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

FEBS Letters

Hidaka, Kiyoshi¹  Shears, Stephen B.²  Matsuda, Miho¹  Caffrey, James J.²  Hirata, Masato¹ 

[1] Department of Biochemistry, Kyushu University, Faculty of Dentistry, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812, Japan;Inositide Signaling Group, National Institute of Environmental Health Sciences, NIH, P.O. Box 12233, Research Triangle Park, NC 27709, USA

关键词: Chondrocyte;    Inositol phosphate;    Bone;    Apoptosis;    Multiple inositol polyphosphate phosphatase;    ER;    endoplasmic reticulum;    HiPER1;    histidine phosphatase of the endoplasmic reticulum-1;    MIPP;    multiple inositol polyphosphate phosphatase;    MLP;    MIPP-like protein;    NTS;    non-translated sequence;   

DOI  :  10.1016/S0014-5793(98)01636-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown