Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Influence of O-glycans in IgA1 hinge on its biological activity in human mesangial cells: A comprehensive gene expression profiling analysis using cDNA array (2001)
    Melbourne, Australia : Blackwell Science Pty
    Nephrology 6 (2001), S. 0 
    Details
    ISSN: 1440-1797
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background: The IgA1 molecule, which is predominantly deposited in glomeruli of IgA nephropathy, has the characteristic O-glycan side chain in its hinge region. Several lines of evidence have demonstrated that underglycosylated IgA1 acquires self-aggregation1 and binding affinities to the extra-cellular matrix,1,2 resulting in deposition in the glomeruli.3,4 However, there is little information concerning actual biological activities of the underglycosylated IgA1 deposited in glomeruli, which lead to mesangial cell proliferation and/or matrix expansion.Aim: To clarify the influence of O-glycan side chain in the hinge of IgA1 on its biological activity in mesangial cells, we performed a comprehensive gene expression profiling analysis of human cultured mesangial cells stimulated by enzymatically underglycosylated IgA1 using cDNA array.Methods: IgA1 was purified by affinity chromatography using anti IgA column followed by Jacalin column. Asialo/agalacto IgA1 was obtained by enzyme digestion using sialidase and β-galactosidase. Heat aggregated IgA1 was obtained by incubation at 63°C for 150 min. Cultured human mesangial cells were stimulated for 3 h by non-treated IgA1, heat aggregated IgA1 or asialo/agalacto IgA1, respectively, and total RNA was obtained. Only the enzyme stimulation was performed as a negative control for asialo/agalacto IgA1. After DNase treatment, isotope labelled probes were prepared by reverse transcription and hybridized to the Atlas Human 1.2 Array (CLONTECH, Palo Alto, CA, USA) according to the manufacturer’s protocol. A total of 1176 arrayed genes were quantitatively evaluated using BAS.Results: Expression profiles of 1176 genes were obtained. In all experiments, none of the three negative controls on the cDNA array was detected. The expression profiles of mesangial cells by each IgA1 stimulation resembled one another, but they were widely different from that of mononuclear cells. On the whole, 10% of the genes expressed in the mesangial cells were up-regulated by asialo/agalacto IgA1 stimulation compared to that by enzyme stimulation. The results suggested that under-O-glycosylated IgA1 has a biological function in human mesangial cells in vitro. In good agreement with previous studies,5 heat aggregated IgA1 stimulation up-regulated IL-6 and TNF-α expressions in mesangial cells compared to by non-treated IgA1. Asialo/agalacto IgA1 stimulation also up-regulated these molecules, suggesting its pathogenetic role in IgA nephropathy. However, since a similar tendency was revealed by enzyme stimulation alone, further study may be necessary to establish these observations.Conclusion. In the present study, we investigated the comprehensive expression profiles of mesangial cells stimulated by various types of IgA1 using cDNA array. This approach may serve as a useful database not only to evaluate the biological activities of under-O-glycosylated IgA1 but also to elucidate the pathogenesis of IgA nephropathy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1440-1797.2001.00018.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of S-100 protein in human cerebral and cerebellar cortices (1983)
    Springer
    Cellular and molecular life sciences 39 (1983), S. 335-337 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary S-100 protein, a highly acidic protein specific to the nervous system, is immunohistochemically localized exclusively in glial cells, but not in any type of neuron in human cerebral and cerebellar cortices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01955336
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    S-100 protein in human glial tumours (1982)
    Springer
    Acta neurochirurgica 65 (1982), S. 239-251 
    Details
    ISSN: 0942-0940
    Keywords: Human glial tumour ; S-100 protein ; differentiation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The authors studied a total of 48 human glial tumours for S-100 protein, an extremely acidic protein specific to the nervous system, by immunohistochemistry and by micro-complement fixation assay in order to evaluate S-100 protein as an index for malignancy of glial tumours. All of 48 glial tumours analyzed in the present study demonstrated variable amounts of S-100 protein which might serve as a biochemical cell marker for glial tumours. The mean value of S-100 protein content in 3 ependymomas is higher than those of 19 low-grade (grades I, II) astrocytomas and 26 high-grade (grades III, IV) astrocytomas, being lowest in the latter. A statistically significant (p〈0.001) difference in S-100 protein levels between low-and high-grade astrocytomas is observed, but not for ependymoma. At present, however, no correlation can be found between S-100 protein content of a tumour and the patient's survival time. Immunoperoxidase staining for S-100 protein in high-grade astrocytomas is generally weak in intensity and heterogeneous throughout the section, whereas that in low-grade astrocytomas and ependymomas is relatively strong and homogeneous, indicating that high-grade astrocytomas consist of a more heterogeneous population of tumour cells in terms of S-100 protein. These results show that the investigation of S-100 protein in a glial tumour is valuable to a certain extent in assessing the degree of differentiation or malignancy of the tumour.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01405850
