Action of collagenase and elastase from human polymorphonuclear leukocytes on human articular cartilage

Baici, Antonio; Salgam, Prathima; Cohen, Gabriel; Fehr, K; Böni, A

doi:10.1007/bf00541264

Cited by 48 publications

(23 citation statements)

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“…Figure 4 shows collagen binding sites and triple helicase mechanisms of MMP types. Elastase and collagenase display about the same collagenolytic potential on human cartilage on a weight basis and the elastase/collagenase system from human polymorphonuclear leukocytes may represent a cooperative proteolytic complex in the destruction of cartilage in rheumatoid arthritis (Baici et al, 1982).…”

Section: Collagenase and Collagenolytic Enzymesmentioning

confidence: 97%

“…In some situations, collagen is considered to be a poor substrate for collagenase, so that the initiation of collagen breakdown is inhibited. However, if the substrate is initially attacked by elastase, proteoglycans are removed from the collagen fibers which make it more susceptible to collagenase attack (Baici et al, 1982;Zeydel et al, 1986).…”

Section: Collagenase and Collagenolytic Enzymesmentioning

confidence: 99%

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Extraction and Purification of Collagenase Enzymes: A Critical Review

Daboor¹,

Budge²,

Ghaly

et al. 2010

American Journal of Biochemistry and Biotechnology

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Problem statement: Enzymes have vital roles in several industrial processes (foods, cosmetics, nutraceuticals and pharmaceuticals) due to their highly selective nature and high activity at very low concentrations. Recent efforts to identify new sources of useful enzymes have been concentrated on the marine environment because of the potential to make use of processing wastes. About 35-50% of the mass of the fish caught is a waste that is disposed off at sea or in landfills. The extraction of enzymes from fish processing waste can reduce environment problems and improve the economics of the fish industry. Collagenases are a group of enzymes that can be extracted from fish waste. Approach: Comprehensive reviews of the literature on the extraction, purification, characterization and use of collagenases was carried out. Results: Collagenases have different molecular weights based on their types and sources. They have the ability to break down the peptide bonds in collagen at physiological pH. They are classified into two types: serine and metallocollagenase. Collagenolytic activities have been shown at a wide range of temperatures (20-40°C) and pH (6-8). Many activators can be used to achive collagenase activity including 4-Aminophenylmercuric Acetate (APMA), trypsin, potassium or sodium thiocyanate, iodoacetamide and potassium iodide. Dithiothreitol (DTT), mercaptoethanol, ethylendiaminetetracetic acid, ophenanthroline and cysteine inactivate the enzyme. Collagenases enzymes can be extracted with a variety of techniques using different buffering systems (tris-HCl, sodium bicarbonate, calcium chloride and cacodylate). All techniques involve the use of ammonium sulphate fractionation and centrifugation to precipitate the enzyme. Collagenases are normally purified using chromatographic techniques such as gel-filtration, ion-exchange and affinity column chromatography. Collagenase can be assayed with a number of methods, including: colorimetric absorbance, viscometry, radioactivity and fluorescence spectroscopy. Collagenases are partly responsible for toughness in red meats and are used as tenderizers in food industry, have application in the fur and hide tanning to ensure uniform dying of leather, used in medicine to treat burns and ulcers, eliminate scar tissues, transplantation of organs. Conclusion: Understanding of the nature of the enzymes and identifying the most suitable resources and the methods for their extraction and purification will have significant impact on the fish processing, food and medical industries.

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Section: Collagenase and Collagenolytic Enzymesmentioning

confidence: 97%

Section: Collagenase and Collagenolytic Enzymesmentioning

confidence: 99%

Extraction and Purification of Collagenase Enzymes: A Critical Review

Daboor¹,

Budge²,

Ghaly

et al. 2010

American Journal of Biochemistry and Biotechnology

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“…MMP-1, MMP-8, MMP-13, and MT1-MMP were chosen based on their ability to cleave types I-III collagen (7,(50)(51)(52)(53)(54). Of the gelatinase family members, MMP-2 is also known to cleave types I and III collagen (55,56), in contrast to MMP-9, which does not process types I-III collagens (57).…”

