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Biomedical subjects

P De Waele

Publications and source records attributed to P De Waele.

14 recordsLinked to original sources
PubMed2006

Osteopontin and bone metabolism in healing cranial defects in rabbits.

Non-collagen proteins such as bone sialoprotein and osteopontin (OPN) form 10% of the extracellular bone matrix. In this study, the influence of OPN on bone repair was investigated. Human OPN (Innogenetics) was produced by a recombinant technique and bonded onto the surface of hydroxyapatite (Interpore 200). Thirty rabbits were divided into six equal groups. A circular defect (10mm) was prepared in each parietal bone. In four rabbits of each group the left and right defects were filled with either OPN-coated hydroxyapatite (OPN-HA) or non-coated hydroxyapatite (HA). One sham animal of each group received no implants. The animals were killed after 1, 2, 6, 12, 18 and 30 weeks. The histological sections were scanned and analysed digitally. There were no statistically significant differences in total bone formation between defects filled with OPN-HA and HA. Bone formation at the borders of the healing area was significantly higher in defects filled with OPN-HA than in those filled with HA. Less bone formation was noted in the OPN-HA and HA groups at the centre of the healing area than at the borders of the healing area and the dural area. Although some animals in the sham group showed a high level of bone formation in the dural area, this was not significantly different to that in the dural area of the other groups. There was no sign of infection or tissue rejection of the graft.

Animals↗
PubMed2005

Osteopontin and bone metabolism: a histology and scintigraphy study in rats.

Osteopontin (OPN) is one of the major non-collagen proteins in extracellular bone matrix. To elucidate the function of OPN in bone metabolism, a cellular defect was created in parietal bone and tibia of 12 rats. In Group 1, the left defects were filled with OPN-coated hydroxyapatite (OPN-H). In Group 2, the right defects were filled with non-coated hydroxyapatite (N-H). In both groups, the contra lateral defects were used as control defects. In Group 3, OPN-H was inserted in the left defects and N-H in the right defects. Bone metabolism was measured by (45)Ca and technetium-99m methylene diphosphonate scintigraphy for 4 weeks. Scintigraphy did not show any significant differences in bone metabolism between the defects filled with OPN-H and N-H. A higher bone metabolism was measured between the parietal defects filled with OPN-H or N-H in comparison with the parietal control defects. This difference, however, was not significant and was less for tibia defects. Histological observation (7th week) shows less inflammatory cells at the tibia defects filled with OPN-H compared to the tibia defects filled with N-H. This study did not show any acceleration or inhibition of bone metabolism in parietal or tibia bone in rats, but there is some evidence that OPN might influence inflammatory cells in bone matrix.

Animals↗
PubMed2005

A prospective multicenter study of the efficacy and tolerability of cryopreserved allogenic human keratinocytes to treat venous leg ulcers.

Allogeneic human keratinocyte cultures have been used to treat burn wounds, donor sites, and chronic skin ulcers with some success. Cryopreservation of these cultures allows for the production of large standardized batches that are readily available for use. The aim of the study presented in this report was to study effects of cryopreserved cultured allogenic human keratinocytes (CryoCeal) on chronic lower extremity wounds. Parameters were measured to study efficacy, tolerability, pain associated with chronic wounds, and quality of life of patients. Twenty-seven patients with hard-to-heal venous leg ulcers received a maximum of 9 applications of CryoCeal in a prospective, uncontrolled multicenter study lasting 48 weeks. Eleven out of 27 patients (41%; 95% CI: 22%-61%) had complete wound closure within 24 weeks (1 week). The time required for complete wound closure in these 11 patients ranged from 4.1 to 24.9 weeks. Only 1 patient had recurrence of the ulcer at 48 weeks. Local (wound) pain scores decreased from a mean of 2.5 at baseline to 0.9 at week 24. Fifty percent of the patients attained a pain score of 0 after 12 weeks and remained stable at this score until the end of the study. Overall, the patient quality of life was better at week 24, compared to baseline values. The treatment was well tolerated, and wound infection was the most frequently occurring adverse event.

