Proteins of the apical and basal plasma membranes of the human placental syncytiotrophoblast: immunochemical and electrophoretic studies.

Abstract

Proteins of the basal and microvillous plasma membranes of the human placental syncytiotrophoblast were compared to elucidate the basis for structural and functional differences in the two membranes. Among the proteins common to both membranes were actin, alkaline phosphatase, albumin, transferrin, immunoglobulin G, proteins of Mr 35,000, 55,000 and 180,000, and five immunochemically detected proteins. Each membrane also contained unique proteins. Major microvillous cytoskeleton proteins of Mr 68,000 80,000 and 105,000 (alpha-actinin) were lacking or absent from basal membrane cytoskeletons which instead contained unique proteins of Mr 14,000, 16,000, 220,000 and 240,000. In addition, immunochemical analyses revealed four glycoprotein antigens unique to microvillous membrane and five unique to basal membrane. Fibronectin was also found to be exclusive to basal membrane. The difference in membrane-associated cytoskeletal proteins correlated with the different organization of actin microfilaments at the two membranes. The protein antigens unique to each of the two membranes provided further evidence for the polarization of membrane proteins and functions in the syncytium.