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

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.

• Authors: J J Caffrey, K Hidaka, M Matsuda, M Hirata, S B Shears
• Journal: FEBS letters (FEBS Lett) Vol. 442 Issue 1 Pg. 99-104 (Jan 08 1999) ISSN: 0014-5793 [Print] England
• PMID: 9923613 (Publication Type: Comparative Study, Journal Article)

Chemical References

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

Topics

• Acid Phosphatase (chemistry, genetics, 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, genetics, metabolism)
• Proteins (chemistry, genetics, metabolism)
• Rats
• Sequence Homology, Amino Acid
• Up-Regulation