The design and application of residualizing labels for studies of protein catabolism
S. R. Thorpe, J. W. Baynes, Zissis Chroneos
Department of Microbiology and Immunology
Division of Hematology and Oncology
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.
FASEB Journal
https://doi.org/10.1096/fasebj.7.5.8462781
10.1096/fasebj.7.5.8462781
Dive into the research topics of 'The design and application of residualizing labels for studies of protein catabolism'. Together they form a unique fingerprint.
Label Chemical Compounds 100%
Endocytosis Medicine & Life Sciences 57%
Glycoconjugates Medicine & Life Sciences 36%
Application Chemical Compounds 35%
Hydrolases Medicine & Life Sciences 33%
Oligosaccharides Medicine & Life Sciences 31%
Thorpe, S. R., Baynes, J. W., & Chroneos, Z. (1993). The design and application of residualizing labels for studies of protein catabolism. FASEB Journal, 7(5), 399-405. https://doi.org/10.1096/fasebj.7.5.8462781
Thorpe, S. R. ; Baynes, J. W. ; Chroneos, Zissis. / The design and application of residualizing labels for studies of protein catabolism. In: FASEB Journal. 1993 ; Vol. 7, No. 5. pp. 399-405.
@article{a0537167176e450dbc7460afd452b3a8,
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.",
author = "Thorpe, {S. R.} and Baynes, {J. W.} and Zissis Chroneos",
doi = "10.1096/fasebj.7.5.8462781",
journal = "FASEB Journal",
publisher = "FASEB",
Thorpe, SR, Baynes, JW & Chroneos, Z 1993, 'The design and application of residualizing labels for studies of protein catabolism', FASEB Journal, vol. 7, no. 5, pp. 399-405. https://doi.org/10.1096/fasebj.7.5.8462781
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.
T1 - The design and application of residualizing labels for studies of protein catabolism
AU - Thorpe, S. R.
AU - Baynes, J. W.
AU - Chroneos, Zissis
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.
U2 - 10.1096/fasebj.7.5.8462781
DO - 10.1096/fasebj.7.5.8462781
JO - FASEB Journal
JF - FASEB Journal
Thorpe SR, Baynes JW, Chroneos Z. The design and application of residualizing labels for studies of protein catabolism. FASEB Journal. 1993;7(5):399-405. https://doi.org/10.1096/fasebj.7.5.8462781