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  • 1
    Electronic Resource
    Electronic Resource
    Inductive Interactions in Heart Development (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 588 (1990), 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.1749-6632.1990.tb13193.x
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  • 2
    Electronic Resource
    Electronic Resource
    Surface coat material associated with the developing otic placode/vesicle in the chick (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 220 (1988), S. 198-207 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Surface coat material (SCM) has been illustrated in association with the apical surfaces of numerous epithelia during morphogenesis. This study investigates the development of a SCM associated with the invaginating otic placode/vesicle in the chick. Glycoconjugate containing SCM was retained by the inclusion of cetylpyridinium chloride (CPC) in the fixative, histochemically visualized by using ruthenium red (RR) staining, and viewed by scanning (SEM) or transmission (TEM) electron microscopy. Initial characterization of the glycoconjugates present in this material was elucidated by using lectins conjugated to fluorescein isothiocyanate. Lectins utilized included concanavalin A (Con A), wheat germ agglutinin (WGA), and soybean agglutinin (SBA). Invagination of the otic placode was apparent as early as stage 12. By stage 15 the vesicle was beginning to separate from the surface ectoderm as evidenced by its aperture, which was altered in shape and reduced in size. All embryos fixed with glutaraldehyde containing either CPC or RR were shown to possess SCM associated with the surface ectoderm, particularly in the area of the otic placode/vesicle. Additional embryos were processed by cryofixation without prior alehyde fixation; these also exhibited SCM. All lectins labelled the epithelium of the otic placode/vesicle. However, their binding patterns were not identical. The binding of Con A and WGA remained constant over the stages studied, while SBA increased as the otic vesicle developed. The data clearly indicate that otic placode morphogenesis is accompanied by the synthesis of SCM rich in glycoconjugates.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092200211
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  • 3
    Electronic Resource
    Electronic Resource
    Partial purification of HLAMP-1 provides direct evidence for the multicomponent nature of the particulate matrix associated with cardiac mesenchyme formation (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 66 (1997), S. 112-122 
    Details
    ISSN: 0730-2312
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: H-LAMP-1 is a 283 kDa protein that is involved in the transformation of endothelial cells into mesenchyme within the AV canal and proximal outflow tract of the heart. This protein is part of the particulate matrix that has been suggested to be composed of multicomponent complexes that have been termed cardiac adherons. However, to date no direct evidence has been provided that these proteins are complexed into an adheron-like particle. This report provides the first such evidence by showing that purification of hLAMP-1, under gentle conditions, results in the isolation of multiple bands of similar molecular weight within the fractions that contain anti-hLAMP-1 activity. J. Cell. Biochem. 66:112-122, 1997. © 1997 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Multiple glycoproteins localize to a particulate form of extracellular matrix in regions of the embryonic heart where endothelial cells transform into mesenchyme (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 232 (1992), S. 285-292 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Cells derived from an epithelial-mesenchymal transformation within the atrioventricular canal and outflow tract are involved in the partitioning of the early embryonic heart into a four-chambered organ. This transformation process has been shown to proceed from an inductive interaction between the myocardium and competent, target endothelial cells within these regions of the heart. Interestingly, immunohistochemistry revealed the presence of fibronectinpositive particulates within the matrix of mesenchyme-forming regions (Mjaatvedt et al., 1987). This particulate matrix is extractable by EDTA and can elicit the epithelial-mesenchymal transformation in culture (Mjaatvedt and Markwald, 1989). Analysis of EDTA extracts of embryonic heart tissue revealed the presence of fibronectin and about 40 unidentified proteins, 6 of which appeared to be enriched in the biologically active 100,000g pellet fraction (Mjaatvedt and Markwald, 1989). Based on these and other data we have proposed that the particulate matrix is composed of a multicomponent complex of fibronectin and one or more of the low-molecular-weight proteins in this pellet. The purpose of the present study was to begin a biochemical characterization of the nonfibronectin proteins thought to be present in the matrix particulates. Given that many matrix constituents are glycoproteins, lectins were used to initially characterize the particulate constituents. Of the lectins tested, soybean agglutinin (SBA) was found to be specific only for matrix particulates. Histochemical analyses showed that SBA and antibodies against fibronectin colocalized regionally and temporally to the same matrix particulates in embryonic heart tissue. SBA-agarose affinity chromatography resulted in the isolation of two major (56 and 69 kDa) and six minor (28, 46, 50, 53, 126, 220 kDa) proteins from EDTA extractable heart matrix. Temporal lectin histochemical studies indicate that SBA-positive particulates are present in the matrix prior to mesenchyme formation, but are absent shortly after the transformation event. These observations support our hypothesis that one or more of these SBA-positive glycoproteins participate in the endothelial-mesenchymal transformation of cardiac endothelium.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092320213
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    Paper (German National Licenses)
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