J. J. Reynolds

Publication List Details

Period

1862 - 2008

Number

62

Co-Authors

Prey Selection by Marine-coastal River Otters (Lontra canadensis) in Newfoundland, Canada (2008)

D. Cote, R. S. Gregory, J. Gosse, J. J. Reynolds, G. B. Stenson, ...

Previous studies have suggested that diets of river otters (Lontra canadensis) vary in response to seasonal shifts in prey availability, and that they select slowly moving fish of moderate size. To...

Bacterial antigens induce collagenase and prostaglandin E2 synthesis in human gingival fibroblasts through a primary effect on circulating mononuclear cells.

Heath, J K, Atkinson, S J, Hembry, R M, Reynolds, J J, Meikle, M C

Our previous work suggests that one mechanism through which connective tissue breakdown might occur in periodontal diseases is the production of metalloproteinases, including collagenase, by gingival...

Transforming growth factor beta modulates the expression of collagenase and metalloproteinase inhibitor.

Edwards, D R, Murphy, G, Reynolds, J J, Whitham, S E, Docherty, A J, Angel, P, ...

Exposure of quiescent MRC-5 human fibroblasts to growth factors such as epidermal growth factor, basic fibroblast growth factor or embryonal carcinoma-derived growth factor resulted in the induction...

Cell-mediated degradation of type IV collagen and gelatin films is dependent on the activation of matrix metalloproteinases.

Atkinson, S J, Ward, R V, Reynolds, J J, Murphy, G

The ability of normal rabbit dermal fibroblasts to degrade films of type IV collagen and gelatin when stimulated by phorbol ester was shown to be dependent on the induction, secretion and activation...

Binding of gelatinases A and B to type-I collagen and other matrix components.

Allan, J A, Docherty, A J, Barker, P J, Huskisson, N S, Reynolds, J J, Murphy, G

Matrix sequestration of matrix metalloproteinases may be important for the facilitation of remodelling events and the migration of cells through the extracellular matrix. Using an ELISA technique we...

Inhibition of bone resorption in vitro by selective inhibitors of gelatinase and collagenase.

Hill, P A, Docherty, A J, Bottomley, K M, O'Connell, J P, Morphy, J R, Reynolds, J J, ...

Two low-molecular-mass inhibitors of matrix metalloproteinases (MMPs), CT1166, a concentration-dependent selective inhibitor of gelatinases A and B, and Ro 31-7467, a concentration-dependent...

Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts.

Ward, R V, Atkinson, S J, Reynolds, J J, Murphy, G

We report that the isolated C-terminal domain of progelatinase A is inhibitory to the activation of this proenzyme by primary skin fibroblast plasma membranes but is unable to inhibit...

Characterization of gelatinase from pig polymorphonuclear leucocytes. A metalloproteinase resembling tumour type IV collagenase.

Murphy, G, Ward, R, Hembry, R M, Reynolds, J J, Kühn, K, Tryggvason, K

The metalloproteinase 'gelatinase' stored in the granules of pig polymorphonuclear leucocytes has been purified in the latent form. The enzyme is secreted as an Mr 97,000 proenzyme that can be...

Comparison of human stromelysin and collagenase by cloning and sequence analysis.

Whitham, S E, Murphy, G, Angel, P, Rahmsdorf, H J, Smith, B J, Lyons, A, ...

A comparison of the cDNA-derived amino acid sequences of human stromelysin and collagenase with the N-terminal sequences of purified enzymes reveals that these metalloproteinases are highly conserved...

Purification and characterization of a rabbit bone metalloproteinase that degrades proteoglycan and other connective-tissue components.

Galloway, W A, Murphy, G, Sandy, J D, Gavrilovic, J, Cawston, T E, Reynolds, J J

A metalloproteinase, 'proteoglycanase', that degrades proteoglycan and insoluble type IV collagen as well as casein was purified to homogeneity from rabbit bone culture medium. The major form of this...

The interaction of purified rabbit bone collagenase with purified rabbit bone metalloproteinase inhibitor.

Cawston, T E, Murphy, G, Mercer, E, Galloway, W A, Hazleman, B L, Reynolds, J J

1. Pure rabbit bone metalloproteinase inhibitor (TIMP) bound tightly to pure rabbit bone collagenase with an apparent Kd of 1.4 X 10(-10) M. 2. The molecular weight of the enzyme-inhibitor complex...

