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Characterization of Clq, Cls and Cl̄ Inh synthesized by stimulated human monocytes in vitro
Author(s) -
Reboul Angeline,
Prandini Marie-Hélène,
Bensa Jean-Claude,
Colomb Maurice G.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80428-2
Subject(s) - cls upper limits , in vitro , chemistry , microbiology and biotechnology , biochemistry , medicine , biology , optometry
Clq, Cls and Cl̄ Inh synthesized and secreted by human monocytes were characterized by SDS‐PAGE. Clq is formed of three chains A ( M r ~35000), B ( M r ~33000) and C ( M r ~25000) which are associated in two subunits A‐B and C‐C. It appears identical to C1q purified from plasma. Cls is secreted as a non‐activated, monocatenar protein of M r ~87000 identical to proenzymic Cls from plasma. Secreted Cl̄ Inh ( M r ~1) has a slightly higher M r than purified plasmatic Cl̄ Inh. Monensin treatment of the cells favours the intracytoplasmic accumulation of products at various glycosylation stages.