The design and application of residualizing labels for studies of protein catabolism

S. R. Thorpe, J. W. Baynes, Zissis Chroneos

Research output: Contribution to journalReview article

57 Citations (Scopus)

Abstract

Residualizing labels (R-labels) are chemical tags for proteins, originally designed for studies of the sites and mechanisms of plasma protein catabolism. The labels consist of oligosaccharides derivatized with radioactive, fluorescent, nuclear magnetic resonance (NMR), or positron emission tomography (PET) active reporter molecules. Because these glycoconjugates generally have molecular masses in excess of 500 daltons and are hydrophilic, they are relatively membrane impermeant. They are also designed to be resistant to lysosomal hydrolases and are therefore retained inside cells with half-lives of 2-5 days after endocytosis and degradation of the carrier protein. The R-labels thus provide a convenient means for following the cumulative uptake and catabolism of proteins by cells in vivo or in vitro. This review summarizes how R-labels have provided insights into the sites and regulation of the turnover of circulating proteins, and pathways for intracellular transport and degradation of endocytosed proteins. The potential use of R-labels for noninvasive studies of the distribution of protein pharmaceuticals in vivo is also discussed.

Original languageEnglish (US)
Pages (from-to)399-405
Number of pages7
JournalFASEB Journal
Volume7
Issue number5
StatePublished - 1993

Fingerprint

protein metabolism
Labels
positron-emission tomography
biopharmaceuticals
glycoconjugates
transport proteins
endocytosis
protein degradation
Endocytosis
hydrolases
oligosaccharides
half life
blood proteins
nuclear magnetic resonance spectroscopy
Proteins
cells
molecular weight
uptake mechanisms
Glycoconjugates
degradation

All Science Journal Classification (ASJC) codes

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

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title = "The design and application of residualizing labels for studies of protein catabolism",
abstract = "Residualizing labels (R-labels) are chemical tags for proteins, originally designed for studies of the sites and mechanisms of plasma protein catabolism. The labels consist of oligosaccharides derivatized with radioactive, fluorescent, nuclear magnetic resonance (NMR), or positron emission tomography (PET) active reporter molecules. Because these glycoconjugates generally have molecular masses in excess of 500 daltons and are hydrophilic, they are relatively membrane impermeant. They are also designed to be resistant to lysosomal hydrolases and are therefore retained inside cells with half-lives of 2-5 days after endocytosis and degradation of the carrier protein. The R-labels thus provide a convenient means for following the cumulative uptake and catabolism of proteins by cells in vivo or in vitro. This review summarizes how R-labels have provided insights into the sites and regulation of the turnover of circulating proteins, and pathways for intracellular transport and degradation of endocytosed proteins. The potential use of R-labels for noninvasive studies of the distribution of protein pharmaceuticals in vivo is also discussed.",
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The design and application of residualizing labels for studies of protein catabolism. / Thorpe, S. R.; Baynes, J. W.; Chroneos, Zissis.

In: FASEB Journal, Vol. 7, No. 5, 1993, p. 399-405.

Research output: Contribution to journalReview article

TY - JOUR

T1 - The design and application of residualizing labels for studies of protein catabolism

AU - Thorpe, S. R.

AU - Baynes, J. W.

AU - Chroneos, Zissis

PY - 1993

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N2 - Residualizing labels (R-labels) are chemical tags for proteins, originally designed for studies of the sites and mechanisms of plasma protein catabolism. The labels consist of oligosaccharides derivatized with radioactive, fluorescent, nuclear magnetic resonance (NMR), or positron emission tomography (PET) active reporter molecules. Because these glycoconjugates generally have molecular masses in excess of 500 daltons and are hydrophilic, they are relatively membrane impermeant. They are also designed to be resistant to lysosomal hydrolases and are therefore retained inside cells with half-lives of 2-5 days after endocytosis and degradation of the carrier protein. The R-labels thus provide a convenient means for following the cumulative uptake and catabolism of proteins by cells in vivo or in vitro. This review summarizes how R-labels have provided insights into the sites and regulation of the turnover of circulating proteins, and pathways for intracellular transport and degradation of endocytosed proteins. The potential use of R-labels for noninvasive studies of the distribution of protein pharmaceuticals in vivo is also discussed.

AB - Residualizing labels (R-labels) are chemical tags for proteins, originally designed for studies of the sites and mechanisms of plasma protein catabolism. The labels consist of oligosaccharides derivatized with radioactive, fluorescent, nuclear magnetic resonance (NMR), or positron emission tomography (PET) active reporter molecules. Because these glycoconjugates generally have molecular masses in excess of 500 daltons and are hydrophilic, they are relatively membrane impermeant. They are also designed to be resistant to lysosomal hydrolases and are therefore retained inside cells with half-lives of 2-5 days after endocytosis and degradation of the carrier protein. The R-labels thus provide a convenient means for following the cumulative uptake and catabolism of proteins by cells in vivo or in vitro. This review summarizes how R-labels have provided insights into the sites and regulation of the turnover of circulating proteins, and pathways for intracellular transport and degradation of endocytosed proteins. The potential use of R-labels for noninvasive studies of the distribution of protein pharmaceuticals in vivo is also discussed.

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