Serum sialyltransferase and fucosyltransferase activities in patients with bronchial carcinoma

Serum sialyltransferases and fucosyltransferases measured by an affinity adsorbent technique were studied in 27 exactly defined patients with malignant pulmonary diseases. Fourteen patients with benign pulmonary diseases and 56 with benign surgical diseases were used as controls. Enzyme activities were expressed as amounts of labeled precursor molecules incorporated into endogenous acceptors in counts per minute (cpm). The mean sialyltransferase activity was 583 cpm in bronchial carcinoma, 485 cpm in benign pulmonary disease and 428 cpm in benign surgical disease. The only statistically significant difference was between bronchial carcinoma and benign surgical disease. The mean fucosyltransferase activity was 813 cpm in bronchial carcinoma, 436 cpm in benign pulmonary disease and 255 cpm in benign surgical disease. All the differences were statistically significant. There were no statistically significant differences between the WHO histologic bronchial carcinoma groups. The correlation between sialyltransferase and fucosyltransferase activity in bronchial carcinoma was statistically significant (r = 0.59). In squamous cell carcinoma (N = 6), it was strongly significant (r = 0.96) and there was a significant correlation also in small cell carcinoma (N = 10; r = 0.79) but not in adenocarcinoma (N = 9; r = 0.30) and benign pulmonary disease (N = 14; r = 0.44). It is suggested that serum sialyltransferases and fucosyl transferases would not be decisive for diagnosis when used alone in bronchial carcinoma, but could be included in a screening test battery.

[1]  G. Ronquist,et al.  Serum glycosyl transferases and carcinoembryonic antigen in patients with colorectal carcinoma in different stages. , 1982, Acta chirurgica Scandinavica.

[2]  W. Dobryszycka,et al.  Clinical usefulness of serum acute-phase reactants in patients with ovarian tumors. , 1981, Neoplasma.

[3]  G. Ronquist,et al.  Serum sialyltransferase activity in benign and malignant diseases. , 1980, Acta chirurgica Scandinavica.

[4]  E. Cervén.  Coupling between non-respiratory energy metabolism and ecto-sialyltransferase activity of intact Ehrlich ascites tumour cell membranes. , 1978, Life sciences.

[5]  W. Reutter,et al.  Decrease of human serum fucosyltransferase as an indicator of successful tumor therapy. , 1978, Science.

[6]  C. Ip,et al.  Alterations in serum glycosyltransferases and 5'-nucleotidase in breast cancer patients. , 1978, Cancer research.

[7]  H. Masuda,et al.  Glycopeptide and glycosaminoglycans in the process of hepatic cancer induced by 3'-methyl-DAB. , 1978, The International journal of biochemistry.

[8]  F. Naghizadeh.  Oxidation of α-hydroxybutyrate by human serum , 1977 .

[9]  M. D. de Broe,et al.  Spontaneous shedding of plasma membrane fragments by human cells in vivo and in vitro. , 1977, Clinica chimica acta; international journal of clinical chemistry.

[10]  T. Powles,et al.  A biochemical approach to the staging of human breast cancer , 1977, Cancer.

[11]  E. Cervén.  Demonstration of sialyl transfer from exogenous CMP-N-acetyl-[14C]neuraminic acid to cell membrane-bound acceptor molecules at the surface of intact Ehrlich ascites tumor cells. , 1977, Biochimica et biophysica acta.

[12]  D. Kessel,et al.  Alterations in plasma sialyltransferase levels in patients with neoplastic disease , 1977, Cancer.

[13]  F. Doljanski,et al.  Cell surface shedding--the phenomenon and its possible significance. , 1976, Journal of theoretical biology.

[14]  C. Porter,et al.  Ultrastructural evidence for ectoglycosyltransferase systems , 1975, Nature.

[15]  C. Lloyd.  SIALIC ACID AND THE SOCIAL BEEIAVIOUR OF CELLS , 1975, Biological reviews of the Cambridge Philosophical Society.

[16]  G. Ronquist,et al.  Demonstration of endogenous sialyltransferase on the surface of ehrlich tumour ascites cells. , 1975, Upsala journal of medical sciences.

[17]  T. Hall,et al.  Enzyme activity in invasive tumors of human breast and colon. , 1974, Proceedings of the National Academy of Sciences of the United States of America.