Partial purification of collagenase and gelatinase from human polymorphonuclear leucocytes. Analysis of their actions on soluble and insoluble collagens.

Murphy, G, Reynolds, J J, Bretz, U, Baggiolini, M

The separation and further purification of human polymorphonuclear-leucocyte collagenase and gelatinase, using modifications of the method of Cawston & Tyler [(1979) Biochem J. 183, 647-656], are...

The latent collagenase and gelatinase of human polymorphonuclear neutrophil leucocytes.

Murphy, G, Bretz, U, Baggiolini, M, Reynolds, J J

Two metallo-proteinases of human neutrophil leucocytes, collagenase and gelatinase, were studied. Collagenase specifically cleaved native collagen into the TCA and TCB fragments, whereas gelatinase...

Zinc metalloenzyme properties of active and latent collagenase from rabbit bone.

Swann, J C, Reynolds, J J, Galloway, W A

1. Inhibition of collagenase from rabbit bone cultures by the chelating agents 1,10-phenanthroline and EDTA is almost completely reversed by Zn2+; other metal cations are less effective in reversing...

Purification of rabbit bone inhibitor of collagenase.

Cawston, T E, Galloway, W A, Mercer, E, Murphy, G, Reynolds, J J

1. Rabbit bones in tissue culture synthesize an inhibitor of collagenase during the first 4 days of culture. 2. The inhibitor was purified by a combination of gel filtration, concanavalin...

An inhibitor of collagenase from human amniotic fluid. Purification, characterization and action on metalloproteinases.

Murphy, G, Cawston, T E, Reynolds, J J

1. An inhibitor of collagenase of apparent mol.wt. 28000 was isolated from term human amniotic fluid. 2. It is active against mammalian collagenases from a number of species and tissues as well as...

Metalloproteinases from rabbit bone culture medium degrade types IV and V collagens, laminin and fibronectin.

Murphy, G, Cawston, T E, Galloway, W A, Barnes, M J, Bunning, R A, Mercer, E, ...

Gel-filtration chromatography of culture medium from rabbit bone explants separates three latent metalloproteinases with activities against collagen, proteoglycan and gelatin respectively. The...

Collagenase is a component of the specific granules of human neutrophil leucocytes.

Murphy, G, Reynolds, J J, Bretz, U, Baggiolini, M

Azurophil and specific granules were isolated from human polymorphonuclear neutrophil leucocytes. Collagenase was almost exclusively a component of the specific granules. This finding is in contrast...

Evidence that latent collagenases are enzyme-inhibitor complexes.

Sellers, A, Cartwright, E, Murphy, G, Reynolds, J J

Specific collagenase from the culture media of various rabbit tissues and cells exists in active and latent forms. Latent collagenase is most effectively activated with 4-aminophenylmercuric acetate,...

Purification and properties of a specific collagenase from rabbit synovial fibroblasts.

Werb, Z, Reynolds, J J

1. A specific collagenase from the culture medium of rabbit synovial fibroblasts was purified by gel filtration and ion-exchange chromatography. 2. The enzyme was homogenous on polyacrylamide-gel...

Immunochemical studies with a specific antiserum to rabbit fibroblast collagenase.

Werb, Z, Reynolds, J J

1. Antisera were raised against the collagenase from rabbit synovial fibroblasts and characterized by immunoprecipitation and immunoinhibition reactions. 2. Immunoglobulins from the antisera were...

Rabbit collagenase. Immunological identity of the enzymes released from cells and tissues in normal and pathological conditions.

Werb, Z, Reynolds, J J

1. The immunological cross-reactivity between rabbit collagenases from a variety of normal and pathological sources was examined. The specific antibody raised against collagenase secreted from normal...

Neutral metallo-proteinases of rabbit bone. Separation in latent forms of distinct enzymes that when activated degrade collagen, gelatin and proteoglycans.

Sellers, A, Reynolds, J J, Meikle, M C

Rabbit bones in culture produce specific collagenase and neutral metallo-proteinase activity in latent forms that can be activated by either 4-aminophenylmercuric acetate or trypsin. Latent neutral...

