Phagocytic Release and Activation of Human Leukocyte Procollagenase

Oronsky, Arnold L.; Perper, R. J.; Schroder, Henry C.

doi:10.1038/246417a0

Cited by 109 publications

(38 citation statements)

References 17 publications

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“…The role of lysosome granule constituents as mediators of the inflammatory process and cartilage destruction is now well documented (6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)29,30). Polymorphonuclear leukocytes or neutrophils are capable of discharging or secreting their lysosoma1 contents into the extracellular environment during cell contact with either phagocytizable (24,27,3 1,32) or nonphagocytizable (2 1,25,26,28,3 1,33) immune reactants.…”

Section: Discussionmentioning

confidence: 99%

Glucocorticosteroid inhibition of nonphagocytic discharge of lysosomal enzymes from human neutrophils

Ignarro

1977

Arthritis & Rheumatism

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Glucocorticosteroids and mineralocorticosteroids were tested for their capacity to inhibit the nonphagocytic discharge of two lysosomal enzymes-a cartilage matrixdegrading neutral protease and ,8-glucuronidase-from highly purified human neutrophils. Lysosomal enzyme discharge from neutrophils adherent to nonphagocytizable, immobilized, heat-aggregated IgC was inhibited by the four glucocorticosteroids-methylprednisolone sodium succinate, triamcinolone acetonide hemisuccinate, paramethasone acetate, and hydrocortisone sodium succinate. These glucocorticoids also inhibited zymosan-induced release of @-glucuronidase from neutrophils that had been pretreated with cytochalasin B in order to completely prevent the onset of phagocytosis. Inhibition by the glucocorticoids of lysosomal enzyme discharge provoked by a soluble divalent cation ionophore was also observed. Neither desoxycorticosterone acetate nor aldosterone hemisuccinate, two mineralocorticosteroids, inhibited lyso-

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Section: Discussionmentioning

confidence: 99%

Glucocorticosteroid inhibition of nonphagocytic discharge of lysosomal enzymes from human neutrophils

Ignarro

1977

Arthritis & Rheumatism

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“…Cleavage of interstitial collagens (types I-III) occurs by a distinct metalloprotease, collagenase [1][2][3]. This enzyme is produced by several cell types including macrophages [4] and fibroblasts [5] and cleaves triple helical collagen such that fragments of one and three quarter length of the entire molecule are released [6]. Since collagenase represents the key enzyme in the degradation of connective tissue, its activity is tightly controlled.…”

Section: Introductionmentioning

confidence: 99%

Collagenase gene expression in fibroblasts is regulated by a three‐dimensional contact with collagen

Mauch¹,

Adelmann-Grill

Hatamochi³

et al. 1989

FEBS Letters

111

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Collagenase activity in fibroblasts is regulated by cytokines and the interaction with the extracellular matrix. In this study we demonstrate that fibroblasts cultured within a three-dimensional collagen gel show a strong induction of collagenase gene expression. In addition to increased de novo synthesis most of the secreted enzyme was found to be activated leading to a high collagenolytic activity and complete degradation of collagen matrices after removal of fetal calf serum. Collagen I gene expression was found to be reduced under these conditions. These data suggest a specific modulation of cellular metabolism in response to contact with a three-dimensional collagenous matrix resulting in the divergent regulation of collagen and collagenase.

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“…In most cases it has been possible to activate these collagenases with trypsin (Vaes, 1972; Vol. 161 Hook et al, 1973;Oronsky et al, 1973;BirkedalHansen et al, 1975a;Bauer et al, 1975). Activating enzymes have also been detected in rheumatoid synovial fluid (Kruze & Wojtecka, 1972;Oronsky et al, 1973;Wize et al, 1975), dental plaque (Robertson et al, 1974) and mast cells (Birkedal-Hansen et al, 1975b).…”

mentioning

confidence: 99%

“…161 Hook et al, 1973;Oronsky et al, 1973;BirkedalHansen et al, 1975a;Bauer et al, 1975). Activating enzymes have also been detected in rheumatoid synovial fluid (Kruze & Wojtecka, 1972;Oronsky et al, 1973;Wize et al, 1975), dental plaque (Robertson et al, 1974) and mast cells (Birkedal-Hansen et al, 1975b). Although it is difficult to determine whether activation of collagenase in these cases is due to the destruction or competitive binding of an endogenous collagenase inhibitor or to the cleavage of a zymogen form to yield active enzyme, the latter interpretation is favoured by most authors.…”

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confidence: 99%

A latent form of collagenase in the involuting rat uterus and its activation by a serine proteinase

Woessner¹

1977

Biochemical Journal

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1. The involuting rat uterus displays an extremely rapid breakdown of collagen. Collagenase activity can be assayed directly in the insoluble 6000g pellet of uterine homogenates. At 1 day post partum, about 85% of this collagenase activity is in a latent form. 2. This latent form can be activated by trypsin or by a serine proteinase present in the uterine pellets. 3. The activating enzyme of the tissue is inhibited by a wide spectrum of trypsin inhibitors, including Trasylol, soya-bean and lima-bean trypsin inhibitors, snail inhibitor and di-isopropyl phosphoro-fluoridate. Partial inhibition is produced by benzamidine, phenylmethanesulphonyl fluoride, epsilon-aminohexanoate, leupeptin, antipain and alpha1-antitrypsin. Ovomucoid, 7-amino-1-chloro-3-tosylamido-1-heptan-2-one and 1-chloro-4-phenyl-3-(N-benzyloxy-carbonyl)amino-L-butan-2-one are not inhibitory. 4. Extraction of uterine pellets with 0.1 M-CaCl2 at 60 degrees C releases both latent and active collagenase. Exclusion chromatography on Sephadex G-100 gives an apparent molecular weight of approx. 77000 for the latent form and 66000 for the active form. The latent form is suggested to be a zymogen of collagenase.

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Phagocytic Release and Activation of Human Leukocyte Procollagenase

Cited by 109 publications

References 17 publications

Glucocorticosteroid inhibition of nonphagocytic discharge of lysosomal enzymes from human neutrophils

Glucocorticosteroid inhibition of nonphagocytic discharge of lysosomal enzymes from human neutrophils

Collagenase gene expression in fibroblasts is regulated by a three‐dimensional contact with collagen

A latent form of collagenase in the involuting rat uterus and its activation by a serine proteinase

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