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Volume 16, Number 21,
Issue of November 1, 1996
pp. 6839-6852
Copyright ©1996 Society for Neuroscience
Characterization of Densin-180, a New Brain-Specific Synaptic
Protein of the O-Sialoglycoprotein Family
Received July 18, 1996; revised Aug. 16, 1996; accepted Aug. 19, 1996.
Michelle L. Apperson,
Il Soo Moon, and
Mary B. Kennedy
Division of Biology, California Institute of Technology, Pasadena,
California 91125
We purified an abundant protein of apparent molecular mass 180 kDa
from the postsynaptic density fraction of rat forebrain and obtained
amino acid sequences of three tryptic peptides generated from the
protein. The sequences were used to design a strategy for cloning the
cDNA encoding the protein by polymerase chain reaction. The open
reading frame of the cDNA encodes a novel protein of predicted
molecular mass 167 kDa. We have named the protein densin-180.
Antibodies raised against the predicted amino and carboxyl sequences of
densin-180 recognize a 180 kDa band on immunoblots that is enriched in
the postsynaptic density fraction. Immunocytochemical localization of
densin-180 in dissociated hippocampal neuronal cultures shows that the
protein is highly concentrated at synapses along dendrites. The message
encoding densin-180 is brain specific and is more abundant in forebrain
than in cerebellum. The sequence of densin-180 contains 17 leucine-rich
repeats, a sialomucin domain, an apparent transmembrane domain, and a
PDZ domain. This arrangement of domains is similar to that of several
adhesion molecules, in particular GPIb , which mediates binding of
platelets to von Willebrand factor. We propose that densin-180
participates in specific adhesion between presynaptic and postsynaptic
membranes at glutamatergic synapses.
Key words:
postsynaptic density;
adhesion molecule;
synapse
development;
synaptic cleft;
microsequencing;
polymerase chain
reaction
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