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

FEBS Lett. 1999 Jan 8;442(1):99-104. doi: 10.1016/s0014-5793(98)01636-6.

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.

Publication types

  • Comparative Study

MeSH terms

  • Acid Phosphatase / chemistry
  • Acid Phosphatase / genetics*
  • Acid Phosphatase / metabolism*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Chickens
  • Chondrocytes / enzymology
  • Cloning, Molecular
  • DNA Primers / genetics
  • Gene Expression Regulation, Developmental
  • Humans
  • In Situ Hybridization
  • Molecular Sequence Data
  • Osteogenesis
  • Phosphoric Monoester Hydrolases / chemistry
  • Phosphoric Monoester Hydrolases / genetics*
  • Phosphoric Monoester Hydrolases / metabolism*
  • Proteins / chemistry
  • Proteins / genetics
  • Proteins / metabolism
  • Rats
  • Sequence Homology, Amino Acid
  • Up-Regulation

Substances

  • DNA Primers
  • HiPER1 protein, Gallus gallus
  • Proteins
  • Acid Phosphatase
  • Phosphoric Monoester Hydrolases
  • multiple inositol-polyphosphate phosphatase

Associated data

  • GENBANK/AF084943
  • GENBANK/AF084944