concanavalin-a and Neoplasms--Germ-Cell-and-Embryonal

Topics: alpha-Fetoproteins; Chromatography, Agarose; Concanavalin A; Humans; Liver Diseases; Neoplasms, Germ Cell and Embryonal

To establish whether alpha-fetoprotein (AFP) produced in the early post-treatment phase of a patient with a germ cell tumour of the testis or the ovary originates from the tumour or is due to an underlying disturbance in liver function, the binding of AFP to concanavalin A (Con A) was investigated as a discriminative variable. A two-step assay is described that can distinguish the type of AFP produced at levels as low as 10 ng/ml. A Con A-binding ratio of 12-43% was found in the patients with disseminated germ cell tumours and in patients with AFP-positive gastrointestinal carcinomas. AFP from the liver gives ratios below 10%.

Topics: alpha-Fetoproteins; Biomarkers, Tumor; Carcinoma, Hepatocellular; Concanavalin A; Female; Gastrointestinal Neoplasms; Humans; Liver Neoplasms; Male; Methods; Neoplasms, Germ Cell and Embryonal; Ovarian Neoplasms; Protein Binding; Testicular Neoplasms

Using a modified method of Con A, LCH or PHA-E affinity crossed-line immunoelectrophoresis, we studied AFP subfractions in 78 sera including 58 from patients with primary hepatoma, 11 from patients with hepatic metastasis of gastric cancer and 9 from patients with germ cell tumors of the gonads (yolk sac tumor, immature solid teratoma or mature solid teratoma). It was found that AFP in primary hepatoma, metastatic hepatoma or germ cell tumors of the gonads were differently glycosylated, and different patterns of AFP subfractions identified by Con A, LCH or PHA-E affinity crossed-line immunoelectrophoresis facilitated a differential diagnosis of such AFP related malignancies.

Topics: alpha-Fetoproteins; Carcinoma, Hepatocellular; Concanavalin A; Female; Humans; Immunoelectrophoresis; Immunoelectrophoresis, Two-Dimensional; Lectins; Liver Neoplasms; Male; Mesonephroma; Neoplasms, Germ Cell and Embryonal; Ovarian Neoplasms; Teratoma; Testicular Neoplasms

Major molecular species of human alpha-fetoprotein(AFP), which were separated as single components by serial affinity chromatography with concanavalin A(Con-A) and Lens culinaris agglutinin, were further resolved into several bands by affinity electrophoresis with erythroagglutinating phytohemagglutinin of Phaseolus vulgaris lectin(E-PHA). Among the newly separated main molecular species, both Con-A- and E-PHA-reactive AFP(AFP-1X1) was demonstrated, contrary to the known sugar specificity of Con-A and E-PHA, in addition to molecular species of AFP reacting with Con-A but not with E-PHA(AFP-1X0) and of AFP reacting with E-PHA but not with Con-A(AFP-0X1). AFP-0X1 was formed from AFP-0X0, and AFP-1X1 from AFP-1X0 by neuraminidase treatment; thus, AFP-0X1 and AFP-1X1 represent asialylated and AFP-0X0 and AFP-1X0 sialylated molecular species. AFP-1X1' and AFP-0X0' were present as minor components. AFP-0X0' had no affinity for E-PHA, and the affinity increased in the order of AFP's-0X0(or 0X1), -1X1', -1X1 and -0X1. Proportions of those components varied depending on the pathophysiological conditions of AFP production.

Topics: alpha-Fetoproteins; Asialoglycoproteins; Carcinoma, Hepatocellular; Chromatography, Affinity; Concanavalin A; Electrophoresis; Enzyme-Linked Immunosorbent Assay; Fetuins; Humans; Liver Neoplasms; Mesonephroma; Neoplasms; Neoplasms, Germ Cell and Embryonal; Phytohemagglutinins; Stomach Neoplasms; Substrate Specificity