What question did this study set out to answer?

To compare the proteoglycanolytic potency of human leukocyte elastase and human cathepsin G using in vitro cartilage substrates and an in vivo joint model.

January 1, 1993Connective Tissue Research

Comparison of the Proteoglycanolytic Activities of Human Leukocyte Elastase and Human Cathepsin G in Vitro and in Vivo

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Authors

JMJoseph McDonnellCentraal Bureau voor de Statistiek JLJulie M. LobnerMerck & Co., Inc., Rahway, NJ, USA (United States)WKWilson B. KnightSouthern Research Institute

Discussion

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Implication

Comparative experimental study demonstrates superior proteoglycan degradation by human cathepsin G over leukocyte elastase in rabbits, suggesting a major role in rheumatoid arthritis.

Key Points

To compare the proteoglycanolytic potency of human leukocyte elastase and human cathepsin G using in vitro cartilage substrates and an in vivo joint model.
Measured in vitro proteoglycanase activity by assessing the ability of purified enzymes to inhibit bovine nasal septum aggrecan from aggregating with hyaluronan.
Tested in vivo activity by injecting purified human leukocyte elastase and cathepsin G intra-articularly into rabbit stifle joints and quantifying released proteoglycan in synovial fluid.
Assayed comparative proteolytic rates against elastin and [3H]-transferrin substrates.
Human cathepsin G was at least tenfold more potent on a molar basis than human leukocyte elastase as a proteoglycanase in vitro.
Human cathepsin G was twofold more potent than human leukocyte elastase at releasing proteoglycans into rabbit stifle joint synovial fluid in vivo.
Human leukocyte elastase degraded elastin approximately 22-fold faster than cathepsin G, while displaying slightly faster hydrolysis of [3H]-transferrin.

Cite This Study

McDonnell et al. (1993) studied this question.

synapsesocial.com/papers/69f29d891b51e2fbf0187650 https://doi.org/10.3109/03008209309032926

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January 1, 1993Connective Tissue Research

Comparison of the Proteoglycanolytic Activities of Human Leukocyte Elastase and Human Cathepsin G in Vitro and in Vivo

View Full Paper

Ask AI

Bookmark

Authors

JMJoseph McDonnellCentraal Bureau voor de Statistiek JLJulie M. LobnerMerck & Co., Inc., Rahway, NJ, USA (United States)WKWilson B. KnightSouthern Research Institute

Discussion

Member takes

Implication

Comparative experimental study demonstrates superior proteoglycan degradation by human cathepsin G over leukocyte elastase in rabbits, suggesting a major role in rheumatoid arthritis.

Key Points

To compare the proteoglycanolytic potency of human leukocyte elastase and human cathepsin G using in vitro cartilage substrates and an in vivo joint model.
Measured in vitro proteoglycanase activity by assessing the ability of purified enzymes to inhibit bovine nasal septum aggrecan from aggregating with hyaluronan.
Tested in vivo activity by injecting purified human leukocyte elastase and cathepsin G intra-articularly into rabbit stifle joints and quantifying released proteoglycan in synovial fluid.
Assayed comparative proteolytic rates against elastin and [3H]-transferrin substrates.
Human cathepsin G was at least tenfold more potent on a molar basis than human leukocyte elastase as a proteoglycanase in vitro.
Human cathepsin G was twofold more potent than human leukocyte elastase at releasing proteoglycans into rabbit stifle joint synovial fluid in vivo.
Human leukocyte elastase degraded elastin approximately 22-fold faster than cathepsin G, while displaying slightly faster hydrolysis of [3H]-transferrin.

Cite This Study

McDonnell et al. (1993) studied this question.

synapsesocial.com/papers/69f29d891b51e2fbf0187650 https://doi.org/10.3109/03008209309032926

Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

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