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  • 1
    Electronic Resource
    Electronic Resource
    Increased activity of dipeptidyl peptidase IV in serum of hepatoma-bearing rats coincides with the loss of the enzyme from the hepatoma plasma membrane (1986)
    Springer
    Cellular and molecular life sciences 42 (1986), S. 826-828 
    Details
    ISSN: 1420-9071
    Keywords: Dipeptidyl peptidase IV ; hepatoma rats ; cancer markers ; immunofluorescence ; cytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The specific activity of dipeptidyl peptidase IV (DPPIV E.C. 3.4.14.-) in the plasma membrane of Morris hepatoma 9121 or hepatoma 7777 was 3.5% and 2.9%, respectively, of that in the plasma membrane of rat liver. The enzyme activity in the serum of hepatoma-bearing rats was 141% (hepatoma 91219) and 162% (hepatoma 7777) of the normal value. cytochemical investigation showed that the DPP IV activity was almost completely absent from the hepatoma cell plasma membrane and was not sequestered within these cells. Indirect immunofluorescence staining with a polyclonal antibody directed against DPP IV indicated that the loss of activity was due to the absence of DPP IV molecules in the plasma membrane. The possibility that the enzyme is transferred from the membrane into the serum as a result of structural alterations is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01941540
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  • 2
    Electronic Resource
    Electronic Resource
    Direct evidence for the binding of rat liver DPP IV to collagen in vitro
    Amsterdam : Elsevier
    Experimental Cell Research 178 (1988), S. 64-72 
    Details
    ISSN: 0014-4827
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0014-4827(88)90378-3
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  • 3
    Electronic Resource
    Electronic Resource
    Rapid purification of dipeptidyl peptidase IV from rat liver plasma membrane
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 924 (1987), S. 543-547 
    Details
    ISSN: 0304-4165
    Keywords: (Rat liver plasma membrane) ; Dipeptidyl peptidase IV ; Proteinase purification
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0304-4165(87)90170-X
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution of glycosyltransferases among Golgi apparatus subfractions from liver and hepatomas of the rat
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 1115 (1991), S. 108-122 
    Details
    ISSN: 0304-4165
    Keywords: (Rat) ; Glycosyltransferase ; Golgi apparatus ; Hepatoma ; Liver
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0304-4165(91)90019-D
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  • 5
    Electronic Resource
    Electronic Resource
    Glaskapillaren zur gaschromatographischen Analyse methylierter Purine und Pyrimidine
    Amsterdam : Elsevier
    Journal of Chromatography A 178 (1979), S. 330-336 
    Details
    ISSN: 0021-9673
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0021-9673(00)89726-5
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  • 6
    Electronic Resource
    Electronic Resource
    Identification of a 110-kDa glycoprotein involved in cell-substratum adhesion
    Amsterdam : Elsevier
    FEBS Letters 204 (1986), S. 57-60 
    Details
    ISSN: 0014-5793
    Keywords: (Hepatoma cell) ; Cell-substratum adhesion ; Glycoprotein ; Plasma membrane
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)81387-4
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  • 7
    Electronic Resource
    Electronic Resource
    Dipeptidyl peptidase (DPP) IV in rat organs (1988)
    Springer
    Histochemistry and cell biology 89 (1988), S. 151-161 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunohistochemistry and activity histochemistry were used to study the localization of dipeptidyl peptidase (DPP) IV in rats. For immunohistochemistry, polyclonal as well as monoclonal anti-DPP IV antibodies were employed. The pattern of DPP IV immunoreactivity, determined with polyclonal anti-DPP IV antibody, corresponds to the histochemical pattern found for the enzymic activity of DPP IV. Immunoreactivity was present, in addition, in nerve cells, lateral membranes of certain surface epithelia, e.g., Fallopian tube, uterus and vesicular gland, in the luminal cytoplasm of e.g., vesicular gland epithelium, and in mucous cells of Brunner's gland. The monoclonal antibodies against DPP IV recognized four different epitopes (A D) of the DPP IV molecule, and revealed that certain epitopes were not detectable by immunohistochemistry in some organs. Generally, the staining intensities for epitopes A, B, C and D decreased in that order. Usually, the monoclonal antibodies against epitopes A and B showed similar reaction patterns to those as obtained with the polyclonal antibody. Epitope D was recognized in the lumen of the duct system of exocrine glands and the intestine. Further-more, high reactivity of this epitope was detected in goblet cells of the intestine, where no DPP IV activity was present.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489918
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  • 8
    Electronic Resource
    Electronic Resource
    Proteases in the human full-term placenta (1987)
    Springer
