The obtained results indicate that in the first episode of schizophrenia the blood levels of non-specific inflammation markers (WBS, CRP, ESR and Gra from the leukocyte formula) were high in the subpopulation of patients with the tendency towards normalization of inflammation parameters after a 4-week antipsychotic treatment.

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Carcinoembryonic antigen (CEA) and tissue polypeptide antigen (TPA) levels in serum and urine from 25 patients with bladder cancer and 42 patients with cancer of the renal pelvis/ureter have been evaluated as an aid for clinical diagnosis of urothelial cancer. The tumour CEA content varied markedly, from values obtained in normal urothelium up to 822 and 7306 ng/g wet tissue in cancer of the renal pelvis/ureter and bladder cancer, respectively. Serum and urine CEA levels were found not to correlate with the tumour CEA content. Serum CEA levels were found increased over 5 microg/L in up to 16% of bladder cancer patients, but only in 4.8% in renal pelvis/ureter cancer. Urine of cancer patients contained usually normal CEA levels. Increased serum TPA levels were found in 48% and 35.7% of patients with bladder cancer and cancer of renal pelvis/ureter, respectively. Urine TPA levels were significantly increased in both, patients with bladder cancer (p<0.001) and cancer of renal pelvis/ureter (p<0.01). The median values of urine TPA were 59, 1095 and 1325 U/L, in controls, patients with bladder cancer and cancer of renal pelvis/ureter, respectively. However, considering previously described increase of TPA in inflammatory diseases of urinary tract and in renal failure patients, results of urinary TPA obtained in the diagnostic workup of urothelial cancer should be cautiously interpreted. This study shows that serum and urine levels of CEA and TPA have no diagnostic accuracy required for clinical diagnosis of urothelial cancer.

Oncogenic cultured rat C6 astroblastoma cells display strikingly high ecto-5'-adenosine monophosphatase (ecto-5'-AMPase) activity, 4.23 +/- 20 mumol of Pi liberated by intact cells from 3 mM extracellular 5'-AMP (mg of protein-1 h-1, as compared with 0.15 +/- 0.01 for nononcogenic cultured hamster astroblasts. A further rise in C6 cell ecto-5'-AMPase activity occurs with increase in cell density during growth. Less than 2 pg of the lectin, concanavalin A (Con A), bound per cell reversibly inhibits most of the cellular ecto-5'-AMPase activity. Inhibition by Con A binding is independent of cellular temperature. Con A binding suppresses phosphohydrolase activity of a pK=7.4 functional group on the cell surface. A direct proportionality is observed between quantity of Con A bound to the cell surface and simultaneous relative decreases both in Michaelis constant and maximum velocity of ecto-5'-AMPase in the intact cell. The findings suggest that a major consequence of the specific high affinity binding of Con A to the C6 cell surface is the inactivation of the enzyme--substrate complex of ecto-5'-AMPase.

Because epidermal growth factor (EGF) is likely to be released in the glomeruli during glomerular injury and mesangial cells possess specific receptors for EGF, we thought it to be of interest to examine whether this growth factor could influence the expression of ectoenzymes in cultured human mesangial cells. EGF stimulated 5′–nucleotidase and aminopeptidase N activities in intact human mesangial cells in a time– (24–72 h) and dose–dependent (0.1–50 ng·ml^–1) manner. Maximum stimulation represented 2.7– and 2–fold basal activities for 5′–nucleotidase and aminopeptidase N, respectively. EGF did not influence cyclic AMP production, and its effect on 5′–nucleotidase was additive to that of forskolin or 8–bromo–cAMP. In contrast, genistein (10 mg·ml^–1), an inhibitor of tyrosine kinase, prevented EGF–dependent stimulation of aminopeptidase N and 5′–nucleotidase, suggesting that protein phosphorylation was involved in the signaling mechanism. EGF stimulated specifically the latter two enzymes since it had no effect on other ectoenzymes including alkaline phosphodiesterase I and Mg²⁺–ATPase activities. These results demonstrate that EGF, via the control of 5′–nucleotidase and aminopeptidase N, which are implied in adenosine formation and peptide processing, respectively, could play a role in human cultured mesangial cell contractility and proliferation.