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  • 1
    Electronic Resource
    Electronic Resource
    Lectin-binding patterns in the embryonic human paraxial mesenchyme (1993)
    Springer
    Anatomy and embryology 188 (1993), S. 579-585 
    Details
    ISSN: 1432-0568
    Keywords: Human embryo ; Paraxial mesenchyme ; Sclerotome ; Lectins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The paraxial mesenchyme in seven human embryos aged between Carnegie stages 12 and 17 was studied by lectin histochemistry with the lectins AIA, Con A, GSA II, LFA, LTA, PNA, RCA I, SBA, SNA, WGA. The paraxial mesenchyme was found to be segmented into sclerotomes by intersegmental vessels and from late stage 12 by intrasclerotomal clefts dividing each sclerotome into a cranial and caudal half. The lectins Con A, GSA II, LFA, LTA, SBA and SNA did not react at all in the paraxial mesenchyme. Staining for AIA, PNA, RCA I and WGA was found in the developing sclerotomes. However, no differences in the staining pattern between the two sclerotomal halves could be seen. It was striking that in contrast to the chick embryo no differences in binding for PNA between the cranial and caudal sclerotomal parts was observed. These findings reveal that PNA-binding sites do not play the same functional role in segmented axonal outgrowth and neural crest immigration into cranial sclerotomal halves in the human embryo, as found in chick embryonic development. Beginning with the stage 16-embryo, the already condensed caudal sclerotomal halves express Con A-, RCA- and PNA-binding sites. The staining for PNA in particular marked the differentiation of chondrogenous structures developing in this half. From the late stage 12 or stage 13, the walls of intersegmental and other vessels showed binding sites for AIA, PNA, RCA I, SNA and WGA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00187013
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  • 2
    Electronic Resource
    Electronic Resource
    Ultrastructural localization of laminin subunits during the onset of mesoderm formation in the mouse embryo (1993)
    Springer
    Anatomy and embryology 187 (1993), S. 601-605 
    Details
    ISSN: 1432-0568
    Keywords: Mouse embryo day 6 and 7 ; Direct immunogold histochemistry ; Laminin subunits of A- and B1-chains ; Mesoderm formation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Using ultrastructural immunogold histochemistry on LR-Gold-embedded 6- and 7-day-old mouse embryos we investigated the appearance of the A- and B1-chains of the laminin molecule during mesoderm formation. With the help of antibodies against the A-chain and the E4 fragment of the B1-chain of the laminin molecule we were able to detect the subunits in vivo. Staining for the E4 fragment of the short arm of the laminin molecule from day 6 was negative. In contrast, strong staining for the A-chain of laminin was observed. Our results show, that the A-chain of laminin appears before the B1-chain in the 6-day-old mouse embryo before a basement membrane is seen between the ectodermal and entodermal cell layers. Furthermore, the staining pattern indicates, that the laminin molecule changes its orientation in the basement membrane of the ectoderm during mesoderm formation. On day 7 staining for the A-chain of laminin and for the E4 fragment was seen in a random distribution throughout the entire basement membrane, whereas in areas were the onset of mesoderm formation was taking place, the E4 fragment was restricted to the edge of the disintegrating basement membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00214439
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  • 3
    Electronic Resource
    Electronic Resource
    Lectin binding pattern in the embryonal and early fetal human vertebral column (1991)
    Springer
    Anatomy and embryology 184 (1991), S. 345-353 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00957896
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  • 4
    Electronic Resource
    Electronic Resource
    Epiphysial ossification centres in iliosacral joints: anatomy and computed tomography (1993)
    Springer
    Surgical and radiologic anatomy 15 (1993), S. 131-137 
    Details
    ISSN: 1279-8517
    Keywords: Sacroiliac joint ; Computed tomography ; Secondary ossification centres ; Os sacrum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Résumé Des formations osseuses apparemment bilatérales, de formes et tailles différentes, localisées dans les parties antéro-supérieures et inférieures des articulations sacroiliaques, ont été observées sur les images de coupes axiales de la région pelvienne chez des patients jeunes. Aucune autre modification pathologique n'a été notée au niveau des articulations sacro-iliaques de ces individus. Chez l'un des patients, les structures osseuses pouvaient aussi être observées sur les radiographies standard. Nous avons aussi étudié cette articulation chez 3 sujets anatomiques juvéniles, par la radiographie, la TDM, l'étude macroscopique et histologique. Chez deux d'entre eux des formations osseuses semblables à celles observées chez les patients jeunes pouvaient être détectées sur les coupes TDM. Les recherches macroscopiques ont montré que ces structures étaient des points d'ossification secondaires localisés dans le cartilage articulaire de la partie latérale du sacrum en regard du 1er et du 3e segments sacrés. Si l'on se réfère à une littérature anatomique plus ancienne, ces points d'ossification épiphysaires contribuent à la surface auriculaire de la partie latérale du sacrum et à la surface libre latérale des parties caudales du sacrum. Ils peuvent être observés entre 12 et 25 ans et commencent à fusionner avec les parties latérales aux environs de la 18e année. Sur les bassins osseux provenant de pièces juvéniles conservées, les ossicules libres n'ont pas pu être décelés dans la région des articulations sacroiliaques. Les particularités histologiques du processus d'ossification observé sont discutés. Ces points d'ossification physiologiques doivent être distingués des altérations pathologiques apparaissant au scanner comme des structures osseuses ou assimilées.
