Tumour necrosis factor α-induced adipose-related protein (TIARP): co-localization with caveolin-1

2005 ◽  
Vol 97 (5) ◽  
pp. 339-347 ◽  
Author(s):  
Anne-Marie Chambaut-Guérin ◽  
Jacques Pairault
Keyword(s):  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
Related Protein ◽  
Caveolin 1 ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Evidence for an interaction of the metalloprotease–disintegrin tumour necrosis factor α convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease–disintegrin MDC9 with a novel MAD2-related protein, MAD2β

1999 ◽  
Vol 343 (3) ◽  
pp. 673-680 ◽  
Author(s):  
Karen K. NELSON ◽  
Johannes SCHLÖNDORFF ◽  
Carl P. BLOBEL
Keyword(s):  
Cell Cycle ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Cytoplasmic Domain ◽  
Mitotic Arrest ◽  
Tumour Necrosis Factor Α ◽  
Related Protein ◽  
Binding Partner ◽  
Factor Α ◽  
Necrosis Factor

Metalloprotease-disintegrins are a family of transmembrane glycoproteins that have a role in fertilization, sperm migration, myoblast fusion, neural development and ectodomain shedding. In the present study we used the yeast two-hybrid system to search for proteins that interact with the cytoplasmic domain of two metalloprotease-disintegrins, tumour necrosis factor α convertase (TACE; ADAM17) and MDC9 (ADAM9; meltrin γ). We have identified mitotic arrest deficient 2 (MAD2) as a binding partner of the TACE cytoplasmic domain, and a novel MAD2-related protein, MAD2β, as a binding partner of the MDC9 cytoplasmic domain. MAD2β has 23% sequence identity with MAD2, which is a component of the spindle assembly (or mitotic) checkpoint mechanism. Northern blot analysis of human tissues indicates that MAD2β mRNA is expressed ubiquitously. The interaction of the TACE and MDC9 cytoplasmic domains with their binding partners has been confirmed biochemically. The independent identification of MAD2 and MAD2β as potential interacting partners of distinct metalloprotease-disintegrins raises the possibility of a link between metalloprotease-disintegrins and the cell cycle, or of functions for MAD2 and MAD2β that are not related to cell cycle control.

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

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