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Aspects of the Animal Collagenases

  • Chapter
Biochemistry of Collagen

Abstract

Information accumulated over the past 13 years since the first animal collagenase was detected (Gross and Lapiere, 1962; Lapiere and Gross, 1963) indicates that collagenolysis in biological systems is accomplished by a series of enzymes one of which, operating at physiologic pH and temperature in the extracellular spaces, produces the first and critical cleavage in the helical body of the molecule within the fibril (Gross and Nagai, 1965; Kang et al., 1966; Sakai and Gross, 1967). This step is followed by one or more enzyme activities which reduce the polypeptide fragments to smaller peptides and amino acids. We know considerably more about the enzyme responsible for the initial attack than we do about subsequent dismantling of the fragments. How much of this latter series of events takes place within the cell has yet to be determined. The possibility of a preliminary cleavage of peptide bonds within the terminal nonhelical regions of the molecule resulting in loss of intermolecular cross-linking in insoluble fibrils is a real one, but such an enzyme activity at neutral pH has not yet been unequivocally detected.

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Authors and Affiliations

  1. The Developmental Biology Laboratory, Department of Medicine, Massachusetts General Hospital and the Harvard Medical School, Boston, Massachusetts, 02114, USA

    Jerome Gross

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  1. Jerome Gross
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  1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India

    G. N. Ramachandran

  2. The Ben May Laboratory for Cancer Research, University of Chicago, Chicago, Illinois, USA

    A. H. Reddi

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Gross, J. (1976). Aspects of the Animal Collagenases. In: Ramachandran, G.N., Reddi, A.H. (eds) Biochemistry of Collagen. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-4602-0_6

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  • DOI: https://doi.org/10.1007/978-1-4757-4602-0_6

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