Partial purification and characterization of a tumor necrosis factor‐α converting activity

Robache-Gallea, Sylvie; Bruneau, Jean-Michel; Robbe, Hugue; Morand, Valérie; Capdevila, Cécile; Bhatnagar, Neerja; Chouaı̈b, Salem; Roman‐Roman, Sergio

doi:10.1002/eji.1830270532

Cited by 14 publications

(6 citation statements)

References 36 publications

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“…Thus the human TNF‐α based peptide was hydrolysed 37 times more rapidly by the catalytic domain of mouse TACE than the mouse TNF‐α based peptide. TNF‐α converting activity, partially purified from a human monocytic cell line (THP‐1), processed human proTNF‐α, but did not cleave mouse proTNF‐α [33]. These data suggest that peptides based on mouse proTNF‐α are poor in vitro substrates of both human and murine TACE.…”

Section: Resultsmentioning

confidence: 89%

TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3

Amour

Slocombe²,

Webster³

et al. 1998

FEBS Letters

576

436

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TNF-K K converting enzyme (TACE; ADAM-17) is a membrane-bound disintegrin metalloproteinase that processes the membrane-associated cytokine proTNF-K K to a soluble form. Because of its putative involvement in inflammatory diseases, TACE represents a significant target for the design of specific synthetic inhibitors as therapeutic agents. In order to study its inhibition by tissue inhibitors of metalloproteinases (TIMPs) and synthetic inhibitors of metalloproteinases, the catalytic domain of mouse TACE (rTACE) was overexpressed as a soluble Ig fusion protein from NS0 cells. rTACE was found to be well inhibited by peptide hydroxamate inhibitors as well as by TIMP-3 but not by TIMP-1, -2 and -4. These results suggest that TIMP-3, unlike the other TIMPs, may be important in the modulation of pathological events in which TNF-K K secretion is involved.z 1998 Federation of European Biochemical Societies.

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Section: Resultsmentioning

confidence: 89%

TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3

Amour

Slocombe²,

Webster³

et al. 1998

FEBS Letters

576

436

View full text Add to dashboard Cite

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“…Proteases including metalloproteases are known to be involved in the shedding from the surface of lymphocytes of many receptors such as CD62L, IL-6 receptor, and TNF␣. [35][36][37] Although the proteases involved in the shedding of CD100 are unknown, they might be activated under certain conditions such as cell activation, resulting in a modulation of immune responses. This is the first report showing the elevations of the level of serum sCD100 in antibody responses in vivo and in an autoimmune disease.…”

Section: Discussionmentioning

confidence: 99%

Functional soluble CD100/Sema4D released from activated lymphocytes: possible role in normal and pathologic immune responses

Wang

Kumanogoh

Watanabe

et al. 2001

Blood

119

110

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CD100/Sema4D is a 150-kd transmembrane protein that belongs to the semaphorin family. The interaction of CD100 with CD72 is critical for the immune system. In CD100-deficient mice, the production of specific antibodies against T-celldependent antigens is severely impaired, but not against T-cell-independent antigens. Here, a functional soluble CD100 protein (sCD100) released from activated lymphocytes is reported. sCD100 was detected in culture supernatants of activated lymphocytes. Either affinity-purified from supernatants of activated T-cells, or produced as a recombinant sCD100 protein consisting of the extracellular region of the mouse CD100 fused to the human IgG1 Fc (CD100-Fc), sCD100 significantly enhanced CD40-induced Bcell responses. Furthermore, sCD100 was detected either in sera of mice immunized with T-cell-dependent antigens, or in sera of MRL/lpr mice, but not in sera of mice immunized with T-cell-independent antigens. A significant correlation was observed between the level of sCD100 and the titer of autoantibodies in the serum of MRL/lpr mice. This study's findings suggest a potential role for sCD100 in immune responses, including production of antibody, and autoimmune diseases. (Blood. 2001;97: 3498-3504)

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“…We have directly demonstrated that sCD100 generated from the cell surface of lymphocytes by proteolytic cleavage had potent costimulatory activity as well as recombinant sCD100 protein (17). Many receptors, including IL-6R and CD62 ligand, are known to be cleaved by proteases such as metalloproteases and released as soluble forms (31)(32)(33). Although it is not clear whether the transmembrane-type CD100 needs to be converted into a soluble form to exert its functions, sCD100 seems to work as the active form in immune responses.…”

Section: Expression Of Truncated and Soluble Forms Of Cd100 Enhances mentioning

confidence: 99%

Enhanced Immune Responses in Transgenic Mice Expressing a Truncated Form of the Lymphocyte Semaphorin CD100

Watanabe

Kumanogoh

Shi

et al. 2001

The Journal of Immunology

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CD100/Sema4D is a 150-kDa transmembrane protein that belongs to the semaphorin family. Binding of CD100 to CD72 enhances the immune response by turning off the negative signaling effects of CD72. To investigate the physiological functions of CD100 in vivo, we generated transgenic mice expressing a truncated form of CD100. A large amount of the soluble form of CD100 was detected in the sera of mice expressing a truncated form of CD100, although the amount of CD100 was only slightly elevated on the surface of B cells. In the mutant mice the development of conventional B and T cells appeared normal in terms of the surface marker phenotypes, while the number of CD5+ B-1 cells in the peritoneal cavity increased in comparison with wild-type mice. In vitro proliferation and Ig production of B cells in response to CD40 stimulation were considerably enhanced in mice expressing a truncated form of CD100. Additionally, in vivo both Ab responses against T cell-dependent Ags and generation of Ag-specific T cells were enhanced. Furthermore, introduction of the CD100-transgene could restore in vitro B cell responses as well as in vivo Ab production against T cell-dependent Ag in CD100-deficient mice. Collectively, these results not only indicate that CD100 has an important role in the immune system, but also that the soluble form of CD100 released from the cell surface can exert functions in vivo.

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Partial purification and characterization of a tumor necrosis factor‐α converting activity

Cited by 14 publications

References 36 publications

TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3

TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3

Functional soluble CD100/Sema4D released from activated lymphocytes: possible role in normal and pathologic immune responses

Enhanced Immune Responses in Transgenic Mice Expressing a Truncated Form of the Lymphocyte Semaphorin CD100

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