Tp. Gschwend et al., NEUROTRYPSIN, A NOVEL MULTIDOMAIN SERINE-PROTEASE EXPRESSED IN THE NERVOUS-SYSTEM, Molecular and cellular neurosciences, 9(3), 1997, pp. 207-219
We have cloned a novel murine cDNA encoding a multidomain serine prote
ase, termed neurotrypsin, which exhibits an unprecedented domain compo
sition. The deduced amino acid sequence defines a mosaic protein of 76
1 amino acids consisting of a kringle domain, followed by three scaven
ger receptor cysteine-rich repeats, and a serine protease domain. Base
d on comparisons of the primary structure, the protease domain belongs
to the subfamily of trypsin-like serine proteases. In situ hybridizat
ion revealed that the expression of neurotrypsin in the adult murine n
ervous system is confined to distinct subsets of neurons. The most pro
minent expression was found in the cerebral cortex, the hippocampus, a
nd the amygdala, i.e., structures engaged in the processing and storag
e of learned behaviors and memories. Together with the recently obtain
ed evidence that extracellular serine proteases play a role in neural
plasticity, this expression pattern suggests that the extracellular pr
oteolytic action of neurotrypsin subserves structural reorganizations
associated with learning and memory operations.