scholarly journals Characterization of human foetal intestinal alkaline phosphatase. Comparison with the isoenzymes from the adult intestine and human tumour cell lines

1983 ◽  
Vol 211 (3) ◽  
pp. 553-558 ◽  
Author(s):  
C M Behrens ◽  
C A Enns ◽  
H H Sussman
Keyword(s):  
Alkaline Phosphatase ◽  
Cell Line ◽  
Tumour Cell ◽  
Tumour Cell Line ◽  
Subunit Structure ◽  
Human Tumour ◽  
Intestinal Alkaline Phosphatase ◽  
Alkaline Phosphatases ◽  
Inhibition Studies

The molecular structure of human foetal intestinal alkaline phosphatase was defined by high-resolution two-dimensional polyacrylamide-gel electrophoresis and amino acid inhibition studies. Comparison was made with the adult form of intestinal alkaline phosphatase, as well as with alkaline phosphatases isolated from cultured foetal amnion cells (FL) and a human tumour cell line (KB). Two non-identical subunits were isolated from the foetal intestinal isoenzyme, one having same molecular weight and isoelectric point as placental alkaline phosphatase, and the other corresponding to a glycosylated subunit of the adult intestinal enzyme. The FL-cell and KB-cell alkaline phosphatases were also found to contain two subunits similar to those of the foetal intestinal isoenzyme. Characterization of neuraminidase digests of the non-placental subunit showed it to be indistinguishable from the subunits of the adult intestinal isoenzyme. This implies that no new phosphatase structural gene is involved in the transition from the expression of foetal to adult intestinal alkaline phosphatase, but that the molecular changes involve suppression of the placental subunit and loss of neuraminic acid from the non-placental subunit. Enzyme-inhibition studies demonstrated an intermediate response to the inhibitors tested for the foetal intestinal, FL-cell and KB-cell isoenzymes when compared with the placental, adult intestinal and liver forms. This result is consistent with the mixed-subunit structure observed for the former set of isoenzymes. In summary, this study has defined the molecular subunit structure of the foetal intestinal form of alkaline phosphatase and has demonstrated its expression in a human tumour cell line.

scholarly journals Purification and characterization of a cytosolic transglutaminase from a cultured human tumour-cell line

1989 ◽  
Vol 264 (3) ◽  
pp. 679-685 ◽  
Author(s):  
C Y Dadabay ◽  
L J Pike
Keyword(s):  
Cell Line ◽  
Tumour Cell ◽  
Polyclonal Antibodies ◽  
Tissue Transglutaminase ◽  
Tumour Cell Line ◽  
Human Tumour ◽  
A431 Cells ◽  
Human Tumour Cell Line ◽  
Apparent Homogeneity ◽  
Wide Range

Transglutaminases are a family of Ca2(+)-dependent enzymes that catalyse the formation of isopeptide bonds between the side chains of glutamine and lysine residues. The enzymes have been hypothesized to be involved in a wide range of cellular processes, including growth and differentiation and stabilization of the cytoskeleton. The human epidermal carcinoma-cell line, A431 cells, have relatively high amounts of a cytosolic transglutaminase activity that varies upon treatment of the cells with epidermal growth factor. We demonstrate here that this cytosolic activity has the biochemical and immunological properties of a tissue transglutaminase. We also report the purification of this enzyme to apparent homogeneity by a protocol which involves a novel affinity-elution step. Polyclonal antibodies to the transglutaminase were raised and used to identify the enzyme by Western blotting. The availability of purified transglutaminase and antitransglutaminase antibodies will permit further study of the role of this enzyme in the growth of this hormone-responsive human tumour-cell line.

