PHARMACOLOGICAL ACTIVITY OF CHEMICALLY-MODIFIED SUBFRAGMENT FROM HUMAN SERUM IGG .14. INHIBITORY EFFECT OF CARBOXAMIDE-METHYLATED LIGHT-CHAIN (G(1)L) ON TYROSINE PHOSPHORYLATION AND TUMOR-NECROSIS-FACTOR-ALPHAPRODUCTION FROM MURINE MACROPHAGES STIMULATED BY LIPOPOLYSACCHARIDE

Authors
MIMURA T TAKEUCHI K HIRAMATSU K TSUJIKAWA K KOHAMA Y ITOH S
Citation
T. Mimura et al., PHARMACOLOGICAL ACTIVITY OF CHEMICALLY-MODIFIED SUBFRAGMENT FROM HUMAN SERUM IGG .14. INHIBITORY EFFECT OF CARBOXAMIDE-METHYLATED LIGHT-CHAIN (G(1)L) ON TYROSINE PHOSPHORYLATION AND TUMOR-NECROSIS-FACTOR-ALPHAPRODUCTION FROM MURINE MACROPHAGES STIMULATED BY LIPOPOLYSACCHARIDE, Biological & pharmaceutical bulletin, 18(10), 1995, pp. 1377-1381
Citations number
22
Categorie Soggetti
Pharmacology & Pharmacy
Journal title
Biological & pharmaceutical bulletin → ACNP
ISSN journal
09186158
Volume
18
Issue
10
Year of publication
1995
Pages
1377 - 1381
Database
ISI
SICI code
0918-6158(1995)18:10<1377:PAOCSF>2.0.ZU;2-G
Abstract
Carboxamide-methylated light chain (G(1)L) from human serum IgG inhibi ted the secretion of tumor necrosis factor (TNF-alpha), one of the inf lammatory cytokines, from adherent splenocytes and thioglycolate-induc ed peritoneal macrophages. The inhibition of TNF-alpha secretion by G( 1)L was associated with disappearance of tyrosine phosphorylation on a bout 40kDa protein when thioglycolate-induced peritoneal macrophages w ere stimulated with lipopolysaccharide (LPS). It is possible that this G(1)L anti-inflammatory activity occurs through the blockage of the p hosphorylation of about 40 kDa protein.