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

First Author  Caffrey JJ Year  1999
Journal  FEBS Lett Volume  442
Issue  1 Pages  99-104
PubMed ID  9923613 Mgi Jnum  J:52074
Mgi Id  MGI:1327776 Doi  10.1016/s0014-5793(98)01636-6
Citation  Caffrey JJ, et al. (1999) The human and rat forms of multiple inositol polyphosphate phosphatase: functional homology with a histidine acid phosphatase up-regulated during endochondral ossification. FEBS Lett 442(1):99-104
abstractText  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.
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