are able to react with these carbohydrates and 2) BSA is a protein which like WGA probably binds N-acetylglucosamine or sialic acid moieties.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In the present work we compared the appearance of carbohydrate binding sites for mannose, maltose, sialic acid and N-acetyl-glucosamine in the 11 to 13-day-old mouse embryo with the appearance of BSA and lectin binding sites. The carbohydrate-binding sites were localized with FITC-coupled neoglycoproteins, synthesized by chemical glycosylation of bovine serum albumin (BSA). These localizations were compared with binding of the FITC-labelled unglycosylated BSA. Furthermore the localizations of neoglycoprotein and BSA binding sites were correlated with binding of the FITC-labelled lectins WGA, RCA I and Con A. Initial appearance of neoglycoprotein binding sites occurred in the lens capsule of the 13 day old mouse embryo. Binding sites for the unglycosylated BSA appeared earlier, i.e. already in the 12-day-old embryo, in the basement membranes of the choroid plexus and the lung bud and lectin binding sites were seen in these structures in the 11-day-old embryo. The staining of the basement membrane and the lens capsule for BSA binding sites in the 12-and 13-day-old embryos correspond to WGA binding to these membranes. From these results we concluded that 1) specific carbohydrates which are probably involved in embryonic development appear much earlier in the embryo than the endogenous lectins which are able to react with these carbohydrates and 2) BSA is a protein which like WGA probably binds N-acetylglucosamine or sialic acid moieties.
    Type of Medium: Electronic Resource
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