Proteoglycan-degrading enzymes of rabbit fibroblasts and granulocytes.

Werb, Z, Dingle, J T, Reynolds, J J, Barrett, A J

A neutral proteinase secreted by rabbit synovial fibroblasts in parallel with specific collagenase was partially purified by ion-exchange chromatography. At pH 7.6 this proteinase degraded...

Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3.

Cowell, S, Knäuper, V, Stewart, M L, D'Ortho, M P, Stanton, H, Hembry, R M, ...

SW1353 chondrosarcoma cells cultured in the presence of interleukin-1, concanavalin A or PMA secreted procollagenase 3 (matrix metalloproteinase-13). The enzyme was detected in the culture medium by...

The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinases-2 and tissue inhibitor of metalloproteinases-1.

Ward, R V, Hembry, R M, Reynolds, J J, Murphy, G

Human gingival fibroblasts in culture were shown to secrete a 72 kDa progelatinase, of which a proportion in the medium was found to be complexed with tissue inhibitor of metalloproteinases-2...

Matrix metalloproteinases in the formation of human synovial joint cavities.

Edwards, J C, Wilkinson, L S, Soothill, P, Hembry, R M, Murphy, G, Reynolds, J J

Matrix metalloproteinases (MMPs) have been implicated in tissue remodelling in growth and development. A histochemical study of human fetal limbs was undertaken to assess the presence, and...

Regional and temporal changes in the synthesis of matrix metalloproteinases and TIMP-1 during development of the rabbit mandibular condyle.

Breckon, J J, Hembry, R M, Reynolds, J J, Meikle, M C

Connective tissues synthesise and secrete a family of matrix metalloproteinases (MMPs; collagenases, gelatinases and stromelysins) capable of degrading all the components of connective tissue...

Bacterial antigens induce collagenase and prostaglandin E2 synthesis in human gingival fibroblasts through a primary effect on circulating mononuclear cells.

Heath, J K, Atkinson, S J, Hembry, R M, Reynolds, J J, Meikle, M C

Our previous work suggests that one mechanism through which connective tissue breakdown might occur in periodontal diseases is the production of metalloproteinases, including collagenase, by gingival...

Transforming growth factor beta modulates the expression of collagenase and metalloproteinase inhibitor.

Edwards, D R, Murphy, G, Reynolds, J J, Whitham, S E, Docherty, A J, Angel, P, ...

Exposure of quiescent MRC-5 human fibroblasts to growth factors such as epidermal growth factor, basic fibroblast growth factor or embryonal carcinoma-derived growth factor resulted in the induction...

Cell-mediated degradation of type IV collagen and gelatin films is dependent on the activation of matrix metalloproteinases.

Atkinson, S J, Ward, R V, Reynolds, J J, Murphy, G

The ability of normal rabbit dermal fibroblasts to degrade films of type IV collagen and gelatin when stimulated by phorbol ester was shown to be dependent on the induction, secretion and activation...

Binding of gelatinases A and B to type-I collagen and other matrix components.

Allan, J A, Docherty, A J, Barker, P J, Huskisson, N S, Reynolds, J J, Murphy, G

Matrix sequestration of matrix metalloproteinases may be important for the facilitation of remodelling events and the migration of cells through the extracellular matrix. Using an ELISA technique we...

Inhibition of bone resorption in vitro by selective inhibitors of gelatinase and collagenase.

Hill, P A, Docherty, A J, Bottomley, K M, O'Connell, J P, Morphy, J R, Reynolds, J J, ...

Two low-molecular-mass inhibitors of matrix metalloproteinases (MMPs), CT1166, a concentration-dependent selective inhibitor of gelatinases A and B, and Ro 31-7467, a concentration-dependent...

Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts.

Ward, R V, Atkinson, S J, Reynolds, J J, Murphy, G

We report that the isolated C-terminal domain of progelatinase A is inhibitory to the activation of this proenzyme by primary skin fibroblast plasma membranes but is unable to inhibit...

Characterization of gelatinase from pig polymorphonuclear leucocytes. A metalloproteinase resembling tumour type IV collagenase.