Adult↗
PubMed1999

Prolonged skin graft survival by administration of anti-CD80 monoclonal antibody with cyclosporin A.

Costimulation via the B7/CD28 pathway is an important signal for the activation of T cells. Maximal inhibition of T-cell activation and the induction of alloantigen-specific nonresponsiveness in vitro was achieved using anti-CD80 monoclonal antibody (mAb) in combination with cyclosporin A (CsA). Based on this knowledge, the efficacy of the prophylactic treatment of anti-CD80 mAb and CsA on allogeneic skin graft survival was tested in a preclinical rhesus monkey model. No side effects have been observed. Administration of anti-CD80 mAb resulted in high mAb serum levels that decreased to undetectable values around day 7. At the same time, the anti-mouse antibody response started to develop. The anti-CD80 mAb bound to peripheral blood mononuclear cells and was detectable in lymph node and grafted skin during the treatment period. The skin graft survival time of untreated or suboptimally CsA-treated rhesus monkeys was 10 days. Treatment with CsA (blood levels of 100-160 ng/ml) in combination with anti-CD80 mAb (0.5 mg/kg) resulted in a significantly increased skin graft survival time to 14 days. Eventually, skin grafts in all rhesus monkeys were rejected, which coincided with an increase in helper and cytotoxic T-cell frequency and induction of an antibody response directed against the donor antigens. Therefore, treatment of anti-CD80 mAb in combination with CsA has significant immunosuppressive potency, but was unable to induce donor-specific nonresponsiveness in skin graft recipients.

Adjuvants, Immunologic↗
PubMed1996

Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors.

Truncated activin type II receptors have been reported to inhibit activin receptor signaling in Xenopus embryos, although the mechanism of action for this effect has not been fully understood. In the present study we demonstrate that in P19 embryonal carcinoma cells both the induction of the activin responsive 3TP-lux reporter construct and the inhibition of retinoic acid-induced neuronal differentiation by activin are blocked by expression of a truncated activin receptor. To reveal the mechanism of action of truncated activin receptors, the interaction between different activin receptors has been investigated upon coexpression in COS cells followed by cross-linking of 125I-activin A and subsequent immunoprecipitation. Complexes between a truncated activin type IIA receptor and activin type IA and type IB receptors can be formed, as demonstrated by coimmunoprecipitation of these type I receptors with the truncated activin type IIA receptor. Other type I receptors known as ALK-1 and ALK-6 also coimmunoprecipitate with the truncated type IIA receptor, whereas ALK-3 and ALK-5 do not. Furthermore, the activin type IIB2 receptor does not coimmunoprecipitate with the truncated type IIA receptor, but decreases activin binding to the truncated type IIA receptor. In double immunoprecipitation experiments with cell lysates from COS cells, in which full-length activin type IIA and type IIB2 receptors were cotransfected, no interaction between these receptors was found. In contrast, homomeric complexes of full-length activin type IIA receptors were detected. These results implicate that truncated activin receptors can interfere with activin signaling by interacting with activin type I receptors. Additionally, truncated activin type IIB2 receptors might also interfere with type IIA receptor signaling by decreasing activin binding to the type IIA receptor and therefore might be more potent in inhibiting activin signal transduction. Furthermore, our data indicate that truncated type IIA receptors can interact with other type I receptors and as such might inhibit signal transduction by type I receptors other than activin type IA and type IB receptors.

Activin Receptors↗
PubMed1993

Apparent Greig cephalopolysyndactyly and sinus node disease.

We present the clinical findings and follow-up data from birth to 10.5 years in a boy with Greig cephalopolysyndactyly who, in addition, presents sinus node disease ("sick sinus syndrome"). The significance of the concurrence of Greig cephalopolysyndactyly syndrome, an autosomal dominant condition mapped at 7p13, and sinus node disease is discussed.

Abnormalities, Multiple↗
PubMed1990

Expression and processing of the activin-A/erythroid differentiation factor precursor: a member of the transforming growth factor-beta superfamily.

