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Biomedical subjects

D Goossens

Publications and source records attributed to D Goossens.

At least 37 records · Page 2Linked to original sources
PubMed1997

A recombinant human scFv anti-Rh(D) antibody with multiple valences using a C-terminal fragment of C4-binding protein.

Monomeric recombinant molecules prove generally unsatisfactory for in vivo use. Most biological systems are indeed multivalent either structurally, associating different chains, or functionally, when cross-linked by their ligands. Mimicking natural molecules for immune intervention implies the need for multimerizing systems to create multivalent molecules capable of interfering with physiological processing. A multivalent anti-Rh(D) recombinant protein has been designed by reconstructing the antibody binding site of a human monoclonal anti-Rh(D) antibody as a single chain Fv mini antibody, then multimerizing it by inserting at its C-terminal end the C-terminal part of the C4 binding protein (C4bp) alpha chain, which is responsible for the octamer multimerization of that molecule. This soluble multivalent recombinant molecule was functional, bound red blood cells (RBCs), agglutinated them, and did not activate complement. This demonstration model opens the way for future in vivo use of multivalent molecules associating antibody valences and other functional molecules for cell targeting, imaging, or removal of cells such as Rh(D)-positive RBCs for preventing Rh alloimmunization.

Amino Acid Sequence↗
PubMed1997

Reoperative aortic root surgery late after use of histo-acryl.

Cardiovascular reoperations after the use of histo-acryl are extremely rare. A patient is described, who underwent an aortic root replacement according to Bentall's technique, for a postdissectional aneurysm. At that time, to achieve hemostasis, histo-acryl adhesive was applied and a Cabrol's fistula was created. Fourteen years later, a recurrent 'false', aneurysm had developed and the fistula had a hemodynamically significant left-right shunt. At reoperation, the composite graft was replaced by a cryopreserved aortic root allograft with long coronary arteries. To our knowledge, this is the first report of a cardiovascular reoperation after previous use of histo-acryl. This patient also merits attention as to the fact that it illustrates a failure of a modified Cabrol's procedure.

Adult↗
PubMed1996

'In vivo' size of knitted Dacron prostheses (Gelseal) used in the thoracic aorta: a computed tomography study.

When replacing the thoracic aorta, gelatin-sealed triaxial knitted Dacron prostheses are used as they have zero porosity and are easy to handle. It is known that knitted prostheses (not triaxially constructed), when implanted in the abdominal aorta or in the peripheral vessels, show a dilatation of 10-20%. The initial in vivo expansion of this prosthesis in the thoracic aorta was assessed using computed tomography scanning in 18 patients. The graft sizes used were 18mm (n = 4). 20mm (n = 5). 22mm (n = 4), 26mm (n = 1), 28mm (n = 2) and 30mm (n = 2). All patients were kept normotensive postoperatively. Computed tomography scan measurement was performed within 4 weeks of operation. using standard computed tomography equipment and no contrast. Two radiologists checked and agreed upon the slice levels and measurements compared with the manufacturer's stated size referring to internal diameter of the crimped prosthesis. The mean(s.d.) 'in vivo' size was 16.2(6)% larger. This 'true size' should be taken as the reference measurement when considering further dilatation over the period of follow-up.

Adult↗
PubMed1995

Purification and partial characterization of the erythrocyte Kx protein deficient in McLeod patients.

A 37-kDa protein was immunopurified from human erythrocytes as a complex with a monoclonal antibody directed against the Kell blood group protein of 93 kDa. A rabbit antibody raised against the purified complex reacted on a Western blot with the 93-kDa and 37-kDa proteins and was able to immunoprecipitate the 37-kDa component from K0 erythrocytes which express large amount of the Kx antigen, but not from erythrocytes of patients suffering from McLeod syndrome, a X-linked disorder in which the Kx antigen is lacking. Additional studies have shown that the 37-kDa protein is not glycosylated, and permitted the sequence of the 22 first N-terminal amino acids to be established. This sequence was identical to the predicted protein product of the XK gene cloned recently, which is deleted or mutated in McLeod patients [Ho, M., Chelly, J., Carter, N., Danek, A., Crocker, P. & Monaco, A. P. (1994) Cell 77, 869-880]. Our findings provide strong evidence that the 37-kDa red cell membrane protein is identical to the Kx protein produced by the XK structural gene and demonstrate that Kx and Kell proteins are two subunits expressed as a complex hold by disulfide bond(s) at the red cell surface.