    Histochemistry and cell biology 86 (1987), S. 405-413 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Aminopeptidase A, not yet defined aminopeptidases and endopeptidases, dipeptidyl peptidase I, II and IV, γ-glutamyl transferase and oxytocinase were investigated in the normal human full-term placenta using qualitative (catalytic) cytochemistry, isoelectric focusing, immunocytochemistry and kinetic fluorometry. Aminopeptidase A could be visualized cytochemically in the smooth muscle cells of the chorionic plate, stem villi and basal plate blood vessels. Aminopeptidases were found in connective tissue fibres of the chorionic plate, villous stroma, basal plate and paraplacenta. Dipeptidyl peptidase IV was detected at the same sites as the aminopeptidases and, in addition, in amniotic epithelial cells, fibroblasts of the villous stroma, endothelium of chorinic plate and villous blood vessels as well as in the basophilic cytotrophoblast cells (x-cells) of the basal plate and paraplacenta, and it possibly also occurred in some domains of the plasma membrane of the syncytiotrophoblast and cytotrophoblast cells. The x-cells surrounded the fetus in the form of a dipeptidyl peptidase IV-positive shell at the border to the mother. The enzyme represented the first specific marker for x-cells. Dipeptidyl peptidase I and II were primarily found in Hofbauer cells (macrophages) of the villous stroma, but also in the syncytiotrophoblast, other villous stromal cells and cells of the chorionic and basal plate. γ-Glutamyl transferase was present in some connective tissue elements of the chorionic plate. Oxytocinase and endopeptidases were not detected. Isoclectric focusing of proteases revealed different molecular forms of dipeptidyl peptidase IV in the paraplacenta and villous tree, while the aminopeptidases shared the same pattern in both regions. Immunocytochemical staining of dipeptidyl peptidase IV in the villous tree resembled the pattern obtained by catalytic cytochemistry except for the blood vessel endothelium and the x-cells of the basal plate. Fluorometrically, all proteases were more active in the villous tree than in the paraplacenta. The kinetic measurements revealed the highest hydrolysis rates for dipeptidyl peptidase IV followed by the aminopeptidases. In contrast to eatalytic cytochemistry all proteases were detectable when using fluorometry.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495002
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  • 9
    Electronic Resource
    Electronic Resource
    Increased expression of a high molecular weight matrix component in rat hepatocellular carcinoma (1987)
    Springer
    Histochemistry and cell biology 87 (1987), S. 237-242 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The urea extract of the glycoproteins from the extracellular matrix of rat liver has been compared with that of Morris hepatoma 7777. A high molecular weight glycoprotein present in Morris hepatoma 7777 was not found in the extract of liver matrix. Under reducing conditions in SDS-gel electrophoresis this component gave two glycoprotein bands with Mr 53 k and 56 k. The indirect immunofluorescence staining with a monospecific antiserum directed against the component showed its abundant presence in Morris hepatoma 7777 as well as in the less malignant Morris hepatoma 9121 in form of extracellular network structures. The antigen also densely filled some cumuli of cells. In contrast the liver tissue showed only very weak staining of the extracellular areas. The overall distribution of the component could be correlated with the distribution of several hydrolases in the tumor matrix, notably β-d-glucuronidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00492416
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  • 10
    Electronic Resource
    Electronic Resource
    Fucosyltransferase III and sialyl-Lex expression correlate in cultured colon carcinoma cells but not in colon carcinoma tissue (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 727-733 
    Details
    ISSN: 1573-4986
    Keywords: colon carcinoma associated mucins ; sialyl-Lex ; fucosyltransferases ; AM-3
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The potential contribution of fucosyltransferases to the overexpression of sialyl-Lex antigen was investigated in the colon carcinoma cell line HT-29 and in human colon carcinoma tissue. In HT-29 cells as well as in normal or malignant colonic tissues Fuc-TIII, Fuc-TIV, Fuc-TVI but not Fuc-TV nor Fuc-TVII were detectable after RT-PCR. Sodium butyrate treatment of HT-29 cells increased (to about 200%) and DMSO treatment decreased (to about 20%) the expression of sialyl-Lex. This modulation of sialyl-Lex was concomitant with the analogous increase/decrease of mRNA of Fuc-TIII but not Fuc-TIV. Fuc-TVI was not detectable by Northern blotting in HT-29 cells. In six human colon carcinomas which exhibited strong overexpression of sialyl-Lex, the expression of Fuc-TIII-mRNA was the same or lower than in the corresponding normal colonic tissue. Thus Fuc-TIII expression may be affecting the expression of the sialyl-Lex moiety in HT-29 cells but not in human colon carcinoma tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00702336
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