The human and rat forms of multiple inositol polyphosphate phosphatase: Functional homology with a histidine acid phosphatase up-regulated during endochondral ossification

James J. Caffrey, Kiyoshi Hidaka, Miho Matsuda, Masato Hirata, Stephen B. Shears

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

We have derived the full-length sequences of the human and rat forms of the multiple inositol polyphosphate phosphatase (MIPP); their structural and functional comparison with a chick histidine acid phosphatase (HiPER1) has revealed new information: (1) MIPP is approximately 50% identical to HiPER1, but the ER-targeting domains are divergent; (2) MIPP appears to share the catalytic requirement of histidine acid phosphatases, namely, a C-terminal His residue remote from the RHGxRxP catalytic motif; (3) rat MIPP mRNA is up-regulated during chondrocyte hypertrophy. The latter observation provides a context for proposing that MIPP may aid bone mineralization and salvage the inositol moiety prior to apoptosis. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)99-104
Number of pages6
JournalFEBS Letters
Volume442
Issue number1
DOIs
Publication statusPublished - Jan 8 1999

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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