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alkaline phosphatase/syöpä
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 1970 tuloksia
Anti-tumor effects of antibody-alkaline phosphatase conjugates in combination with etoposide phosphate.
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Two anti-tumor monoclonal antibodies, L6 (anticarcinoma) and 1F5 (anti-B lymphoma), were covalently linked to alkaline phosphatase (AP), forming conjugates that could bind to the surface of antigen-positive tumor cells. The conjugates were capable of converting a relatively noncytotoxic prodrug,
Radionuclide imaging of epithelial ovarian tumours with 123I-labelled monoclonal antibody (H317) specific for placental-type alkaline phosphatase.
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A murine monoclonal antibody, H317, specific for placental-type alkaline phosphatase was labelled with 123I and assessed as an imaging agent using a gamma camera computer system in 18 patients suspected of possible recurrent or metastatic ovarian cancer 1-4 years after removal of the primary tumour.
Differential effects of sodium butyrate and dimethylsulfoxide on gamma-glutamyl transpeptidase and alkaline phosphatase activities in MCF-7 breast cancer cells.
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Sodium butyrate and dimethylsulfoxide (DMSO), two known chemical inducers of cell differentiation, were examined on MCF-7 breast cancer cells. Both agents reduce the proliferative capacity of MCF-7 cells, as reflected by inhibition of colony formation in semisolid agar. Sodium butyrate is shown to
Differential patterns of expression of glycosylphosphatidylinositol-anchored carcinoembryonic antigen and alkaline phosphatase in various cancer cell lines.
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The expression of glycosylphosphatidylinositol (GPI-anchored) carcinoembryonic antigen (CEA) and alkaline phosphatase (ALP) on the cell surface of various cancer cell lines and a lung diploid cell line (WI38) was investigated, with exposure of the cell lines to a cell differentiation agent (sodium
[Modulation of alkaline phosphatase by butyrate and prednisolone in uterine cervical cancer cell line (SKG-III)].
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The production of late placental alkaline phosphatase (ALP) isoenzyme and the co-presence of a small amount of tissue-unspecific ALP isoenzyme was confirmed in the newly established uterine cervical epidermoid cancer cell line SKG-III. Sodium butyrate (3mM), which has been shown to modulate
Effect of hyperosmolality on alkaline phosphatase and stress-response protein 27 of MCF-7 breast cancer cells.
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MCF-7, a continuous cell line derived from a human breast carcinoma, exhibits very low alkaline phosphatase (ALP) activity. The enzyme is heat-stable and is inhibited by L-phenylalanine and L-phenylalanylglycylglycine, but not by L-homoarginine, 1-bromotetramisole, or levamisole. These data indicate
A difference in the regulation of mRNA expression between the phenotypic and the embryonic alkaline phosphatase genes in human cancer cells.
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The steady-state levels of mRNAs encoding alkaline phosphatase isoenzymes were examined in two human breast carcinoma cell lines. MDA-MB-157 cells expressed the phenotypic breast alkaline phosphatase and BT20 cells expressed the nonphenotypic placental alkaline phosphatase isoenzyme, frequently
Tetramisole analogues as inhibitors of alkaline phosphatase, an enzyme involved in the resistance of neoplastic cells to 6-thiopurines.
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A series of tetramisole derivatives was synthesized and tested for inhibitory activity against alkaline phosphatase which was partially purified from a murine ascitic neoplasm resistant to 6-thiopurines (Sarcoma 180/TG). These agents included derivatives substituted with halogens, CH3, or NO2 groups
Construction, characterisation and kinetics of a single chain antibody recognising the tumour associated antigen placental alkaline phosphatase.
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The murine monoclonal antibody H17E2 recognises placental alkaline phosphatase (PLAP), an antigen present in the human term placenta and also expressed by many tumours. The antibody is of value in both immunoscintigraphy and radioimmunotherapy in testicular and ovarian cancer. The small size of
Placental alkaline phosphatase-like isoenzymes produced by human gastric cancer cells.
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The human gastric cancer cell lines, MKN1 and SCH, were biochemically and biologically characterized according to the monophenotypic expression of placental alkaline phosphatase (PLAP)-like enzymes. The MKN1 cell line, derived from adenosquamous carcinoma, showed the same enzyme properties as the
[Alkaline phosphatase isoenzymes and alpha-1-fetoprotein in hepatic neoplasms].
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A study was made of possible relations between the placental alkaline phosphatase-isoenzyme (PAP), alpha 1-fetoprotein and liver neoplasia. Ninety-six with various liver diseases were examined, including 10 with primary and 16 with metastatic carcinoma. It was found that both PAP and AFP may be
Lectin affinity electrophoresis of serum alkaline phosphatase in metastasized breast cancer.
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The use of serum alkaline phosphatase (ALP) isoenzymes as markers of breast cancer metastases and treatment efficacy has received little attention. Twenty-six breast cancer women (56+/-13 years, all post-menopausal) were prospectively evaluated during their first and third course of chemotherapy
Diagnosis of primary liver cancer using lectin affinity chromatography of serum alkaline phosphatase.
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Serum alkaline phosphatase (sALP) can be separated into unbound liver type (L-ALP) and bound bone type (B-ALP) by means of WGA affinity chromatography. The L-ALP from the sera of normal adults and various liver diseases was found to show different chromatographic behaviours on DSA affinity column
Electrophoretic patterns of alkaline phosphatase isoenzymes in human sera with abnormally high activity, and an unusual band observed in sera of patients with pancreatic cancer.
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Alkaline phosphatase isoenzymes in sera were resolved by electrophoresis on cellulose acetate membranes into seven different bands (L1, B, Pl, L2, l1, l2, and Pa, in decreasing order of electrophoretic mobility). The slowest moving band (Pa) was observed in the sera of 16 patients--15 with cancer of
Direct immunoperoxidase staining for Regan isoenzyme of alkaline phosphatase in human tumor tissues.
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Immunoperoxidase staining for Regan isoenzyme of alkaline phosphatase was performed on cryostat sections of five human tumor tisssues. With a direct immunoperoxidase staining for the localization of Regan isoenzyme at the light and electron microscope levels, sections previously fixed with 0.05 M
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