PMID- 8974008
OWN - NLM
STAT- MEDLINE
DCOM- 19970410
LR  - 20061115
IS  - 1079-9907 (Print)
IS  - 1079-9907 (Linking)
VI  - 16
IP  - 12
DP  - 1996 Dec
TI  - In vitro comparison of inhibiting ability of soluble TNF receptor p75 (TBP II) 
      vs. soluble TNF receptor p55 (TBP I) against TNF-alpha and TNF-beta.
PG  - 1047-53
AB  - Tumor necrosis factor-alpha (TNF-alpha) and lymphotoxin (LT, TNF-beta) are 
      pleiotropic cytokines involved in diverse biologic processes, including immune 
      and inflammatory reactions. The biologic responses to TNF are mediated through 
      two forms of cell surface receptors, p55R and p75R. Both receptors exist in a 
      soluble form (p55-sR or TBP I and p75-sR or TBP II), generated by the proteolytic 
      cleavage of the extracellular regions of the molecule. These soluble forms may 
      act by binding and, hence, neutralizing circulating TNF. In the present study, 
      the murine A9 cell line in vitro bioassay was used to test TBP I and TBP II for 
      their neutralizing activity against recombinant human TNF-alpha (rHu-TNF-alpha), 
      and TNF-beta (rHu-TNF-beta) and recombinant murine TNF-alpha (rMu-TNF-alpha). 
      Moreover, TBP I and TBP II were tested for their ability to displace TBP I in the 
      TNF-TBP receptor binding assay (RIBA) against human and murine TNF-alpha as well 
      as TNF-beta. TBP I, from either recombinant (from CHO and Escherichia coli) or 
      urinary origin, was the most effective inhibitor with respect to rHu-TBP II (from 
      CHO) against either human or murine TNF-alpha both in the A9 cells bioassay and 
      in the RIBA assay. Both TBP I and TBP II preparations were less effective in 
      protecting the A9 cells from the toxic effects of rMu-TNF-alpha than from those 
      of rHu-TNF-alpha. The rHu-TBP II preparation was the most effective in inhibiting 
      the cytocidal effect of rHu-TNF-beta on A9 cells and as active as TBP I in the 
      RIBA assay. This result seems to indicate rHu-TBP II as the better soluble TNF 
      receptor able to reverse the rHu-TNF-beta-induced toxicity, at least on A9 cells, 
      leading to consideration of its therapeutic use in those diseases, such as 
      multiple sclerosis, where a role for TNF-beta is indicated.
FAU - Terlizzese, M
AU  - Terlizzese M
AD  - Istituto di Ricerca Cesare Serono SpA, Rome, Italy.
FAU - Simoni, P
AU  - Simoni P
FAU - Antonetti, F
AU  - Antonetti F
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - J Interferon Cytokine Res
JT  - Journal of interferon & cytokine research : the official journal of the 
      International Society for Interferon and Cytokine Research
JID - 9507088
RN  - 0 (Antigens, CD)
RN  - 0 (Lymphotoxin-alpha)
RN  - 0 (Receptors, Tumor Necrosis Factor)
RN  - 0 (Receptors, Tumor Necrosis Factor, Type I)
RN  - 0 (Receptors, Tumor Necrosis Factor, Type II)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tumor Necrosis Factor-alpha)
SB  - IM
MH  - Animals
MH  - Antigens, CD/biosynthesis/genetics/*physiology
MH  - Biological Assay
MH  - CHO Cells
MH  - Cell Line
MH  - Cricetinae
MH  - Escherichia coli
MH  - Humans
MH  - Lymphotoxin-alpha/*metabolism/toxicity
MH  - Mice
MH  - Receptors, Tumor Necrosis Factor/biosynthesis/genetics/*physiology
MH  - Receptors, Tumor Necrosis Factor, Type I
MH  - Receptors, Tumor Necrosis Factor, Type II
MH  - Recombinant Proteins/biosynthesis
MH  - Solubility
MH  - Tumor Necrosis Factor-alpha/*metabolism/toxicity
EDAT- 1996/12/01 00:00
MHDA- 1996/12/01 00:01
CRDT- 1996/12/01 00:00
PHST- 1996/12/01 00:00 [pubmed]
PHST- 1996/12/01 00:01 [medline]
PHST- 1996/12/01 00:00 [entrez]
AID - 10.1089/jir.1996.16.1047 [doi]
PST - ppublish
SO  - J Interferon Cytokine Res. 1996 Dec;16(12):1047-53. doi: 
      10.1089/jir.1996.16.1047.