Malignant and normally developing trophoblastic cells of human placenta display different characteristics defined by histochemical and biochemical mapping of endogenous lectins.
Trophoblastic cells with their strictly controlled propensity for invasive growth hereby bear limited resemblance to malignant cells. Therefore, detailed description of molecular characteristics of this cell type in comparison to histologically related tumor cells may aid in defining physiologically relevant differences. In view of the potential importance of selective protein-carbohydrate interactions in recognitive processes, labelled neoglycoproteins were employed to evaluate systematically the presence and distribution of sugar receptors in tumor cells of chorionepithelioma and in trophoblastic cells of an early stage of gestation. Control reactions in glycohistochemistry, involving prolonged incubation, pH variation and use of nucleotides excluded the possibility that glycosidases or glycosyltransferases govern the sugar-specific binding to the tissue sections. Pronounced differences were detected in the expression of receptors (lectins) for alpha- and beta-glucosides as well as for N-acetylgalactosamine and N-acetylglucosamine. Further differences were revealed by probing both types of tissue with lactosylated, fucosylated, xylosylated and sialylated carrier protein. Upon developmental maturation of the normal cells in placenta the extent of binding of the neoglycoproteins decreased. The glycohistochemical differences between malignant and normally developing trophoblastic cells were found to be reflected in the alteration of expression of certain endogenous lectins, as ascertained by affinity chromatography and gel electrophoretic analysis. Consequently, we assume that the transient presence of certain endogenous lectins during early stages of gestation and their differential expression in relation to tumor cells of chorionepithelioma may be relevant for the special invasive and adhesive behavior of human trophoblastic cells.
Gabius
H J
HJ
Max-Planck-Institut für experimentelle Medizin, Abteilung Chemie, Göttingen, Federal Republic of Germany.
Debbage
P L
PL
Lang
N
N
Lange
W
W
D002822:Choriocarcinoma / Q000032:analysis / Q000473:pathology* / Q000503:physiopathology; D005260:Female; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D010920:Placenta / Q000166:cytology*; D019038:Platelet Glycoprotein GPIb-IX Complex; D010980:Platelet Membrane Glycoproteins; D011247:Pregnancy; D011261:Pregnancy Trimester, First / Q000378:metabolism; D011263:Pregnancy Trimester, Third / Q000378:metabolism; D011971:Receptors, Immunologic / Q000032:analysis* / Q000378:metabolism; D014327:Trophoblasts / Q000166:cytology* / Q000378:metabolism / Q000502:physiology; D014594:Uterine Neoplasms / Q000032:analysis / Q000473:pathology* / Q000503:physiopathology
D006023:Glycoproteins; D019038:Platelet Glycoprotein GPIb-IX Complex; D010980:Platelet Membrane Glycoproteins; D011971:Receptors, Immunologic; C032193:glycoprotein receptor GPIb-IX