Murphy, G, Ward, R, Hembry, R M, Reynolds, J J, Kühn, K, Tryggvason, K

The metalloproteinase 'gelatinase' stored in the granules of pig polymorphonuclear leucocytes has been purified in the latent form. The enzyme is secreted as an Mr 97,000 proenzyme that can be...

Comparison of human stromelysin and collagenase by cloning and sequence analysis.

Whitham, S E, Murphy, G, Angel, P, Rahmsdorf, H J, Smith, B J, Lyons, A, ...

A comparison of the cDNA-derived amino acid sequences of human stromelysin and collagenase with the N-terminal sequences of purified enzymes reveals that these metalloproteinases are highly conserved...

The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinases-2 and tissue inhibitor of metalloproteinases-1.

Ward, R V, Hembry, R M, Reynolds, J J, Murphy, G

Human gingival fibroblasts in culture were shown to secrete a 72 kDa progelatinase, of which a proportion in the medium was found to be complexed with tissue inhibitor of metalloproteinases-2...

Purification and characterization of a rabbit bone metalloproteinase that degrades proteoglycan and other connective-tissue components.

Galloway, W A, Murphy, G, Sandy, J D, Gavrilovic, J, Cawston, T E, Reynolds, J J

A metalloproteinase, 'proteoglycanase', that degrades proteoglycan and insoluble type IV collagen as well as casein was purified to homogeneity from rabbit bone culture medium. The major form of this...

The interaction of purified rabbit bone collagenase with purified rabbit bone metalloproteinase inhibitor.

Cawston, T E, Murphy, G, Mercer, E, Galloway, W A, Hazleman, B L, Reynolds, J J

1. Pure rabbit bone metalloproteinase inhibitor (TIMP) bound tightly to pure rabbit bone collagenase with an apparent Kd of 1.4 X 10(-10) M. 2. The molecular weight of the enzyme-inhibitor complex...

Partial purification of collagenase and gelatinase from human polymorphonuclear leucocytes. Analysis of their actions on soluble and insoluble collagens.

Murphy, G, Reynolds, J J, Bretz, U, Baggiolini, M

The separation and further purification of human polymorphonuclear-leucocyte collagenase and gelatinase, using modifications of the method of Cawston & Tyler [(1979) Biochem J. 183, 647-656], are...

The latent collagenase and gelatinase of human polymorphonuclear neutrophil leucocytes.

Murphy, G, Bretz, U, Baggiolini, M, Reynolds, J J

Two metallo-proteinases of human neutrophil leucocytes, collagenase and gelatinase, were studied. Collagenase specifically cleaved native collagen into the TCA and TCB fragments, whereas gelatinase...

Zinc metalloenzyme properties of active and latent collagenase from rabbit bone.

Swann, J C, Reynolds, J J, Galloway, W A

1. Inhibition of collagenase from rabbit bone cultures by the chelating agents 1,10-phenanthroline and EDTA is almost completely reversed by Zn2+; other metal cations are less effective in reversing...

Purification of rabbit bone inhibitor of collagenase.

Cawston, T E, Galloway, W A, Mercer, E, Murphy, G, Reynolds, J J

1. Rabbit bones in tissue culture synthesize an inhibitor of collagenase during the first 4 days of culture. 2. The inhibitor was purified by a combination of gel filtration, concanavalin...

An inhibitor of collagenase from human amniotic fluid. Purification, characterization and action on metalloproteinases.

Murphy, G, Cawston, T E, Reynolds, J J

1. An inhibitor of collagenase of apparent mol.wt. 28000 was isolated from term human amniotic fluid. 2. It is active against mammalian collagenases from a number of species and tissues as well as...

Metalloproteinases from rabbit bone culture medium degrade types IV and V collagens, laminin and fibronectin.

Murphy, G, Cawston, T E, Galloway, W A, Barnes, M J, Bunning, R A, Mercer, E, ...

Gel-filtration chromatography of culture medium from rabbit bone explants separates three latent metalloproteinases with activities against collagen, proteoglycan and gelatin respectively. The...

Collagenase is a component of the specific granules of human neutrophil leucocytes.

Murphy, G, Reynolds, J J, Bretz, U, Baggiolini, M

Azurophil and specific granules were isolated from human polymorphonuclear neutrophil leucocytes. Collagenase was almost exclusively a component of the specific granules. This finding is in contrast...

