Example sentences for: factor-α

How can you use “factor-α” in a sentence? Here are some example sentences to help you improve your vocabulary:

  • With improved cardiac function, there should be a reduction inactivation of the adrenergic-renin-angiotensin axes as well as adecrease in activated cytokines such as tumor-necrosis factor-α.In our model of heart failure, cardiac function correlated withthe incidence of apoptosis.

  • Ghrelin and its receptor are expressed in human T-lymphocytes, where they can inhibit cytokine activation, including interleukins, tumor necrosis factor-α and leptin [18].

  • Although the etiologies and pathologies of RA and OA differ, it is clear that in both of these diseases pro-inflammatory cytokines are present, resulting in an inflammatory state as well as cartilage degradation [ 14 ] . As further evidence for the role of pro-inflammatory cytokines in RA, anti-tumor necrosis factor-α (anti-TNF-α) and anti-interleukin 1 (anti-IL-1) therapies can reduce inflammation and retard the progression of disease as assessed radiographically [ 15 16 ] . However, side-effects with these approaches, such as the development of lymphomas in patients using anti-TNF-α therapies, demonstrate that alternative therapies are needed [ 17 ] .

  • Macrophages in RA synovium secrete many inflammatory mediators (IL-1, IL-6, IL-8, tumor necrosis factor-α [TNF-α] and PGE 2 ) and a variety of matrix metalloproteinases, and are thought to play a central role in the inflammation and joint destruction characteristic of RA [ 2].

  • Chess and coworkers have shown that transforming growth factor-α and hepatocyte growth factor increase the phosphorylation of p44/p42 MAPK in H441 cells [ 23 ] . Epidermal growth factor, which binds to the same receptor as transforming growth factor-α, increases SP-A content in human fetal lung [ 24 ] . Hepatocyte growth factor has also been shown to upregulate the synthesis of SP-A in rat type II cells [ 25 ] . Thus, phosphorylation of p44/42 MAPK may be involved in the up-regulation of SP-A gene expression, results consistent with our observation that inhibition of basal levels of p44/42 MAPK phosphorylation may decrease SP-A gene expression.


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