Studies on the defect which causes absence of decay accelerating factor (DAF) from the peripheral blood cells of an individual with the Inab phenotype

Tate, Christopher G.; Uchikawa, Makoto; Tanner, M. J. A.; Judson, P. A.; Parsons, Stephen; Mallinson, Gary; Anstee, D. J.

doi:10.1042/bj2610489

Cited by 40 publications

(11 citation statements)

References 21 publications

(24 reference statements)

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“…Monoclonal antibodies 791T/36 (IgG2b anti-791Tgp72; Embleton et al, 1981), BRIC 216 (IgG1 anti-SCR 3 of CD55; Tate et al, 1989), BRIC 220 (IgG1 anti-SCR 1 of CD55; Tate et al, 1989), BRIC 110 (IgG1 anti-SCR 2 of CD55; Spring et al, 1987;Coyne et al, 1992) have been reported previously. BRIC 229 and E4.3 (Sparrow and Mckenzie, 1983) recognize CD59 and CD46 respectively.…”

Section: Monoclonal Antibodiesmentioning

confidence: 66%

CD55 is over-expressed in the tumour environment

Spendlove

Morgan

et al. 2001

Br J Cancer

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Summary CD55 is a protein that protects cells from complement-mediated attack. 791Tgp72 is an antigen which has been used succesfully as a target for both tumour imaging and cancer vaccines. 791Tgp72 has recently been identified as CD55. Quantitative expression of CD55 in the tumour environment was therefore studied. Tumour cells showed a 4-100-fold increase in CD55 cell surface expression when compared to normal cells. Immunohistochemical staining of colorectal tumours also revealed high expression of CD55 in the stroma. To examine the source of this stromal CD55 the ability of both epithelial cells and endothelial cells to produce extracellular CD55 was measured. Tumour cell lines deposit CD55 into their extracellular matrix (ECM) in direct proportion to their cell surface expression. In contrast the ECM from HUVEC cells contained large amounts of CD55 despite expressing low levels of CD55 on their cell surface. Furthermore expression of CD55 on HUVEC cells was increased by exposure to VEGF. Although it remains unclear why CD55 is upregulated in the tumour environment its high level of expression on tumour cells and associated endothelium may explain why it is a good target for both imaging and immunotherapy. © 2001 Cancer Research Campaign http://www.bjcancer.com Keywords: CD55 (DAF), tumour expression; endothelium; stroma; vascular endothelial growth factor (VEGF) 80Received 27 September 1999 Revised 3 February 2000 Accepted 15 March 2000 Correspondence to : LG Durrant British Journal of Cancer (2001) 84(1), 80-86 © 2001 Cancer Research Campaign doi: 10.1054/ bjoc.2000.1570, available online at http://www.idealibrary.com on http://www.bjcancer.com and tumour-conditioned medium or VEGF (10-300 µg ml -1 : Zeneca, Alderley Park, UK) respectively for 48 h prior to harvesting the HUVECs. Tumour-conditioned media was derived from the MDA 231 breast cancer cell line. These were grown to confluence and the media replaced with serum free M199:Hams F12 medium. Following 24 h incubation the resultant conditioned media was filtered for use with the HUVEC. Fresh media was used to culture the control HUVECs. Freshly resected tumours were finely minced and dissociated in collagenase (0.05%; Boehringer Mannheim) and DNase (0.1%; Boehringer Mannheim) for 1 h at 37˚C. Monoclonal antibodiesMonoclonal antibodies 791T/36 (IgG2b anti-791Tgp72;Embleton et al, 1981), BRIC 216 (IgG1 anti-SCR 3 of CD55; Tate et al, 1989), BRIC 220 (IgG1 anti-SCR 1 of CD55; Tate et al, 1989), BRIC 110 (IgG1 anti-SCR 2 of CD55; Spring et al, 1987;Coyne et al, 1992) have been reported previously. BRIC 229 and E4.3 (Sparrow and Mckenzie, 1983) recognize CD59 and CD46 respectively. The BRIC antibodies were purchased from the Blood Group Reference laboratory (Bristol, UK). Normal mouse IgG (Sigma, Dorset, UK) and 708 monoclonal antibody (IgG2b) was used as negative control antibodies. Indirect immunofluorescenceCell lines were incubated with monoclonal antibody for 1 h at 4˚C. Cells were washed twice in fresh media containing 1% FCS and then incubat...

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Section: Monoclonal Antibodiesmentioning

confidence: 66%

CD55 is over-expressed in the tumour environment

Spendlove

Morgan

et al. 2001

Br J Cancer

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“…The following antibodies were used in the study: BRIC 5, reactive with lymphocyte-function-associated antigen-3 (LFA-3, CD58) [14]; BRIC 125, reactive with a glycoprotein of Mr 47,000-52,000 associated with the Rh complex [15], that has been classified as CD47 [16]; BRIC 128, reactive with decay-accelerating factor (DAF) [17]; BS46, of anti-LW'lb specificity [18].…”

Section: Monoclonal Antibodiesmentioning

confidence: 99%

“…These erythrocytes have a deficiency of a number of GPI-linked proteins [28], and thus serve as a useful model system. In view of the variability of expression of such proteins in different patients [29], patient samples were selected that demonstrated a marked deficiency of LFA-3, DAF and acetylcholinesterase [17], although no attempt was made to fractionate the PNH red cells. Immu noblotting with anti-Gya and anti-Hy revealed a gross re duction of binding intensity of both antibodies when com pared with control membranes (Gya, three patients tested;…”

Section: Immunoprécipitationmentioning

confidence: 99%

Evidence That the Human Blood Group Antigens Gya and Hy Are Carried on a Novel Glycosylphosphatidylinositol-Linked Erythrocyte Membrane Glycoprotein

Spring¹,

Reid²

1991

Vox Sanguinis

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Immunoblotting under non-reducing conditions with purified human anti-Gy^a and anti-Hy locates both antigens to an erythrocyte membrane glycoprotein of apparent M(r) 46,750-57,500. The antigens are destroyed on intact red cells by the enzymes pronase, trypsin and chymotrypsin, and by treatment with reducing agents. Immunoblotting with anti-Gy^a and anti-Hy to membranes prepared from red cells pre-treated with an Endo F preparation caused a mean reduction in apparent M(r) of the glycoprotein by 11 kDa at the leading and trailing edges, when compared with control membranes. These results suggest that the glycoprotein has one or more complex N-glycans that are not completely sensitive to Endo F digestion on intact cells. The majority of Gy^a/Hy-active molecules are not tightly associated with the red cell membrane skeleton. A gross reduction in reactivity with anti-Gy^a and anti-Hy by immunoblotting was observed in red cell membranes from patients with paroxysmal nocturnal haemoglobinuria, suggesting a possible membrane linkage via glycosylphosphatidylinositol for the glycoprotein that carries the Gy^a and Hy antigens. Immunoprécipitation of the glycoprotein by anti-Gy^a showed that the protein migrates faster under reducing conditions (Mr 45,000-54,000). A putative dimer was also evident in the precipitates. The glycoprotein was demonstrated to be distinct from lymphocyte-function-associated antigen-3 (CD58), the LW^ab-active glycoprotein, the Fy^a-active glycoprotein, the Ok^a-active glycoprotein and the BRIC 125 glycoprotein (CD47).

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“…commun.]. Recent evidence suggests that the failure of red cells of the Inab phenotype to express DAF results from a mutation which affects the transcription or processing of DAF mRNA [159]. It seems likely that Cromer-related antigens are located on one or other of the four disulphide-bonded globular domains, since all the an tigens require intact disulphide bonds for activity ( fig.…”

Section: Cromer-related Antigens Are On Decay-accelerating Factormentioning

confidence: 99%

Blood Group-Active Surface Molecules of the Human Red Blood Cell

Anstee¹

1990

Vox Sanguinis

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The surface of the human red blood cell is dominated by a small number of abundant blood group active proteins. The major proteins are the anion transport protein (band 3) which has AB(H) activity, and Glycophorin A which has MN activity. Band 3 and Glycophorin A are of equal abundance in the normal red cell membrane (approximately 10^6 copies of each) and the two proteins may associate together as a complex. The glucose transporter (band 4.5) has AB(H) activity and there are about 5 x 10^5 copies/red cell. Several polypeptides associate together to form the Rh complex. The major components of this complex (abundance 1-2 x 10^5 copies/red cell) are polypeptides of M(r) 30,000, polypeptides of M(r) 45,000-100,000 and Glycophorin B. The antigens of the Rh blood group system appear to be associated with the polypeptides of M(r) 30,000 and those of M(r) 45,000-100,000 (the latter also express AB(H) activity). Glycophorin B expresses the blood group ‘N’ antigen and the Ss antigens. Glycophorins C and D carry the Gerbich antigens and, together, these polypeptides comprise approximately 10^5 copies/red cell. The complete protein sequence of all the above-mentioned proteins is known, except for the M(r) 30,000 and M(r) 45,000-100,000 polypeptides of the Rh complex for which only partial sequences are available, and Glycophorin D, the sequence of which can be inferred from that of Glycophorin C. Several of the minor blood group active proteins at the red cell surface (abundance <1.2 x 10^4 /red cell) have been the subject of recent studies. The polypeptide expressing Cromer-related blood group antigens has been identified as decay-accelerating factor and that carrying the In^a / In^b antigens as CD44. The protein sequence of both of these proteins has been deduced form nucleotide sequencing. The polypeptides expressing Kell antigens, Lutheran antigens, Fy antigens, and LW antigens have also been identified and partially characterised.

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Studies on the defect which causes absence of decay accelerating factor (DAF) from the peripheral blood cells of an individual with the Inab phenotype

Cited by 40 publications

References 21 publications

CD55 is over-expressed in the tumour environment

CD55 is over-expressed in the tumour environment

Evidence That the Human Blood Group Antigens Gya and Hy Are Carried on a Novel Glycosylphosphatidylinositol-Linked Erythrocyte Membrane Glycoprotein

Blood Group-Active Surface Molecules of the Human Red Blood Cell

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