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The human and rat forms of multiple inositol polyphosphate phosphatase: functional homology with a histidine acid phosphatase up‐regulated during endochondral ossification
Author(s) -
Caffrey James J.,
Hidaka Kiyoshi,
Matsuda Miho,
Hirata Masato,
Shears Stephen B.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01636-6
Subject(s) - biochemistry , acid phosphatase , phosphatase , histidine , inositol , biology , endochondral ossification , chemistry , microbiology and biotechnology , amino acid , enzyme , receptor , anatomy , cartilage
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.