Words similar to factor-α
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:
Once in the tissue, monocytes undergo the poorly understood process of transformation to macrophages with altered morphology and function [ 19 ] . In arthritis, synovial macrophages might cause joint destruction by differentiating to bone-resorbing osteoclasts [ 20 ] or by releasing cartilage-degrading enzymes and cytokines, such as interleukin-1 and tumor necrosis factor-α [ 8 ] . It has therefore been suggested that therapies for chronic arthritis should be aimed at depleting joint mononuclear cells or controlling the activation of synovial macrophages [ 21 ] . Indeed, elimination of macrophages by clodronate-laden liposomes in rat models of adjuvant [ 22 ] and antigen-induced arthritis [ 23 ] induces amelioration of the arthritis.
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].
Tumour necrosis factor-α blockade reduces synovial expression of CCL2 and CXCL8 and reduces inflammatory cell migration into RA joints [ 9 ] . In addition, these chemokines, produced by RA synovial stromal cells, have been shown to stimulate monocyte migration [ 10 ] . The functional importance of chemokines in joint inflammation has also been established in animal models of RA where antibodies to these mediators significantly reduce both the number of leukocytes recruited and the severity of disease.
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.
For instance, tumor necrosis factor-α (TNF-α) can modify intracellular signal transduction and regulate ionic channel activities in various epithelial cells [ 9 ] . A few studies have shown that cytokines can alter biliary epithelial cell function [ 10 11 ] .
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