α-L-Iduronidase in normal and mucopolysaccharidosis-type-I human skin fibroblasts

J. A. Taylor, G. J. Gibson, D. A. Brooks, J. J. Hopwood

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

α-L-Iduronidase synthesis and maturation were analysed in fibroblasts from normal controls and from α-L-iduronidase-deficient mucopolysaccharidosis-type-I (MPS-I) patients. Fibroblasts were radiolabelled with [3H]leucine and α-L-iduronidase was isolated from cell lysates or culture medium by monoclonal-antibody affinity chromatography. Pulse-chase labelling of normal control fibroblasts showed that α-L-iduronidase was synthesized as an 81 kDa precursor and processed within 24 h via intermediates of 76 kDa and 70 kDa to a 69 kDa species. The incorporation of radiolabel into α-L-iduronidase in fibroblasts from three of four MPS-I patients was at levels that were either very low or undetectable. Fibroblasts from one MPS-I patient, however, exhibited levels of incorporation of radiolabelled amino acid into α-L-iduronidase similar to those shown by normal control fibroblasts, despite having undetectable α-L-iduronidase enzyme activity. The maturation of α-L-iduronidase in fibroblasts from this patient was delayed compared with normal controls and showed accumulation of the 76 kDa intermediate, as well as the major 69 kDa, form of the enzyme.

LanguageEnglish
Pages263-268
Number of pages6
JournalBiochemical Journal
Volume274
Issue number1
DOIs
Publication statusPublished - 1 Jan 1991
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Taylor, J. A., Gibson, G. J., Brooks, D. A., & Hopwood, J. J. (1991). α-L-Iduronidase in normal and mucopolysaccharidosis-type-I human skin fibroblasts. Biochemical Journal, 274(1), 263-268. https://doi.org/10.1042/bj2740263
Taylor, J. A. ; Gibson, G. J. ; Brooks, D. A. ; Hopwood, J. J. / α-L-Iduronidase in normal and mucopolysaccharidosis-type-I human skin fibroblasts. In: Biochemical Journal. 1991 ; Vol. 274, No. 1. pp. 263-268.
@article{c3f1acfe4904489fa793b27470608d5f,
title = "α-L-Iduronidase in normal and mucopolysaccharidosis-type-I human skin fibroblasts",
abstract = "α-L-Iduronidase synthesis and maturation were analysed in fibroblasts from normal controls and from α-L-iduronidase-deficient mucopolysaccharidosis-type-I (MPS-I) patients. Fibroblasts were radiolabelled with [3H]leucine and α-L-iduronidase was isolated from cell lysates or culture medium by monoclonal-antibody affinity chromatography. Pulse-chase labelling of normal control fibroblasts showed that α-L-iduronidase was synthesized as an 81 kDa precursor and processed within 24 h via intermediates of 76 kDa and 70 kDa to a 69 kDa species. The incorporation of radiolabel into α-L-iduronidase in fibroblasts from three of four MPS-I patients was at levels that were either very low or undetectable. Fibroblasts from one MPS-I patient, however, exhibited levels of incorporation of radiolabelled amino acid into α-L-iduronidase similar to those shown by normal control fibroblasts, despite having undetectable α-L-iduronidase enzyme activity. The maturation of α-L-iduronidase in fibroblasts from this patient was delayed compared with normal controls and showed accumulation of the 76 kDa intermediate, as well as the major 69 kDa, form of the enzyme.",
author = "Taylor, {J. A.} and Gibson, {G. J.} and Brooks, {D. A.} and Hopwood, {J. J.}",
year = "1991",
month = "1",
day = "1",
doi = "10.1042/bj2740263",
language = "English",
volume = "274",
pages = "263--268",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

Taylor, JA, Gibson, GJ, Brooks, DA & Hopwood, JJ 1991, 'α-L-Iduronidase in normal and mucopolysaccharidosis-type-I human skin fibroblasts', Biochemical Journal, vol. 274, no. 1, pp. 263-268. https://doi.org/10.1042/bj2740263

α-L-Iduronidase in normal and mucopolysaccharidosis-type-I human skin fibroblasts. / Taylor, J. A.; Gibson, G. J.; Brooks, D. A.; Hopwood, J. J.

In: Biochemical Journal, Vol. 274, No. 1, 01.01.1991, p. 263-268.

Research output: Contribution to journalArticle

TY - JOUR

T1 - α-L-Iduronidase in normal and mucopolysaccharidosis-type-I human skin fibroblasts

AU - Taylor, J. A.

AU - Gibson, G. J.

AU - Brooks, D. A.

AU - Hopwood, J. J.

PY - 1991/1/1

Y1 - 1991/1/1

N2 - α-L-Iduronidase synthesis and maturation were analysed in fibroblasts from normal controls and from α-L-iduronidase-deficient mucopolysaccharidosis-type-I (MPS-I) patients. Fibroblasts were radiolabelled with [3H]leucine and α-L-iduronidase was isolated from cell lysates or culture medium by monoclonal-antibody affinity chromatography. Pulse-chase labelling of normal control fibroblasts showed that α-L-iduronidase was synthesized as an 81 kDa precursor and processed within 24 h via intermediates of 76 kDa and 70 kDa to a 69 kDa species. The incorporation of radiolabel into α-L-iduronidase in fibroblasts from three of four MPS-I patients was at levels that were either very low or undetectable. Fibroblasts from one MPS-I patient, however, exhibited levels of incorporation of radiolabelled amino acid into α-L-iduronidase similar to those shown by normal control fibroblasts, despite having undetectable α-L-iduronidase enzyme activity. The maturation of α-L-iduronidase in fibroblasts from this patient was delayed compared with normal controls and showed accumulation of the 76 kDa intermediate, as well as the major 69 kDa, form of the enzyme.

AB - α-L-Iduronidase synthesis and maturation were analysed in fibroblasts from normal controls and from α-L-iduronidase-deficient mucopolysaccharidosis-type-I (MPS-I) patients. Fibroblasts were radiolabelled with [3H]leucine and α-L-iduronidase was isolated from cell lysates or culture medium by monoclonal-antibody affinity chromatography. Pulse-chase labelling of normal control fibroblasts showed that α-L-iduronidase was synthesized as an 81 kDa precursor and processed within 24 h via intermediates of 76 kDa and 70 kDa to a 69 kDa species. The incorporation of radiolabel into α-L-iduronidase in fibroblasts from three of four MPS-I patients was at levels that were either very low or undetectable. Fibroblasts from one MPS-I patient, however, exhibited levels of incorporation of radiolabelled amino acid into α-L-iduronidase similar to those shown by normal control fibroblasts, despite having undetectable α-L-iduronidase enzyme activity. The maturation of α-L-iduronidase in fibroblasts from this patient was delayed compared with normal controls and showed accumulation of the 76 kDa intermediate, as well as the major 69 kDa, form of the enzyme.

UR - http://www.scopus.com/inward/record.url?scp=0026026198&partnerID=8YFLogxK

U2 - 10.1042/bj2740263

DO - 10.1042/bj2740263

M3 - Article

VL - 274

SP - 263

EP - 268

JO - Biochemical Journal

T2 - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -