Family studies on the third component of complement (C3), 6h1-antitrypsin polymorphism (locus E1 and E2) in the area of Marburg (Germany)

1972 ◽  
Vol 17 (1) ◽  
pp. 85-87 ◽  
Author(s):  
H. W. Goedde ◽  
L. Hirth ◽  
H. -G. Benkmann ◽  
S. Singh ◽  
G. G. Wendt
Keyword(s):  
Family Studies ◽  
Complement C3 ◽  
The Third ◽  
Third Component Of Complement

scholarly journals THE BIOLOGIC SIGNIFICANCE OF THE THIRD COMPONENT OF COMPLEMENT (C3) IN NONIMMUNE HOST DEFENSES

1974 ◽  
Vol 8 (4) ◽  
pp. 421-421
Author(s):  
Jerry A Winkelstein ◽  
Mary Ruth Smith ◽  
Hyun S Shin ◽  
David H Carver
Keyword(s):  
Complement C3 ◽  
Host Defenses ◽  
The Third ◽  
Third Component Of Complement

scholarly journals Metabolism of the third component of complement (C3) in patients with rheumatoid arthritis

1972 ◽  
Vol 15 (1) ◽  
pp. 49-56 ◽  
Author(s):  
Arthur Weinstein ◽  
Keith Peters ◽  
David Brown ◽  
Rodney Bluestone
Keyword(s):  
Rheumatoid Arthritis ◽  
Complement C3 ◽  
The Third ◽  
Third Component Of Complement

scholarly journals Biosynthesis of the third component of complement (C3) by the human monocytic-cell line U-937 Induction by phorbol myristate acetate

1986 ◽  
Vol 239 (3) ◽  
pp. 711-716 ◽  
Author(s):  
S Bengio ◽  
D Gilbert ◽  
P Peulve ◽  
M Daveau ◽  
M Fontaine
Keyword(s):  
Phorbol Myristate Acetate ◽  
Complement C3 ◽  
Enzyme Linked Immunosorbent Assay ◽  
Haemolytic Activity ◽  
Subunit Structure ◽  
Single Chain ◽  
Myristate Acetate ◽  
Monocytic Cell ◽  
The Third ◽  
Third Component Of Complement

Phorbol myristate acetate (PMA)-stimulated human monocyte-like cells (U-937) were found to synthesize the third component of complement (C3), as shown by enzyme-linked immunosorbent assay and immunoprecipitation from [35S]methionine-labelled culture supernatants. C3 synthesis occurred at a rate of about 160 ng of C3/24 h per 10(6) cells on day 7 after addition of PMA; it was blocked by cycloheximide treatment and was restored after removal of the inhibitor. SDS/polyacrylamide-gel-electrophoretic analysis of the immunoprecipitated protein showed that the size and subunit structure of the newly synthesized C3 were identical with those of plasma C3, and that a single-chain intracellular precursor was present in the cell lysates. Haemolytic assays showed that the synthesized C3 fully expressed functional activity in early culture within 4 h. After longer culture, a loss of haemolytic activity was observed. The possibility that newly secreted C3 is cleaved by U-937 cells themselves was suggested.

Expression of the third component of complement, C3, in regenerating limb blastema cells of urodeles

1998 ◽  
Vol 35 (6-7) ◽  
pp. 372 ◽  
Author(s):  
Katia Del Rio-Tsonis ◽  
Panagiotis A. Tsonis ◽  
Ioannis K. Zarkadis ◽  
Andreas G. Tsangas ◽  
John D. Lambris
Keyword(s):  
Complement C3 ◽  
The Third ◽  
Third Component Of Complement

scholarly journals Two populations of granulocytes in paroxysmal nocturnal hemoglobinuria

Blood ◽  
1979 ◽  
Vol 53 (5) ◽  
pp. 928-934 ◽  
Author(s):  
M Stern ◽  
WF Rosse
Keyword(s):  
Stem Cell ◽  
Paroxysmal Nocturnal Hemoglobinuria ◽  
Complement C3 ◽  
51Cr Release ◽  
Normal Cells ◽  
Lytic Action ◽  
The Third ◽  
Two Populations ◽  
Complement Lysis ◽  
Third Component Of Complement

Abstract The granulocytes in paroxysmal nocturnal hemoglobinuria (PNH) are defective, and the defect is similar to that previously described for the PNH erythrocyte. Using anti-I antibody to activate complement and 51Cr release to detect cell lysis, we found two populations of granulocytes that differed in their susceptibility to lysis by complement in 5 of 6 patients. A proportion of the cells were lysed by one-fifteenth to one-twentieth the amount of complement required to lyse normal cells; the remainder of the granulocytes appeared to be normal in their susceptibility to the lytic action of complement. The binding of the third component of complement (C3) to PNH granulocytes was at least twice that bound to normal cells, even though the binding of antibody was the same for normal and PNH cells. This suggests that the binding of C3 and probably the efficiency of the terminal steps of complement lysis are increased in the abnormal PHN granulocyte. These defects affect only a portion of the granulocytes, thus suggesting that the disorder is a clonal stem cell abnormality.

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