Evidence that latent collagenases are enzyme-inhibitor complexes.

Sellers, A, Cartwright, E, Murphy, G, Reynolds, J J

Specific collagenase from the culture media of various rabbit tissues and cells exists in active and latent forms. Latent collagenase is most effectively activated with 4-aminophenylmercuric acetate,...

Matrix metalloproteinases in the formation of human synovial joint cavities.

Edwards, J C, Wilkinson, L S, Soothill, P, Hembry, R M, Murphy, G, Reynolds, J J

Matrix metalloproteinases (MMPs) have been implicated in tissue remodelling in growth and development. A histochemical study of human fetal limbs was undertaken to assess the presence, and...

Purification and properties of a specific collagenase from rabbit synovial fibroblasts.

Werb, Z, Reynolds, J J

1. A specific collagenase from the culture medium of rabbit synovial fibroblasts was purified by gel filtration and ion-exchange chromatography. 2. The enzyme was homogenous on polyacrylamide-gel...

Immunochemical studies with a specific antiserum to rabbit fibroblast collagenase.

Werb, Z, Reynolds, J J

1. Antisera were raised against the collagenase from rabbit synovial fibroblasts and characterized by immunoprecipitation and immunoinhibition reactions. 2. Immunoglobulins from the antisera were...

Rabbit collagenase. Immunological identity of the enzymes released from cells and tissues in normal and pathological conditions.

Werb, Z, Reynolds, J J

1. The immunological cross-reactivity between rabbit collagenases from a variety of normal and pathological sources was examined. The specific antibody raised against collagenase secreted from normal...

Neutral metallo-proteinases of rabbit bone. Separation in latent forms of distinct enzymes that when activated degrade collagen, gelatin and proteoglycans.

Sellers, A, Reynolds, J J, Meikle, M C

Rabbit bones in culture produce specific collagenase and neutral metallo-proteinase activity in latent forms that can be activated by either 4-aminophenylmercuric acetate or trypsin. Latent neutral...

Proteoglycan-degrading enzymes of rabbit fibroblasts and granulocytes.

Werb, Z, Dingle, J T, Reynolds, J J, Barrett, A J

A neutral proteinase secreted by rabbit synovial fibroblasts in parallel with specific collagenase was partially purified by ion-exchange chromatography. At pH 7.6 this proteinase degraded...

Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3.

Cowell, S, Knäuper, V, Stewart, M L, D'Ortho, M P, Stanton, H, Hembry, R M, ...

SW1353 chondrosarcoma cells cultured in the presence of interleukin-1, concanavalin A or PMA secreted procollagenase 3 (matrix metalloproteinase-13). The enzyme was detected in the culture medium by...

Regional and temporal changes in the synthesis of matrix metalloproteinases and TIMP-1 during development of the rabbit mandibular condyle.

Breckon, J J, Hembry, R M, Reynolds, J J, Meikle, M C

Connective tissues synthesise and secrete a family of matrix metalloproteinases (MMPs; collagenases, gelatinases and stromelysins) capable of degrading all the components of connective tissue...

Immunolocalisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis.

Hembry, R M, Bagga, M R, Reynolds, J J, Hamblen, D L

OBJECTIVE--To assess the likely importance of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in the arthritic process. METHODS--Synovial samples from seven joints with rheumatoid...

Rabbit models of arthritis: immunolocalization of matrix metalloproteinases and tissue inhibitor of metalloproteinase in synovium and cartilage.

Hembry, R. M., Bagga, M. R., Murphy, G., Henderson, B., Reynolds, J. J.

The distribution of the matrix metalloproteinases, collagenase, stromelysin, gelatinases A and B, and the tissue inhibitor of metalloproteinases in cartilage and synovium removed from rabbits up to...

Tissue inhibitor of metalloproteinases and collagenase inhibitory activity in lung secretions from patients with chronic obstructive bronchitis: effect of corticosteroid treatment.

Burnett, D, Reynolds, J J, Ward, R V, Afford, S C, Stockley, R A

Tissue inhibitor of metalloproteinases (TIMP) and collagenase inhibitory activity were measured in the sputum from nine subjects with chronic bronchitis before and five days after treatment with...