SwePub
Sök i SwePub databas

  Extended search

Träfflista för sökning "WFRF:(Truedsson Lennart) srt2:(1990-1994)"

Search: WFRF:(Truedsson Lennart) > (1990-1994)

  • Result 1-2 of 2
Sort/group result
   
EnumerationReferenceCoverFind
1.
  • Truedsson, Lennart, et al. (author)
  • Antiproliferative effects on human peripheral blood mononuclear cells and inhibition of in vitro immunoglobulin synthesis by Podophyllotoxin (CPH86) and by semisynthetic lignan glycosides (CPH82)
  • 1993
  • In: Clinical and Experimental Rheumatology. - 1593-098X. ; 11:2, s. 179-182
  • Journal article (peer-reviewed)abstract
    • A mixture of natural and semisynthetic (modified) glycosides from Podophyllum emodi (Proresid) has been used for many years in the treatment of rheumatoid arthritis, but its use is hampered by gastrointestinal side effects. Highly purified podophyllotoxin (CPH86) and a preparation containing two semisynthetic podophyllotoxin glycosides (CPH82) are currently being tested in clinical trials. In this study these drugs were shown to inhibit in vitro [3H]-thymidine uptake of human peripheral blood mononuclear cells stimulated by the mitogens concanavalin A, phytohemagglutinin and pokeweed mitogen. Complete inhibition was observed with CPH86 in concentrations > or = 20 ng/ml and with CPH82 in concentrations > or = 1 microgram/ml. In vitro production of IgG, IgM and IgA by PWM-stimulated cells cultured for 7 days was unaffected by 10 ng/ml CPH86 and 100 ng/ml CPH82, but was strongly inhibited by concentrations of CPH86 at > or = 20 ng/ml and CPH82 at > or = 1 microgram/ml. In conclusion, both CPH86 and CPH82 inhibit mitogen induced lymphocyte proliferation and immunoglobulin synthesis and the results may be of help in determining optimal dose levels if related to treatment effects.
  •  
2.
  • Truedsson, Lennart, et al. (author)
  • HC-IgA antibodies of different specificities are normally present in serum : quantitation by ELISA and relationship to the major Ig classes
  • 1990
  • In: APMIS : acta pathologica, microbiologica, et immunologica Scandinavica. - : Wiley. - 0903-4641. ; 98:1-6, s. 249-254
  • Journal article (peer-reviewed)abstract
    • Enzyme-linked immunosorbent assays (ELISA) were developed for direct measurement of protein HC-IgA complexes (HC-IgA) in serum with antibody specificity for rabbit IgG (rheumatoid factor (RF) activity), lipopolysaccharide from Yersinia enterocolitica serotype O:3 (Y3) and tetanus toxoid (TT). About 80% of patients with rheumatoid arthritis had increased concentrations of HC-IgA-RF. The values were correlated with the concentrations of IgA-RF and IgM-RF. HC-IgA anti-Y3 was measured in 45 sera with anti-Y3 antibodies of IgM, IgG and IgA class. The HC-IgA anti-Y3 levels were correlated with those of anti-Y3 of IgG and IgM class, but not of IgA class. For HC-IgA anti-Y3, the closest correlation was that with the specific IgM antibody concentration, rs = 0.63 (p less than 0.001). In 25 normal sera, significant correlations were observed between HC-IgA anti-TT and specific antibodies of IgG and IgA class, but not of IgM class. In 107 sera containing IgA M-components, the total concentration of HC-IgA correlated poorly with both protein HC and with IgA concentrations. It was concluded that specific HC-IgA antibodies are normal constituents of serum, and that their concentrations are not directly related to the serum content of specific IgA antibodies.
  •  
Skapa referenser, mejla, bekava och länka
  • Result 1-2 of 2
Type of publication
journal article (2)
Type of content
peer-reviewed (2)
Author/Editor
Truedsson, Lennart (2)
Geborek, Pierre (1)
Sturfelt, Gunnar (1)
Grubb, Anders (1)
Eberhardt, Kerstin (1)
Karypidis, Anna-Hele ... (1)
University
Lund University (2)
Language
English (2)
Research subject (UKÄ/SCB)
Medical and Health Sciences (2)

Year

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view