Amino Acid Sequence↗
PubMed1994

Perforation of a vascular prosthesis by an eroded thoracic vertebral body.

A case of prosthetic graft rupture due to friction against the vertebral column, eroded by a previously repaired thoracic aortic aneurym, is described. Chiselling away the sharp bony edges of the eroded vertebrae, could have prevented this complication. To our knowledge, this complication has never been reported before.

Aortic Aneurysm↗
PubMed1993

Preparation and biological properties of monoclonal antibodies against human erythropoietin.

Several monoclonal antibodies (Mabs) against human erythropoietin (H-EPO) were obtained by fusion of myeloma cells with splenocytes from mice immunized with purified recombinant H-EPO. Three Mabs (D7, E14 and E73) were selected by radioimmunoprecipitation on the basis of their high affinity against H-EPO. Their dissociation constants were 0.3 nM for E14 and D7, and 17 nM for E73. The immunochemical properties of these Mabs were analyzed in respect to their capacity to react, to purify, and to inhibit the biological activities of H-EPO. a) detection by Western blotting techniques: among the 3 Mabs only D7 was effective by this technique. b) purification: the best results were observed with E14, an approximately 200-fold purification of H-EPO from culture supernatants was obtained in a single immunopurification step. c) inhibition of the biological activity: the specific binding of 125I-labelled H-EPO to its cellular receptor was inhibited by E14 and E73 but not by D7. These three Mabs exhibited similar effects as far as the inhibition of the proliferation of H-EPO dependent cells (measured by 3H-thymidine incorporation) was concerned.

Animals↗
PubMed1992

Niemann Pick c or storage by excessive blood cell destruction: a case presenting a diagnosis problem.

A case of storage disease followed up during 12 a was studied by morphological, histochemical, immunological, and biochemical techniques. Data were analysed in an attempt to differentiate an acquired storage by excessive cell degradation from a storage of genetic origin. If, as it is our belief, a conclusion of acquired storage can be made, this observation in which the same cholesterol metabolism abnormalities as in Niemann Pick type C were seen, leads to a rediscussion of their diagnostic significance.

Blood Cells↗
PubMed1990

Surface orientation and antigen properties of Rh and LW polypeptides of the human erythrocyte membrane.

Time course digestion of intact human erythrocytes and right side-out vesicles with carboxypeptidase Y altered the Rh polypeptides and removed the 125I label that is normally incorporated by cell-surface radioiodination, but did not affect the RhD, Rhc, or RhE antigens. Under the same conditions, however, the LW antigens were rapidly destroyed. Digestion of inside-out and right side-out vesicles with aminopeptidase M was without any detectable effect on the Rh and LW antigens or polypeptides, although glycophorin A was degraded from right side-out but not from inside-out vesicles. These findings demonstrate that the C-terminal domain of the Rh and LW polypeptides is exposed at the external surface of human erythrocytes and indicate, in addition, that the LW antigens and tyrosine residue(s) of the LW and Rh proteins, respectively, are located close to the C termini of these polypeptides. Further studies using monoclonal and polyclonal antibodies showed that LW antigen expression is inhibited by treatment of red cells with EDTA and is selectively restored by Mg2+, but not by Mn2+ or Ca2+, whereas the Rh antigens were not affected under these conditions. In addition, O- and N-glycanase digestion of the LW glycoprotein removed its sugar chains, but did not alter significantly the epitopes recognized by the monoclonal anti-LW antibody.

Aminopeptidases↗
PubMed1990

Production and characterization of human monoclonal antibodies against core protein p25 and transmembrane glycoprotein gp41 of HIV-1.

