Binding of human tumor necrosis factor to high affinity receptors on HeLa and lymphoblastoid cells sensitive to growth inhibition.

Inflammatory properties of recombinant tumor necrosis factor in rabbit skin in vivo.

“…The short duration of action of TNF in vivo may be related to its rapid internalization and degradation after binding to its receptor (16) . This short biological halflife of TNF in vivo may be compensated for by the high amounts of TNF that can be produced by macrophages (up to 2% of their protein biosynthesis).…”

Cachectin/tumor necrosis factor exerts endocrine, paracrine, and autocrine control of inflammatory responses.

“…Most cell types including liver, kidney, muscle, and adipose tissue have been shown to possess specific high affinity receptors for cachectin/TNF (11), and the consequences of ligand binding appear to be tissue specific. Cachectin/TNF exhibits a high affinity for its receptor with a Ka estimated at 109 M -| (7,11,48,123). Polyclonal antisera raised in rabbits against peptides representing the NH2 terminus of human recombinant cachectin/TNF have been shown to block both receptor binding and bioactivity (111).…”

“…In vitro and in vivo studies indicate that the biological effects of cachectin/TNF are maximally expressed at receptor occupancies as low as 5-10%. Binding of cachectin/TNF to its receptor is followed by rapid internalization (7) and degradation (123).…”

Relationship between tumour necrosis factor-alpha (TNFα) production and a specific multiple sclerosis (MS) associated TNF gene haplotype

“…These TNF receptors have been detected in a variety of normal tissues and cell lines which are either sensitive or resistant to TNF. 11,12 Two distinct TNF receptors with 55 ± 60 kDa (I) and 75 ± 80 kDa (II) have now been identi®ed. 13,14 Soluble forms of these have also been identi®ed and both are able to neutralise circulating TNFa.…”