Regulation of Sertoli cell activin A and inhibin B by tumour necrosis factor α and interleukin 1α: Interaction with follicle-stimulating hormone/adenosine 3′,5′-cyclic phosphate signalling

2011 ◽  
Vol 335 (2) ◽  
pp. 195-203 ◽  
Author(s):  
Saito Kazutaka ◽  
Wendy R. Winnall ◽  
Julie A. Muir ◽  
Mark P. Hedger
Keyword(s):  
Tumour Necrosis Factor ◽  
Sertoli Cell ◽  
Tumour Necrosis ◽  
Follicle Stimulating Hormone ◽  
Inhibin B ◽  
Tumour Necrosis Factor Α ◽  
Interleukin 1Α ◽  
Cyclic Phosphate ◽  
Factor Α ◽  
Necrosis Factor

Immunoexpression of tumour necrosis factor-α, interleukin-1α and interleukin-10 on odontogenic cysts and tumours

2016 ◽  
Vol 50 (5) ◽  
pp. 437-445 ◽  
Author(s):  
M. C. Sá ◽  
F. R. de Matos ◽  
T. S. Conceição ◽  
A. C. G. H. Leitão ◽  
R. A. Freitas
Keyword(s):  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Interleukin 10 ◽  
Odontogenic Cysts ◽  
Tumour Necrosis Factor Α ◽  
Interleukin 1Α ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Fibronectin-fragment-induced cartilage chondrolysis is associated with release of catabolic cytokines

1997 ◽  
Vol 321 (3) ◽  
pp. 751-757 ◽  
Author(s):  
Gene A. HOMANDBERG ◽  
Francis HUI ◽  
Catherine WEN ◽  
Christopher PURPLE ◽  
Kelly BEWSEY ◽  
...  
Keyword(s):  
Articular Cartilage ◽  
Growth Factor ◽  
Tumour Necrosis Factor ◽  
Interleukin 6 ◽  
Tumour Necrosis ◽  
Cartilage Damage ◽  
Tumour Necrosis Factor Α ◽  
Interleukin 1Α ◽  
Factor Α ◽  
Necrosis Factor

Fibronectin fragments have both catabolic and anabolic activities toward articular cartilage explants in vitro. Whereas a 1 nM concentration of an N-terminal 29 kDa fibronectin fragment (Fn-f) increases the proteoglycan (PG) content of cartilage without induction of matrix metalloproteinases (MMPs), 0.1Ő1 ƁM Fn-f temporarily suppresses PG synthesis and enhances MMP release. The higher concentrations cause an initially rapid PG depletion during the first week of culture, followed by much slower PG loss and gradually increasing rates of PG synthesis. To test for the involvement of mediators, human articular cartilage was cultured with Fn-f, and conditioned media were assayed for selected cytokines and factors. With 1 nM Fn-f, the release of the anabolic factors, insulin growth factor-I and transforming growth factor β1, from cultured cartilage was enhanced by 50Ő100% during the entire 28-day culture period and this was associated with both supernormal rates of PG synthesis and PG content. However, the higher concentrations of Fn-f additionally enhanced release, by at least 10-fold, of the cytokines, tumour necrosis factor α, interleukin-1α, interleukin-1β and interleukin-6 while causing depletion of cartilage PG. Release of tumour necrosis factor α, interleukin 1β and interleukin 1α peaked at days 2, 3 and 9 during or slightly after the period of maximal PG depletion and decreased to control levels by days 7, 7 and 21 respectively, whereas release of interleukin 6 was enhanced throughout the culture period. Neutralizing antibodies to the catabolic cytokines reduced Fn-f-mediated MMP-3 release and suppression of PG synthesis. The temporal aspects of this interplay between catabolic and anabolic factors are consistent with the kinetics of Fn-f-mediated cartilage damage and attempted repair and may be relevant to cartilage damage and repair in vivo.

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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