Establishment and Characterization of a Novel Primitive Yolk Sac Tumour Cell Line, TC587

2020 ◽  
Vol 40 (2) ◽  
pp. 759-766 ◽  
Author(s):  
TAKESHI IWASAKI ◽  
KENICHI KOHASHI ◽  
MASASUKE OHNO ◽  
TOMOAKI TAGUCHI ◽  
YOSHINAO ODA
Keyword(s):  
Cell Line ◽  
Tumour Cell ◽  
Yolk Sac ◽  
Tumour Cell Line ◽  
Yolk Sac Tumour

Hypersensitivity of a Human Tumour Cell Line to Very Low Radiation Doses

1993 ◽  
Vol 63 (5) ◽  
pp. 639-650 ◽  
Author(s):  
P. Lambin ◽  
B. Marples ◽  
B. Fertil ◽  
E.P. Malaise ◽  
M.C. Joiner
Keyword(s):  
Cell Line ◽  
Tumour Cell ◽  
Tumour Cell Line ◽  
Radiation Doses ◽  
Human Tumour ◽  
Human Tumour Cell Line ◽  
Low Radiation Doses

Immortalization and characterization of a new canine mammary tumour cell line FR37-CMT

2016 ◽  
Vol 15 (3) ◽  
pp. 952-967 ◽  
Author(s):  
L. R. Raposo ◽  
C. Roma-Rodrigues ◽  
P. Faísca ◽  
M. Alves ◽  
J. Henriques ◽  
...  
Keyword(s):  
Cell Line ◽  
Tumour Cell ◽  
Mammary Tumour ◽  
Tumour Cell Line ◽  
Canine Mammary Tumour

Cytotoxicity and activation of CB1954 in a human tumour cell line

1991 ◽  
Vol 41 (9) ◽  
pp. 1293-1298 ◽  
Author(s):  
Andrew Suntes ◽  
John Baer ◽  
Kenneth D. Bagshawe
Keyword(s):  
Cell Line ◽  
Tumour Cell ◽  
Tumour Cell Line ◽  
Human Tumour ◽  
Human Tumour Cell Line

Cytotoxic Cholestane and Pregnane Glycosides from Tribulus macropterus

2007 ◽  
Vol 62 (5-6) ◽  
pp. 319-325 ◽  
Author(s):  
El-Sayed S. Abdel-Hameed ◽  
Hanan A. El-Nahas ◽  
Eman A. El-Wakil
Keyword(s):  
Cytotoxic Activity ◽  
Cell Line ◽  
Tumour Cell ◽  
Methanol Extract ◽  
Methanolic Extract ◽  
Chemical Data ◽  
Tumour Cell Line ◽  
Human Tumour ◽  
Human Tumour Cell Line ◽  
Chromatographic Techniques

The methanol extract of the whole parts of Tribulus macropterus Boiss. (family Zygophyllaceae) showed cytotoxic activity against a human tumour cell line (hepatocyte generation 2, HepG2) (IC50 = 2.9 μg/ml). The n-butanolic fraction obtained from successive fractionation of the methanolic extract exhibited activity against HepG2 (IC50 = 2.6 μg/ml). Therefore, this fraction was subjected to separation using different chromatographic techniques. Five compounds, 1-5, were isolated and identified as: (22S,25S)-16β,22,26-trihydroxy-cholest-4- en-3-one-16-O-β-D-glucopyranosyl-(1→3)-β-D-xylopyranoside (1), (22S,25S)-16β,22,26-trihydroxy- cholest-4-en-3-one-16-O-β-D-glucopyranosyl-(1→3)-β-d-glucopyranoside (2), sucrose (3), d-pinitol (4) and 3β-hydroxy-5α-pregn-16(17)en-20-one-3-O-β-D-xylopyranosyl-(1→2)- [β-d-xylopyranosyl-(1→3)]-β-D-glucopyranosyl-(1→4)-[α-L-rhamnopyranosyl-(1→2)]-β-D-galactopyranoside (5) on the basis of spectroscopic and chemical data. The three steroidal compounds 1, 2 and 5 were also tested against the same cell line HepG2 and their IC50 values were 2.4, 2.2 and 1.1 μg/ml, respectively.

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