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Enzymatic properties and localization of motopsin (PRSS12), a protease whose absence causes mental retardation.

Abstract
Motopsin (PRSS12) is a mosaic protease expressed in the central nervous system. Truncation of the human motopsin gene causes nonsyndromic mental retardation. Understanding the enzymatic properties and localization of motopsin protein in the central nervous system will help identify the molecular mechanism by which the loss of motopsin function causes mental retardation. Recombinant motopsin showed amidolytic activity against the synthetic substrate benzyloxycarbonyl-l-phenylalanyl-l-arginine 4-methyl-coumaryl-7-amide. Motopsin activated the single-chain tissue plasminogen activator precursor and exhibited gelatinolytic activity. This enzymatic activity was inhibited by typical serine protease inhibitors such as aprotinin, leupeptin, and (4-amidinophenyl) methanesulfonyl fluoride. Immunocytochemistry using anti-motopsin IgG revealed that both human and mouse motopsin proteins were distributed in discrete puncta along the dendrites and soma as well as axons in cultured hippocampal neurons. In the limbic system, including the cingulate and hippocampal pyramidal neurons and piriform cortex, high level of motopsin protein was expressed at postnatal day 10, but a very low level at 10-week-old mice. Motopsin and tissue plasminogen activator were co-expressed in the cingulate pyramidal neurons at postnatal day 10 and were distributed along dendrites of cultured pyramidal neurons. In cranial nuclei, a moderate level of motopsin protein was detected independently on the developmental stage. Our results suggest that motopsin has multiple functions, such as axon outgrowth, arranging perineuronal environment, and maintaining neuronal plasticity, partly in coordination with other proteases including tissue plasminogen activator.
AuthorsShinichi Mitsui, Nozomi Yamaguchi, Yoji Osako, Kazunari Yuri
JournalBrain research (Brain Res) Vol. 1136 Issue 1 Pg. 1-12 (Mar 09 2007) ISSN: 0006-8993 [Print] Netherlands
PMID17223089 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Recombinant Proteins
  • Serine Endopeptidases
  • neurotrypsin
Topics
  • Animals
  • Animals, Newborn
  • Axons (enzymology)
  • Brain (cytology, enzymology)
  • Cells, Cultured
  • Dendrites (enzymology)
  • Enzyme Activation
  • Gene Expression Regulation, Developmental (physiology)
  • Humans
  • Mice
  • Mice, Inbred C57BL
  • Neurons (cytology, enzymology)
  • Recombinant Proteins (metabolism)
  • Serine Endopeptidases (genetics, metabolism)
  • Transfection (methods)

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