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Localization of SV40 T antigen in mitotic cells by an immunoperoxidase method (1980)
    Springer
    Cellular and molecular life sciences 36 (1980), S. 1053-1054 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The immunoperoxidase technique has clearly demonstrated that SV40 T antigen is dissociated from the chromosomes in mitotic cells, and massive transport of T antigen from the cytoplasm to the nucleus appears to take place during or immediately after the telophase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01965963
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Immunoelectron microscopic localization of S-100 protein in cultured rat glioma cells (1978)
    Springer
    Acta neuropathologica 44 (1978), S. 159-162 
    Details
    ISSN: 1432-0533
    Keywords: S-100 Protein ; Immunoelectron microscopy ; Cultured rat glioma cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Immunoelectron microscopic localization of the nervous system specific protein S-100 in the cultured rat glioma cells was successfully conducted by an unique immunocytochemical technique using peroxidase-labeled antigen binding Fab' fragments. The intensely electron dense reaction product for S-100 protein was localized mainly at ribosome granules associated with endoplasmic reticulum membranes and at free ribosome granules. S-100 protein was also associated to some extent with the cytoplasmic and nuclear membranes. A positive reaction was localized at the nuclear pores as if it were being prevented from entering into the nucleus. No activity was found in the nucleoplasm except for a slightly positive reaction product associated with nucleolus. The possible role for S-100 protein in neural cells was discussed in relation to the nuclear acidic proteins involved in genomic regulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00691485
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Immunohistochemical demonstration of IgG in meningioma (1981)
    Springer
    Acta neurochirurgica 55 (1981), S. 201-211 
    Details
    ISSN: 0942-0940
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Twenty human meningiomas were examined for IgG and IgM by the direct immunofluorescence or immunoperoxidase methods, or both. IgG was conspicuously found in and around the blood vessels, whorls, and psammoma bodies. It was also clearly present on the cytoplasmic membranes of the tumour cells. On the other hand, IgM was seen only within the blood vessels. Significance of these findings is briefly discussed including possible humoral immune reactions in regard to whorl and psammoma body formation in meningioma.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01808437
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Open spaces and molecular motions of polyether-based network polymers probed by positron annihilation (1998)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 36 (1998), S. 1919-1925 
    Details
    ISSN: 0887-6266
    Keywords: positron annihilation ; polymer electrolyte ; network polymer ; poly(glycidyl ether) ; polyether ; Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The lifetimes of positrons have been measured for network polymers based on polyethers. From the temperature dependence of the lifetime of ortho-positronium (o-Ps), τ3, for the network polymer of poly(ethylene oxide-co-propylene oxide) [P(EO/PO)], an onset temperature for limited local motions of molecules, Tγ, and the glass transition temperature, Tg, were determined to be 57 and 201 K, respectively. For the network polymer of poly[EO-co-2-(2-methoxyethoxy)ethyl glycidyl ether] [P(EO/MEEGE)], Tγ and Tg were determined to be 57 and 185 K, respectively. For both specimens, above 270 K, the observed linear temperature dependence of τ3 was attributed to the thermal expansion of open spaces in a liquid state. In the temperature range between Tγ and 270 K, for the P(EO/MEEGE) network, τ3 was longer and its intensity was smaller than those for the P(EO/PO) network. These results were attributed to the increase in the size of open spaces for the P(EO/MEEGE) network polymer and the blocking of these regions by motions of side chains and chain ends. © 1998 John Wiley & Sons, Inc. J Polym Sci B: Polym Phys 36: 1919-1925, 1998
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...