The biosynthesis and intracellular processing of the polypeptide precursor of the beta A-chain of the fertility hormone inhibin were assessed by infecting a wide spectrum of cell types with a recombinant vaccinia virus. Most cell lines, including follicular granulosa cells, secrete both prohormone and mature hormone as homodimers (activin) composed of disulfide-linked subunits of 54 kDa (proactivin-A) and 14 kDa (activin-A), respectively, and a small amount of prohormone-mature hormone heterodimers. Mature activin is secreted from mouse pituitary cells (AtT-20), while pig kidney cells [PK(15)] secrete mostly proactivin. More prohormone is secreted in the presence of NH4Cl, suggesting that prohormone processing is facilitated by low pH. Proactivin-A is not a ligand for the mannose-6-phosphate/insulin growth factor-II receptor. The recombinant activin stimulates FSH release from pituitary cells and differentiates erythroleukemia cell lines in vitro.

Acetylglucosaminidase↗
PubMed1988

Expression in non-lymphoid cells of mouse recombinant immunoglobulin directed against the tumour marker human placental alkaline phosphatase.

From a mouse hybridoma cell line secreting a monoclonal antibody directed against the tumour marker human placental alkaline phosphatase, mRNA coding for the H and L chains of this antibody was isolated and cloned as cDNA. Sequence analysis of the H and L chain cDNAs confirmed the IgG2b,kappa subtype previously established. Recloning the H and L chain cDNA information into SV40-based vectors enabled us to obtain expression of functional immunoglobulin upon cotransfection into COS or CHO dhfr- cells. This illustrates that non-lymphoid cells also have the capacity to assemble active immunoglobulins.

Alkaline Phosphatase↗
PubMed1988

Expression of functional mouse antibodies directed against the tumour marker human placental alkaline phosphatase in non-lymphoid cells.

A mouse hybridoma cell line was isolated which produces monoclonal antibodies (MAbs) of the IgG2b, kappa subtype directed against the tumour-associated marker human placental alkaline phosphatase (hPLAP). The mRNAs coding for the heavy (H) and light (L) chains were cloned as cDNA copies. These genes were then separately inserted into the eukaryotic expression vector pSV23p, under control of the SV40 early promoter. Both genes were introduced with the DEAE-dextran technique in COSI cells, and 72 hr after transfection, 10 ng/ml functional antibodies could be detected in the supernatant of the cells. Permanent CHO cell lines secreting 100 ng/ml functional antibodies were established upon transfection of CHO (dhfr-) cells with the plasmids containing the H and L cDNAs and the plasmid pAdD26SVp-(A)-3 carrying the mouse dihydrofolate reductase (dhfr) gene. A plasmid construction in which we inserted a stop codon-containing sequence behind the hinge region of the H-chain cDNA sequence yielded immuno-competent F(ab')2 molecules upon transfection of COS or CHO cells. Our results indicate that not only lymphoid cells, but also non-lymphoid cells, are capable of synthesis and assembly of immunoglobulin chains that are immunologically fully competent.

Alkaline Phosphatase↗
PubMed1983

Use of monoclonal antibodies to detect human placental alkaline phosphatase.

Convenient, sensitive, and specific solid-phase immunoassays involving monoclonal antibody are described for the determination of human placental alkaline phosphatase (hPLAP). An endogenous enzyme immunoassay combined the specificity of the immunological and the enzymatic reactions. Alternatively, a solid-phase "sandwich" radioimmunoassay involving immobilized polyclonal rabbit anti-hPLAP in combination with iodinated monoclonal antibody provided some additional advantages. Both tests can be used to detect hPLAP from various sources, e.g., in human sera during pregnancy or as a tumor marker. The radioimmunoassay detected an increase in hPLAP at nine weeks of gestation. We discuss the use of monoclonal antibodies for the differentiation of different alkaline phosphatase isoenzyme types by electrophoresis on starch gel.

Alkaline Phosphatase↗