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
Filter
  • Articles: DFG German National Licenses  (3)
  • Thromboxane synthase  (2)
  • Breast carcinoma  (1)
Source
  • Articles: DFG German National Licenses  (3)
Material
Years
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Localization of thromboxane synthase in human tissues by monoclonal antibody Tü 300 (1992)
    Springer
    Virchows Archiv 421 (1992), S. 249-254 
    Details
    ISSN: 1432-2307
    Keywords: Thromboxane ; Thromboxane synthase ; Immunohistochemistry ; Mononuclear phagocyte system ; Epithelia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Using the monoclonal antibody Tü 300 we localized thromboxane synthase, a secondary enzyme of the arachidonic acid cascade, employing the alkaline phosphatase anti-alkaline phosphatase method and indirect double labelling immunofluorescence in frozen sections of human tissues. Aside from platelets, the source of the antigen, all cells of the mononuclear phagocytic system were positive, including epithelioid cells and associated giant cells, starry sky macrophages, dendritic cells of T-cell areas, Langerhans cells and Kupffer cells. In addition, some epithelial cells such as epithelia of tonsillar crypts, reticular epithelia of the thymic cortex and ductular epithelia in liver, pancreas, female breast and salivary glands showed occasional focal reactivity for thromboxane synthase. We suggest that the mAb Tü 300 is a key marker for the macrophage system and the thromboxane generating system in normal and pathological conditions. It may detect functional activities of as yet unknown significance in some specialized epithelial cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01611182
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    The immunohistochemical reactivity of a new anti-epithelial monoclonal antibody (MAb b-12) against breast carcinoma and other normal and neoplastic human tissues (1988)
    Springer
    Virchows Archiv 413 (1988), S. 3-10 
    Details
    ISSN: 1432-2307
    Keywords: Breast carcinoma ; Adenocarcinoma ; Tumour cell heterogeneity ; Monoclonal antibody b-12 ; Tumour marker ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A mouse monoclonal antibody, MAb b-12, has been described previously (Stähli et al. 1985) which reacts with a Mr 350 kD glycoprotein with mucin-like characteristics (Stähli et al. 1987) expressed in cytoplasm and on the surface of human breast carcinoma cell lines (MCF-7 and ZR-75-1). In the present report the immunohistochemical reactivity of this MAb with normal and malignant human tissues is analyzed. Pre-experiments showed that the epitope b-12 is resistant to formalin treatment allowing the use of tissue processed by standard paraffin embedding methods. 167 normal and 408 neoplastic tissues were tested by indirect immunofluorescence or the avidin-biotin complex method. MAb b-12 stained the apical cytoplasm of secretory epithelia and their secretions including the acinar and ductular epithelia of the breast. It reacted with all breast carcinomas independent of their histological type or stage, frequently with all but in some cases with a fraction of the tumour cells. Some other carcinomas, primarily those of adenomatous differentiation, were also reactive. In these, however, the fraction of positive tumour cells was usually lower. The b-12 epitope is thus a marker for normal and neoplastic epithelia with secretory functions, particularly for breast carcinomas of all histological types and stages, and perhaps a differentiation marker for abortive adenomatous differentiation in solid carcinomas of the gastro-intestinal, uro-genital or respiratory tract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00844275
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    The localization of thromboxane synthase in normal and pathological human kidney tissue using a monoclonal antibody Tü 300 (1994)
    Springer
    Virchows Archiv 424 (1994), S. 69-74 
    Details
    ISSN: 1432-2307
    Keywords: Kidney ; Thromboxane ; Thromboxane synthase ; Tü 300 monoclonal antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Thromboxane, excreted in the urine in increased amounts in glomerular, vascular and tubulo-interstitial diseases, is considered to originate from the kidney. The localization of thromboxane synthase, a key enzyme of arachidonic acid metabolism, was studied in the human kidney by immunohistology using the monoclonal antibody Tü 300. In the interstitial tissue dendritic reticulum cells surrounding the tubules expressed high concentrations of the enzyme. In glomeruli the enzyme was weakly expressed in podocytes. This was confirmed by co-localization with an antiserum directed to podocalyxin, a marker of the visceral epithelial cells. In the study of various kidney diseases, massive accumulation of thromboxane synthase containing cells was observed in interstitial diseases, whereas in glomerular diseases there were no differences from normal kidney; in a case of thrombotic microangiopathy podocytes exhibited an increase in thromboxane-synthase. The thromboxane-synthase positive infiltrating interstitial cells were shown by conventional light microscopy to be mononuclear phagocytic cells. The physiological sources of renal thromboxane are dendritic reticular cells and podocytes. In interstitial renal disease infiltrating cells of the monocyte/macrophage system constitute the major site of thromboxane synthesis. In glomerular disease, a characteristic alteration of thromboxane-synthase was not found.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197395
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...