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  • 1
    Electronic Resource
    Electronic Resource
    Disturbed expression of ribonucleotide reductase and cytokeratin polypeptides in focal epithelial hyperplasia (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 15 (1986), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Four cases of focal epithelial hyperplasia (FEH) were studied immunohistochemically, using monoclonal antibodies against the M1 subunit of ribonucleotide reductase and different cytokeratin polypeptides. The FEH lesions showed, compared to normal oral mucosa, extensive alterations in their staining patterns. This included ectopic suprabasal M1 staining and the novel expression of cytokeratin polypeptides differing from those previously reported for other HPV infections. The results arc discussed in relation to the causative agent, human papillomuvirus, and its expression in focal epithelial hyperplasia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1986.tb00619.x
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of cytokeratins in odontogenic jaw cysts: monoclonal antibodies reveal distinct variation between different cyst types (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 16 (1987), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Immunostaining with monoclonal antibodies was used to study and compare the cytokeratin content of odontogenic cysts and normal gingival epithelium. Two monoclonal antibodies, PKK2 and KA1, stained the whole epithelium in all cyst samples. In gingivu, PKK2 gave a suprabasal staining and KA1 reacted with all epithelial cell layers. Antibodies PKK1, KM 4.62 and Ks 8.12 gave a heterogeneous staining in follicular and radicular cysts. In keratocysts and in gingiva PKK1 and KM 4.62 reacted mainly with basal cells and Ks 8.12 gave a suprabasal staining. Antibodies reacting with the simple epithelial cytokeratin polypeptide No. 18 (PKK3, Ks 18.18) recognized in gingiva only solitary cells compatible with Merkel cells. In a case of follicular ameloblastoma a distinct staining of tumor epithelium was revealed with these antibodies. In 2 follicular cysts, but not in other cyst types, a layer of cytokeratin 18-positive cells was revealed. KA5 and Kk 8.60 antibodies, reacting exclusively with keratinizing epithelia, including normal gingiva, gave no reaction in radicular cysts, keratocysts and ameloblastoma. Two of the follicular cysts, were negative for PKK3 and Ks 18.18, but reacted strongly with KA5 and Kk 8.60. The present results show that odontogenic jaw cysts have distinct differences in their cytokeratin content. With the exception of some follicular cysts, they lack signs of keratinizing epithelial differentiation. Only follicular cysts appear to share with some types of ameloblastoma the expression of cytokeratin polypeptide No. 18.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1987.tb00705.x
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  • 3
    Electronic Resource
    Electronic Resource
    Expression of metalloproteinase genes in human prostate cancer (1991)
    Springer
    Journal of cancer research and clinical oncology 117 (1991), S. 144-150 
    Details
    ISSN: 1432-1335
    Keywords: Metalloproteinase ; Collagenase ; Prostate adenocarcinoma ; Matrix metalloproteinase-7 (MMP-7)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Twenty-five surgical specimens of malignant human prostate, 3 lymph nodes with metastatic prostate carcinoma, 11 normal human prostates, as well as 3 human prostate cell lines (DU-145, PC3 and LNCaP) were examined for the expression of the human matrix metalloproteinase-7 gene (MMP-7) from the human collagenase family (originally called PUMP-1 for putative metalloproteinase-1) [Quantin et al. (1989) Biochemistry 28:5327–5334; Muller et al. (1988) Biochem J 253:187–192; Matrisian and Bowden (1990) Semin Cancer Biol 1:107–115]. Northern blots were prepared using total RNA extracted from 18 prostate adenocarcinomas, 2 lymph nodes with metastatic prostate carcinoma and 11 normal human prostates. When the northern blots were hybridized with a32P-labeledMMP-7 cDNA probe, a 1.2-kb mRNA was detected in 14 out of 18 prostate adenocarcinomas, 1 out of 2 metastatic lymph nodes, and 3 out of 11 normal prostates. The 3 human prostate cell lines did not show any evidence of theMMP-7 transcript. In situ hybridization was conducted to localize theMMP-7 mRNA to individual cells using a35S-labeledMMP-7 cRNA. In situ hybridization was carried out on snap-frozen tissue sections of 7 prostate adenocarcinomas and 3 lymph nodes containing metastatic prostate adenocarcinoma using the same tissues previously probed by northern analysis as well as new samples. In situ hybridization revealed that theMMP-7 gene was expressed in the epithelial cells of primary prostate adenocarcinoma as well as in invasive and metastatic cells.MMP-7 expression was also seen focally in some dysplastic glands but not in stroma. Additional northern blot analysis was performed using probes to human type-IV collagenase, type-I collagenase and stromelysin I in human prostate adenocarcinoma as well as normal prostate tissue. Our results indicated that 6 out of 10 adenocarcinoma samples and none of the 4 normal samples were positive for type-IV collagenase transcripts. Tissue samples were also examined for the expression of type-I collagenase (9 adenocarcinomas and 4 normal) and stromelysin I (13 adenocarcinomas) by northern analysis. None of the tissues was found to express the transcripts of interest at detectable levels. These data suggest that certain metalloproteinases are present in prostatic adenocarcinoma and may play a role in invasion and metastasis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01613138
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and characterization of human placental chorionic villar extracellular matrix (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 12 (1979), S. 457-466 
    Details
    ISSN: 0091-7419
    Keywords: human placental basement membrane ; extracellular matrix ; human chorionic villar basement membrane ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The cell-free extracellular matrix of human placental chorionic villi has been prepared by a procedure employing extraction of the terminal villar fragments with the detergents Triton X-100 and sodium deoxycholate. The isolated human placental extracellular matrix retains an intact, but collapsed, histoarchitecture, as observed by scanning and transmission electron microscopy. It remains intact, in large part because of the presence of continuous sheets of villar basement membranes and associated interstitial collagen fibers and scattered patches of fibrin. The staining characteristics and chemical composition of the isolated human placental extracellular matrix are similar to those reported for basement membranes in several tissues and indicate the presence of collagen-like and glycoprotein components in this preparation. Gel electrophoresis of urea-SDS-mercaptoethanol extracts of the matrix showed that it consists of several polypeptide components of various molecular weights, some of which are associated into high molecular weight complexes by disulfide bonds.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400120405
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    Paper (German National Licenses)
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