With a view to obtaining human monoclonal antibodies against HIV-1 antigens we used the Epstein-Barr virus immortalization technique to induce lymphoblastoid cell lines from peripheral blood lymphocytes of 10 people who were seropositive for HIV-1 and had no clinical symptoms. A number of polyclonal lines were obtained which synthesized antibodies against most of the major proteins and glycoproteins of HIV-1. Three stable clones were characterized for class, secretion characteristics and specificity. Two of these clones produce antibodies which react with gp41, and the third reacts with p25. One of the anti-gp41 antibodies was found to have neutralizing activity.

Amino Acid Sequence↗
PubMed1989

Characterization of the blood group Kell (K1) antigen with a human monoclonal antibody.

A human monoclonal anti-Kell (K1) antibody secreted by an Epstein-Barr virus (EBV)-transformed B-cell line was used for binding studies and immunopurification of the K1 blood group antigen. The 125I-labeled antibody bound to 4 to 5 x 10(3) and 2.5 to 3 x 10(3) antigenic sites on K1K1 and K1K2 erythrocytes, respectively, with an affinity constant of 5 x 10(8) mol/L-1. Immunoprecipitation analysis showed that the K1 antigen is carried by a 93 Kd glycoprotein containing several cysteine residues, and approximately six N-glycosidically linked sugar chains but no detectable O-linked sugar. A minor labeled component of 32 Kd was also immunoprecipitated from K1K1 RBCs but the 93- and 32-Kd components were absent from K2K2 and Kell null erythrocytes. Under nonreducing conditions, three bands were detected at 200 (weak), 120, and 93 Kd. We suggest that the 120-Kd component represents a heterodimer of the 93- and 32-Kd proteins covalently linked by disulfide bridge(s). The 93-Kd glycoprotein is a transmembrane component which interacts with the membrane skeleton but is distinct from band 3 as shown by one-dimensional peptide mapping. The site density of K1 antigen blood group on Gerbich-negative RBCs (Ge:-2,-3) was threefold lower than on K1K1 erythrocytes, but the qualitative properties of the 93-Kd component were not modified.

Amino Acids↗
PubMed1989

Heterogeneity in the ability of IgG1 monoclonal anti-D to promote lymphocyte-mediated red cell lysis.

Thirty-four IgG anti-D human monoclonal antibodies (mAb) derived from 18 donor were assessed for their ability to mediate lysis of D+ red cells by lymphocytes in antibody-dependent cell-mediated cytotoxicity assays. Cell-bound antibody was quantified and the mAb were compared at similar levels of sensitization. The majority (23/31) of IgG1 and all (3/3) IgG3 mAb were ineffective; two donors produced both lytic and non-lytic anti-D mAb. Greater sensitivity was achieved using fluid-phase antibody (as culture supernatants) in the assay than was obtained with pre-sensitized red cells. Minimum levels of 2000 anti-D molecules per cell were required for lysis using pre-sensitized cells. Partial D red cells (DIVa, DVa and DVI) were lysed by three mAb that were lytic with normal D+ cells. There was no relationship between lytic ability and Gm allotype or D epitope specificity of the antibodies. Four mAb to other blood group specificities were tested: two (anti-E and anti-G) were lytic and two (anti-c and anti-Kell) were not lytic. Possible reasons for the heterogeneity of the lytic activity by the mAb are discussed.

Antibodies, Monoclonal↗
PubMed1989

Amino acid sequence of the variable domains of a human anti-Rh(c) antibody: presence of an unusually long CDR3 in the lambda chain.

The complete amino acid sequence of the lambda light chain and the variable domain of the heavy chain of an anti-Rh(c) human monoclonal antibody were determined. The lambda chain presents a long third complementarity-determining region sequence with unusual amino acid insertions at the C-terminus. The proposed sequence indicates that this lambda chain may be assigned to the variable region subgroup I. The J segment is identical to that of J lambda 2 except for the first amino acid residue. Positions 152 (serine) and 190 (arginine) from this sequence correspond to the Kern-Oz- isotype, respectively. The VH segment can be classified as a VHIII subgroup member. The CDR1 segment of the anti-Rh(c) VH region has the same sequence as the VH of human BRO protein except for the first residue of the CDR1. The amino acid sequence of the anti-Rh(c) D segment does not match any published D segment. The JH segment used in this protein can be classified as a JH3 with a single amino acid difference at the fourth residue.

Amino Acid Sequence↗