    Notes: Summary Bilateral apparently bony structures of different forms and sizes located in the inferior and superior ventral parts of the sacroiliac joints were observed on axial CT images of the pelvic region of juvenile patients. No other pathological changes were noted in the sacroiliac joints of these individuals. In one patient the bony structures could also be seen on a conventional plain radiograph. We also examined 3 juvenile autopsy specimens of this joint using radiology, CT, macroscopical evaluation and histology. In two of them, structures could be detected on the CT scans which were similar to those observed in the young patients. Macroscopic investigations revealed the structures to be secondary ossification centres located in the articular cartilage of the lateral part of the os sacrum at the levels of the first and third sacral segments. According to older anatomical literature, these epiphysial ossification centres contribute to the auricular surface of the lateral part of the os sacrum and the free lateral surface of the inferior sacral parts. They can be observed between the ages of 12 and 25 years and begin to synostose with the lateral part around the age of 18 years. In macerated juvenile specimens of the bony pelvis, free ossicles were not detectable in the region of the sacroiliac joints. Histological peculiarities of the ossification process observed are discussed. These physiologically occurring ossification centres are to be differentiated from pathological alterations appearing as bony or bone-like structures on CT scans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01628312
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  • 5
    Electronic Resource
    Electronic Resource
    Ultrastructural localization of WGA, RCA I, LFA and SBA binding sites in the seven-day-old mouse embryo (1990)
    Springer
    Histochemistry and cell biology 94 (1990), S. 525-530 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In the present investigation we localized binding sites for the lectins WGA (wheat germ agglutinin), RCA I (Ricinus communis agglutinin), LFA (Limax flavus agglutinin) and SBA (soya bean agglutinin) in the 7-day-old mouse embryo at the ultrastructural level. Lectin binding sites were localized on formaldehyde fixed embryos, embedded in LR-Gold, using gold-labelled lectins. Binding sites for WGA and RCA I were observed at the surface of the embryonic ectoderm oriented towards the proamnion cavity and the outer surface of the extraembryonic and the embryonic endoderm. Staining for SBA and LFA binding sites was seen in the basement membrane of the ectoderm. Moreover, binding sites for LFA were observed in the nucleoli of cells of the ectodermal, the mesodermal and the endodermal layer and in free ribosomes located in the cytoplasm of these cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00272617
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  • 6
    Electronic Resource
    Electronic Resource
    Correlations between the binding of neoglycoproteins, bovine serum albumin (BSA) and lectins in 10 to 13-day-old mouse embryos (1991)
    Springer
    Histochemistry and cell biology 95 (1991), S. 297-301 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00745002
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  • 7
    Electronic Resource
    Electronic Resource
    Correlations between the binding of neoglycoproteins, bovine serum albumin (BSA) and lectins in 10 to 13-day-old mouse embryos (1991)
    Springer
    Histochemistry and cell biology 95 (1991), S. 297-301 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00266780
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  • 8
    Electronic Resource
    Electronic Resource
    Postembedding immunogold histochemistry for the localization of laminin and its E4 and P1 fragments in mouse kidney embedded in LR-White and LR-Gold (1991)
    Springer
    Journal of molecular histology 23 (1991), S. 267-272 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A method is presented which permits the ultrastructural localization of laminin and its E4 and P1 subunits in the renal cortex of the mouse embedded in LR-White or LR-Gold. It was performed with postembedding immunogold histochemistry using polyclonal antibodies against either the entire laminin molecular or the E4 fragment or with a monoclonal antibody against the P1 fragment. Localization of laminin was achieved in LR-White and in LR-Gold embedded kidney. Using polyclonal antibodies against the entire laminin molecule, laminin could be localized with direct as well as with indirect immunogold histochemistry with a gold labelled IgG as secondary antibody. In contrast, immunostaining for the E4 or the P1 fragments was possible only with antibodibodies directly labelled with gold.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01045045
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  • 9
    Electronic Resource
    Electronic Resource
    Light and electron microscopical immunohistochemical localization of the small proteoglycan core proteins decorin and biglycan in human knee joint cartilage (1994)
    Springer
    Journal of molecular histology 26 (1994), S. 939-945 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of decorin and biglycan was investigated at the light and electron microscopical level in adult human articular cartilage. In general, the amount of decorin and biglycan was found to decrease with the depth of the layer of the cartilage. Decorin was found in the interterritorial matrix where most of the collagen is located. This fits in well with the assumption that decorin may modulate collagen metabolism. Biglycan was found next to the chondrocytes in the pericellular matrix and is assumed to be responsible for cellular activities. At the ultrastructural level, decorin was localized in the interterritorial matrix and in vesicles in chondrocytes. Biglycan was found, usually though not exclusively in the pericellular matrix. Both small proteoglycans were detected close to and on the collagen fibres and also associated with the more globular structures of the matrix between the fibrils. A double-staining approach revealed that the two molecules could be located along the same collagen fibril. However, staining for biglycan and decorin was not observed simultaneously within the same region of the fibre.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00174010
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  • 10
    Electronic Resource
    Electronic Resource
    Light and electron microscopical immunohistochemical localization of the small proteoglycan core proteins decorin and biglycan in human knee joint cartilage (1994)
    Springer
    Journal of molecular histology 26 (1994), S. 939-945 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of decorin and biglycan was investigated at the light and electron microscopical level in adult human articular cartilage. In general, the amount of decorin and biglycan was found to decrease with the depth of the layer of the cartilage. Decorin was found in the interterritorial matrix where most of the collagen is located. This fits in well with the assumption that decorin may modulate collagen metabolism. Biglycan was found next to the chondrocytes in the pericellular matrix and is assumed to be responsible for cellular activities. At the ultrastructural level, decorin was localized in the interterritorial matrix and in vesicles in chondrocytes. Biglycan was found, usually though not exclusively in the pericellular matrix. Both small proteoglycans were detected close to and on the collagen fibres and also associated with the more globular structures of the matrix between the fibrils. A double-staining approach revealed that the two molecules could be located along the same collagen fibril. However, staining for biglycan and decorin was not observed simultaneously within the same region of the fibre.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02388571
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