Section: Cleavage Site Specificity and Selectivitymentioning

confidence: 99%

Differentiation of Secreted and Membrane-Type Matrix Metalloproteinase Activities Based on Substitutions and Interruptions of Triple-Helical Sequences

et al. 2007

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The turnover of collagen triple-helical structure (collagenolysis) is a tightly regulated process in normal physiology, and has been ascribed to small number of proteases. Several members of the matrix metalloproteinase (MMPs) family possess collagenolytic activity, and the mechanisms by which these enzymes process triple-helices are beginning to be unraveled. The present study has utilized 2 triple-helical sequences to compare the cleavage site specificities of 10 MMPs. One substrate featured a continuous Gly-Xxx-Yyy sequence (Pro-Leu-Gly~Met-Arg-Gly) while the other incorporated an interruption in the Gly-Xxx-Yyy repeat (Pro-Val-Asn~Phe-Arg-Gly). Both sequences were selectively cleaved by MMP-13 while in linear form, but neither proved to be selective within a triple-helix. This suggests that the conformational presentation of substrate sequences to an MMP active site is critical for enzyme specificity, in that activities differ when sequences are presented from an unwound triple-helix versus an independent single strand. Differences in specificity between secreted and membranetype (MT) MMPs were also observed for both sequences, where MMP-2 and MT-MMPs showed an ability to hydrolyze a triple-helix at an additional site (Gly-Gln bond). Interruption of the triple-helix had different effects on secreted MMPs and MT-MMPs, as MT-MMPs could not hydrolyze the Asn-Phe bond, but instead cleaved the triplehelix nearer the C-terminus at a Gly-Gln bond. It is possible that MT-MMPs have a requirement for Gly in the P 1 subsite in order to be able to efficiently process a triple-helical molecule. Analysis of individual kinetic parameters and activation energies indicated different substrate preferences within secreted MMPs, as MMP-13 preferred the interrupted sequence while MMP-8 showed little discrimination between non-interrupted and interrupted triple-helices. Based on the present and prior studies, we can assign unique triple-helical peptidase behaviors to the collagenolytic MMPs. Such † This work was supported by the National Institutes of Health (AR 40994 to K.B., CA 98799 and EB 000289 to G.B. The sequence specificities of collagenolytic MMPs have been extensively examined utilizing single-stranded peptides, peptide libraries, and phage display libraries. These include studies of MMP-1, MMP-2, and MMP-8 (10,11), 13), and MT1-MMP (11,14-17). However, there are only a few studies that described the effects of amino acid substitutions within a triple-helical context on MMP activity (5,9,18,19). The influence of triple-helical structure on the interaction between MMP subsites and individual substrate residues has not been explored, but may provide additional information for the mechanism of collagenolysis, the understanding of collagen specificity, and the design of selective inhibitors. NIH Public AccessCollagenolytic activity may also be considered in light of an array of diseases caused by mutations occurring in collagen, such as osteogenesis imperfecta (20) MATERIALS AND METHODSAll standard chemicals were ...

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“…PMN-derived enzymes have been implicated in the degradative process of cartilage (5)(6)(7). The belief that they play a key role is primarily due to the presence of large numbers of PMNs in arthritic synovial fluid and the capacity of PMN-derived proteinases to evoke both acute and chronic forms of arthritis when injected into rabbits (9, coupled with their ability to degrade proteoglycans.…”

Section: Binding Of Chondrocytes Jennifer S Bartholomew and Denis Amentioning

confidence: 99%

Receptor‐mediated binding of leukocyte elastase by chondrocytes

Bartholomew

Lowther

1987

Arthritis & Rheumatism

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Studies on the effect of leukocyte elastase on the metaboliSm of chondrocytes in culture have demonstrated that these cells possess a specific cell surface receptor for leukocyte-derived elastase. Purified elastase from rabbit and human leukocytes is capable of modulating the metabolism of the cell by causing a marked decrease in both proteoglycan and protein biosynthesis. Addition of '251-labeled elastase to chondrocytes maintained in suspension culture has shown that binding occurs, and that it is saturable and is inhibited by the addition of unlabeled enzyme. We ascertained that the active site of the enzyme was necessary for binding to the chondrocyte, since phenylmethylsulfonyl fluoriib inactivated leukocyte elastase failed to bind. Pancreatic elastase had only a slight afiinity for the receptof, whereas trypsin and bovine serum albumin failed to bind to any significant extent. Autoradiographic studies and the use of inhibitors of endocytosis, such as dansyl cadaverine, confirmed that endocytosis of elastase was the secondary event after cell binding.The characteristic features of chronic inflammatory arthritis include the formation of an invasive pannus, the result of synovial cell proliferation cou-

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Action of collagenase and elastase from human polymorphonuclear leukocytes on human articular cartilage

Cited by 48 publications

References 23 publications

Extraction and Purification of Collagenase Enzymes: A Critical Review

Extraction and Purification of Collagenase Enzymes: A Critical Review

Differentiation of Secreted and Membrane-Type Matrix Metalloproteinase Activities Based on Substitutions and Interruptions of Triple-Helical Sequences

Receptor‐mediated binding of leukocyte elastase by chondrocytes

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