Degradation of collagen by a human granulocyte collagenolytic system

Gerald S. Lazarus; John R. Daniels; Robert S. Brown; Howard A. Bladen; Harold M. Fullmer

doi:10.1172/JCI105945

^{Laboratory of Histology and Pathology of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Laboratory of Biochemistry of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Medicine Branch of the National Cancer Institute, Bethesda, Maryland 20014}

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^{Laboratory of Histology and Pathology of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Laboratory of Biochemistry of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Medicine Branch of the National Cancer Institute, Bethesda, Maryland 20014}

Find articles by Daniels, J. in: JCI | PubMed | Google Scholar

^{Laboratory of Histology and Pathology of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Laboratory of Biochemistry of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Medicine Branch of the National Cancer Institute, Bethesda, Maryland 20014}

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^{Laboratory of Histology and Pathology of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Laboratory of Biochemistry of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Medicine Branch of the National Cancer Institute, Bethesda, Maryland 20014}

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^{Laboratory of Histology and Pathology of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Laboratory of Biochemistry of the National Institute of Dental Research, Bethesda, Maryland 20014}

^{Medicine Branch of the National Cancer Institute, Bethesda, Maryland 20014}

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Published in Volume 47, Issue 12 on December 1, 1968
J Clin Invest. 1968;47(12):2622–2629. https://doi.org/10.1172/JCI105945.
© 1968 The American Society for Clinical Investigation

Published December 1, 1968 - Version history

This report suggests a mechanism for collagen degradation mediated by human granulocytic leukocytes. A specific collagenase, which is extractable from human granulocytes, has been partially purified by DEAE chromatography. This collagenolytic enzyme is operative at physiological pH and is inhibited by EDTA, cysteine, and reduced glutathione but not by human serum. The enzyme cleaves the collagen molecule into two specific products, without loss of helical conformation. Electron micrographs of segment long spacing aggregates indicate that the cleavage occurs one-quarter of the length from the carboxy terminal end of the molecule. Experiments with crude extracts from granulocytes suggest that the specific products of granulocyte collagenase activity are then degraded by other proteases present in the human granulocyte.

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