Journal of Neuroscience, Vol 2, 722-734, Copyright © 1982 by Society for Neuroscience
Isolation, morphology, and protein and glycoprotein composition of synaptic junctional fractions from the brain of lower vertebrates: antigen PSD-95 as a junctional marker
M Nieto-Sampedro, CM Bussineau and CW Cotman
Synaptic junction (SJ) fractions were isolated from the brains of the gray
shark, bonito, common frog, several reptiles, and common chicken and
compared to those prepared from mammalian brain. All SJ preparations, as
judged by electron microscopic analysis, were at least 85% pure, consisting
primarily of postsynaptic densities (PSDs) with or without an overlying
plasma membrane and, to a lesser extent, of complete synaptic junctions.
Complete junctions were less abundant in preparations from lower
vertebrates. The electrophoretic pattern of SJs from different vertebrate
species showed considerable conservation of the major protein bands. The
most abundant were fibrous proteins, especially tubulins, actin, and the
PSD-specific polypeptide with a molecular weight of 52,000 (PSD-52).
Glycoproteins capable of binding concanavalin A were present in SJs from
all vertebrates; their apparent molecular weight and relative abundance
were characteristic of each animal order examined, showing more
similarities in species more closely related phylogenetically. Finally, a
protein (antigen PSD-95) previously shown to be located specifically in the
postsynaptic densities of the mammalian brain was present in all species.
The binding of antibody specific to this protein decreased with descending
phylogenetic order from mammals to shark. Nonetheless, PSD-95 was present
in all vertebrate species and appeared to be a general specific marker for
PSDs.