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On the lysis of paroxysmal nocturnal hemoglobinuria erythrocytes by complement: Dual role of C3b (1982)

Jones, C. Michael ; Shin, Moon L. ; Mayer, Manfred M.

Springer

Annals of hematology 45 (1982), S. 249-259

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ISSN: 1432-0584

Keywords: Complement, C3b ; Hemoglobinuria, paroxysmal ; Anemia, hemolytic

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Summary The efficiency of cytolysis by the terminal complement proteins C5b-9 can be markedly enhanced by C3b molecules bound on the target cell membrane (Hammer et al. 1976). This enhancement was shown to be proportional to the number of C3b molecules on the cell membrane. The present experiments have shown that the hemolytic efficiency of the complement membrane attack system is two to five times greater on paroxysmal nocturnal hemoglobulinuria erythrocytes (PNHE) than on normal human E. This difference is attribut to a derivative of C3, probably C3b, on PNHE since it was abolished by anti-C3 but not by anti-C2. The efficiency of C5b-9 to lyse PNHE was only partially decreased by C3b inactivator and β 1H, indicating that the C3b on PNHE is not readily inactivated by its regulatory proteins. Furthermore, cells from a single severely affected patient consumed 3-fold more C5b6 than normal human E yet concommitantly measured membrane fluidity was normal. From these observations we conclude that cell-bound C3b on PNHE serves two functions: (a) it increases the hemolytic efficiency of membrane attack components of the complement system; and (b) it provides sites for assembly of the alternative pathway convertases.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00320192

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Fast atom bombardment and collisional activation mass spectrometry of retinyl phosphate mannose synthesized by liver membranes (1985)

Clifford, A. J. ; Silverman-Jones, C. S. ; Creek, K. E. ; [et al.]

Chichester : Wiley-Blackwell

Biological Mass Spectrometry 12 (1985), S. 221-227

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ISSN: 1052-9306

Keywords: Chemistry ; Analytical Chemistry and Spectroscopy

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: Fast atom bombardment (FAB) and collisional activation dissociation (CAD) mass-analysed ion kinetic energy (MIKE) spectra have confirmed the structures of retinyl phosphate (Ret-P), retinyl phosphate mannose (Ret-P-Man) and guanosine 5′-diphospho-D-mannose (GDP-Man). Ret-P-Man was made in vitro while Ret-P and GDP-Man were chemically synthesized. Positive ion FAB mass spectrometry of Ret-P showed an observable short-lived spectrum with a mass ion at m/z 367 [M + H]+, and a major fragment ion at m/z 269 [M+H—H3PO4]+. Negative ion FAB mass spectrometry of Ret-P showed a strong stable spectrum with a parent ion at m/z 365 [M—H]-, a glycerol (G) adduct ion at m/z 457 [M—H+G]- and a dimer ion at m/z 731 [2M—H]-. GDP-Man showed an intense spectrum with parent ion at m/z 604 [M—H]- and cationized species at m/z 626 [M+Na-2H]- and 648 [M+2Na-3H]-. Negative ion FAB mass spectrometry of Ret-P-Man showed a parent ion at m/z 527 [M—H]- and a fragment ion at m/z 259 [C6H12PO9]-. The CAD-MIKE spectra showed structurally significant fragment ions at m/z 442 and 361 for the [M—H]- ion of GDP-Man, and at m/z 509, 406, 364 and 241 for the [M—H]- ion of Ret-P-Man. FAB and CAD-MIKE spectra have been applied successfully to confirm the structure of Ret-P-Man made in vitro from Ret-P and GDP-Man.

Additional Material: 5 Ill.