The structure and composition of human placental fibrinoid were studied on cryostat and paraffin sections and by transmission electron microscopy as well as immunohistochemistry using antibodies directed against fibrin, fibronectin isoforms, collagens IV and VI, laminin and tenascin. The findings suggest two structurally and immunohistochemically different subtypes of fibrinoid: fibrin-type fibrinoid and matrix-type fibrinoid. Fibrin-type fibrinoid was characterized by immunoreactivity for fibrin and cellular fibronectin, including the ED-A sequence. Immunostaining for all other extracellular matrix molecules was negative. Ultrastructurally, this fibrinoid subtype consisted of a meshwork of fibers with 20-nm cross striation typical of fibrin. Fibrin-type fibrinoid never contained extravillous trophoblast cells. It is therefore primarily a blood clot product derived from maternal and fetal blood. In contrast, matrix-type fibrinoid showed virtually no evidence of fibrin; it was immunopositive for extracellular matrix molecules such as the fibronectins, particularly oncofetal fibronectin (containing the ED-B sequence), collagen IV, laminin and tenascin. Oncofetal fibronectin, which was neither expressed in fibrin-type fibrinoid nor in the villous stromal core, seemed to be a specific marker for matrix-type fibrinoid. Single or clustered nonproliferative extravillous trophoblast cells were embedded within the matrix molecules. It is very likely that these cells secrete the matrix in a nonpolarized fashion. Fibrin-type fibrinoid would appear to be involved in shaping the intervillous space and in replacing damaged syncytiotrophoblast acting as a transport and immune barrier. Matrix-type fibrinoid, as a secretory product of the extravillous trophoblast, should be discussed in context with the invasive properties of this cell population.