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

James J. Caffrey, Kiyoshi Hidaka, Miho Matsuda, Masato Hirata, Stephen B. Shears

Research output: Contribution to journalArticle

26 Citations (Scopus)

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. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)99-104
Number of pages6
JournalFEBS Letters
Volume442
Issue number1
DOIs
Publication statusPublished - Jan 8 1999

Fingerprint

Acid Phosphatase
Histidine
Osteogenesis
Rats
Salvaging
Physiologic Calcification
Inositol
Chondrocytes
Hypertrophy
Bone
Observation
multiple inositol-polyphosphate phosphatase
Apoptosis
Messenger RNA

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

The human and rat forms of multiple inositol polyphosphate phosphatase : Functional homology with a histidine acid phosphatase up-regulated during endochondral ossification. / Caffrey, James J.; Hidaka, Kiyoshi; Matsuda, Miho; Hirata, Masato; Shears, Stephen B.

In: FEBS Letters, Vol. 442, No. 1, 08.01.1999, p. 99-104.

Research output: Contribution to journalArticle

@article{a80f7dcf43d44ff883a739381c2ca1ab,
title = "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. Copyright (C) 1999 Federation of European Biochemical Societies.",
author = "Caffrey, {James J.} and Kiyoshi Hidaka and Miho Matsuda and Masato Hirata and Shears, {Stephen B.}",
year = "1999",
month = "1",
day = "8",
doi = "10.1016/S0014-5793(98)01636-6",
language = "English",
volume = "442",
pages = "99--104",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - The human and rat forms of multiple inositol polyphosphate phosphatase

T2 - Functional homology with a histidine acid phosphatase up-regulated during endochondral ossification

AU - Caffrey, James J.

AU - Hidaka, Kiyoshi

AU - Matsuda, Miho

AU - Hirata, Masato

AU - Shears, Stephen B.

PY - 1999/1/8

Y1 - 1999/1/8

N2 - 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. Copyright (C) 1999 Federation of European Biochemical Societies.

AB - 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. Copyright (C) 1999 Federation of European Biochemical Societies.

UR - http://www.scopus.com/inward/record.url?scp=0032927675&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032927675&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(98)01636-6

DO - 10.1016/S0014-5793(98)01636-6

M3 - Article

C2 - 9923613

AN - SCOPUS:0032927675

VL - 442

SP - 99

EP - 104

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -