References of "FOIDART, Jean-Michel"
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See detailDetection of specific collagen types in normal and keratoconus corneas.
Newsome, D. A.; Foidart, Jean-Michel ULg; Hassell, J. R. et al

in Investigative Ophthalmology & Visual Science (1981), 20(6), 738-50

Keratoconus is a corneal disease of unknown cause that involves a progressive thinning and scarring of the corneal connective tissue. We examined normal human and keratoconus corneas, including one healed ... [more ▼]

Keratoconus is a corneal disease of unknown cause that involves a progressive thinning and scarring of the corneal connective tissue. We examined normal human and keratoconus corneas, including one healed penetrating keratoplasty specimen. Organ cell cultures of normal and keratoconus corneal specimens were labeled with radioactive proline and analyzed by CM-cellulose chromatography and slab gel electrophoresis to determine collagen biosynthesis. Collagen types I and III were synthesized in similar amounts by normal and keratoconus stromacytes in culture. Specifically purified antibodies were used to determine the distribution of collagen types in tissue sections by immunofluorescence. The distribution of collagen types I, III, and IV in keratoconus was also similar to that in normal corneas, except that scarred regions in keratoconus and at the host-graft juncture were largely type III. Immunofluorescent reaction of the anti-type IV collagen antibodies with Bowman's layer, in particular, and Descemet's membrane in keratoconus specimens indicated extensive destruction. Basement membrane destruction may play an important role in this disease. [less ▲]

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See detailCollagen localization in normal and fibrotic human skeletal muscle.
Foidart, M.; Foidart, Jean-Michel ULg; Engel, W. K.

in Archives of Neurology (1981), 38(3), 152-7

The distribution of types I to IV collagen, types I and III p-N collagen, and fibronectin in human skeletal muscle was studied by immunofluorescence using purified antibodies to those proteins. In normal ... [more ▼]

The distribution of types I to IV collagen, types I and III p-N collagen, and fibronectin in human skeletal muscle was studied by immunofluorescence using purified antibodies to those proteins. In normal muscle, types I and III collagen, types I and III p-N collagen, and fibronectin were localized in the endomysium and perimysium. Type IV collagen was restricted to basement membrane. Type II collagen was not present. In Duchenne's musclar dystrophy and dermatomyositis/polymyositis (DM/PM), the prominently increased endomysial and perimysial fibrosis consisted of types I and III collagen, types I and III p-N collagen, and fibronectin. In DM/PM, thickening of the walls of perimysial venular and arteriolar vessels was associated with accumulation of types I and III collagen, types I and III p-N collagen, and fibronectin, as well as type IV collagen. There was no disease-specific accumulation of collagen, p-N collagen, or fibronectin. [less ▲]

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See detailThe production and localization of laminin in cultured vascular and corneal endothelial cells.
Gospodarowicz, D.; Greenburg, G.; Foidart, Jean-Michel ULg et al

in Journal of Cellular Physiology (1981), 107(2), 171-83

The production and localization of laminin, as a function of cell density (sparse versus confluent cultures) and growth stage (actively growing versus resting cultures), has been compared on the cell ... [more ▼]

The production and localization of laminin, as a function of cell density (sparse versus confluent cultures) and growth stage (actively growing versus resting cultures), has been compared on the cell surfaces of cultured vascular and corneal endothelial cells. Comparison of the abilities of the two types of cells to secrete laminin and fibronectin into their incubation medium reveals that vascular endothelial cells can secrete 20-fold as much laminin as can corneal endothelial cells. In contrast, both cell types produce comparable amounts of fibronectin. Furthermore, if one compares the secretion of laminin and fibronectin as a function of cell growth, it appears that the laminin released into the medium by either vascular or corneal endothelial cells, is a function of cell density and cell growth, since this release is most pronounced when the cells are sparse and actively growing, and decreases by 10- and 30-fold, respectively, when either vascular or corneal endothelial cell cultures become confluent. With regard to fibronectin secretion, no such variation can be seen with vascular endothelial cell cultures, regardless of whether they are sparse and actively growing or confluent and resting. Corneal endothelial cell cultures, demonstrated a twofold increase in fibronectin production when they were confluent and resting as compared to when they were sparse and actively growing. When the distribution of laminin versus fibronectin within the apical and basal cell surfaces of cultured corneal and vascular endothelial cells is compared, one can observe that unlike fibronectin, which in sparse and subconfluent cultures can be seen to be associated with both the apical and basal cell surfaces, laminin does not ever seem to be present on the apical cell surface. In confluent cultures, laminin can be found associated primarily with the extracellular matrix beneath the cell monolayer, where it codistributes with type IV collagen. [less ▲]

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See detailCollagen heterogeneity in normal human bone marrow
Bentley, S. A.; Alabaster, O.; Foidart, Jean-Michel ULg

in British Journal of Haematology (1981), 48(2), 287-91

Paraffin embedded sections of formalin fixed, decalcified, normal, human, vertebral bone were stained immunohistochemically for collagen types I, III and IV using the peroxidase--anti-peroxidase (PAP ... [more ▼]

Paraffin embedded sections of formalin fixed, decalcified, normal, human, vertebral bone were stained immunohistochemically for collagen types I, III and IV using the peroxidase--anti-peroxidase (PAP) technique. Preparations stained for collagen types I and III were virtually identical in appearance. These substrates were localized to the cytoplasm and fibrillar processes of a population of cells which were sparsely distributed within the haemopoietic compartment of the bone marrow, being particularly prominent in relation to the marrow sinusoids and fat spaces. They would thus appear to parallel the known distributions of reticulum cells, although their morphology differed in some respects from classical descriptions of the latter cell type. Type IV collagen was found in association with the endothelial lining of the sinusoids. Other connective tissue elements (bone, periosteum, endosteum, blood vessels, etc.) showed characteristic collagen heterogeneity. These results indicate that collagen is a significant component of the bone marrow connective tissue. [less ▲]

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See detailImmunopathological and clinical studies in herpes gestationis.
Foidart, Jean-Michel ULg; Yaar, M.; Hall, R. et al

in British Journal of Obstetrics & Gynaecology (1981), 88(2), 153-9

Herpes gestationis is a recurring pruritic, vesiculobullous disease of pregnancy and puerperium. Recently, Lawley et al (1979) reported a high frequency (38 per cent) of fetal morbidity and mortality in ... [more ▼]

Herpes gestationis is a recurring pruritic, vesiculobullous disease of pregnancy and puerperium. Recently, Lawley et al (1979) reported a high frequency (38 per cent) of fetal morbidity and mortality in 40 cases of immunologically proven herpes gestationis. This study was undertaken to determine whether the antibody to skin basement membrane (found in most patients with herpes gestationis) is able to bind to the placenta basement membranes and thereby to threaten the pregnancy. We were unable to detect this antibody in the placental basement membranes of a patient with herpes gestationis, nor could we demonstrate that the anti-basement membrane antibody, found in the sera of herpes gestationis patients, binds to homologous or autologous placentas and fetal membranes. The importance of an accurate diagnosis and appropriate treatment of this condition is discussed. [less ▲]

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See detailBetamethasone and the rhesus fetus: effect on lung morphometry and connective tissue.
Beck, J. C.; Mitzner, W.; Johnson, J. W. et al

in Pediatric Research (1981), 15(3), 235-40

Pregnant rhesus monkeys (Macaca mulatta) at 67 to 85% of term pregnancy were treated with betamethasone for 3 days and then delivered by cesarean section. These treated fetuses had larger lung volumes (32 ... [more ▼]

Pregnant rhesus monkeys (Macaca mulatta) at 67 to 85% of term pregnancy were treated with betamethasone for 3 days and then delivered by cesarean section. These treated fetuses had larger lung volumes (32.6 +/- 1.8 ml/kg of body weight) compared to gestational age-matched controls (22.9 +/- 3.2 ml/kg of body weight; P less than 0.025) but no alterations in surfactant properties as measured by amniotic fluid L/S ratios, alveolar deflation stability, or lung phosphatidylcholine. These findings suggest that betamethasone effects an increase in fetal lung volume by some method other than alteration in alveolar surfactant concentrations. Results also demonstrated an 11% increase in the collagen to elastin concentration in the treated fetuses as compared to the control animals (P less than 0.01), suggesting alterations in lung connective tissue. Morphometric studies done on the air-fixed inflated lung demonstrated a decrease in the number of alveoli per unit volume of lung among the treated animals (0.95 +/- 0.07 x 10(6)) compared to the control animals (1.19 +/- 0.08 x 10(6); P less than 0.025) and a reduction in the mean surface area of the lungs of the treated animals (506 +/- 10 cm2 per cm3) compared to the control animals (561 +/- 9 cm2 per cm3; P less than 0.005). These findings suggest that at least part of the increased maximal lung volumes is related to increased alveolar distensibility. Together, these pressure volume findings, biochemical studies, and morphometric analyses indicate that a major effect of betamethasone on the rhesus fetal lung is to alter lung connective tissue characteristics. Alterations in lung surfactant appear to be of less functional significance in this rhesus fetal model. The disparity between these findings and other animal studies might be due to differences in species, the preparation, or the method of glucocorticoid administration [less ▲]

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See detailBiosynthesis of type IV and V (alpha A-alpha B) collagens by human placenta.
Foidart, Jean-Michel ULg; Tryggvason, K.; Robey, P. G. et al

in Collagen and Related Research (1981), 1(2), 137-50

The collagenous proteins synthesized by placenta in organ culture were characterized. Types I and III collagen accounted for about two-thirds of the collagenous protein produced by the tissue while type ... [more ▼]

The collagenous proteins synthesized by placenta in organ culture were characterized. Types I and III collagen accounted for about two-thirds of the collagenous protein produced by the tissue while type IV procollagen comprised around 10%. Type IV collagen contained two chains of 185,000 and 175,000 daltons which are genetically distinct from one another as determined by a peptide mapping procedure. The type IV procollagen was identical to that produced by other tissues based on ratios of 3- to 4-hydroxyproline and hydroxyproline to proline, and on the pattern produced upon polyacrylamide gel electrophoresis before and after peptide mapping procedures. About 20% of the collagen resembled type V collagen in the proportions of 3- and 4-hydroxyproline to proline and of hydroxylysine to lysine, in solubility, and in peptide maps. However, it contained disulfide linked chains larger than those found in the type V collagen solubilized by pepsin. Following pepsin treatment, the disulfide bonds were removed and the mobility of the chains of the labeled protein resembled those in type V collagen. It is likely that the disulfide linked protein represents the intact type V collagen molecule. [less ▲]

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See detailChanges in the distribution of type IV collagen, laminin, proteoglycan, and fibronectin during mouse tooth development
Thesleff, I.; Barrach, H. J.; Foidart, Jean-Michel ULg et al

in Developmental Biology (1981), 81(1), 182-92

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See detailDistribution of fibronectin and collagen during mouse limb and palate development.
Silver, M. H.; Foidart, Jean-Michel ULg; Pratt, R. M.

in Differentiation : Research in Biological Diversity (1981), 18(3), 141-9

Indirect immunofluorescence has been used to study the distribution of fibronectin and collagen types I, II, and III in the developing primary and secondary palatal processes and forelimb buds of the ... [more ▼]

Indirect immunofluorescence has been used to study the distribution of fibronectin and collagen types I, II, and III in the developing primary and secondary palatal processes and forelimb buds of the Swiss Webster (NIH) mouse. In the palatal processes fibronectin and types I and III collagen are distributed throughout the mesenchyme. Fibronectin is present in the basement membrane, while types I and III collagen are localized in a linear, discontinuous fashion beneath the basement membrane. Fibronectin is not observed in the epithelium, including the presumptive fusion areas. In the forelimb bud these components show a similar distribution prior to chondrogenesis (early day 11). When chondrogenesis commences (late day 11 or early day 12) fibronectin and, to a lesser degree, types I and III collagen are apparently concentrated in the core mesenchyme, suggesting that fibronectin has a role in initiating chondrogenesis, perhaps by increasing cellular aggregation. Type II collagen is observed only in chondrogenic regions. The codistribution of fibronectin and types I and III collagen supports in vitro studies which indicate that cells use fibronectin to bind to collagen in the matrix. The developing chondrogenic regions appear to lose fibronectin gradually, concomitant with the appearance of type II collagen, suggesting that fibronectin is not involved in the maintenance of functional chondrocytes in their matrices. [less ▲]

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See detailHypertension and the arterial wall
Rorive, Georges ULg; Carlier, P.; Foidart, Jean-Michel ULg et al

in Bulletin et Mémoires de l'Académie Royale de Médecine de Belgique (1981), 136(4), 237-53

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See detailCollagens and non collagenous proteins in the human eye. I. Corneal stroma in vivo and keratocyte production in vitro.
Benezra, D.; Foidart, Jean-Michel ULg

in Current eye Research (1981), 1(2), 101-10

Human corneal stroma in situ and keratocyte activity in vitro were studied by the indirect immunofluorescent technique using highly purified antibodies to the various types of collagens, fibronectin and ... [more ▼]

Human corneal stroma in situ and keratocyte activity in vitro were studied by the indirect immunofluorescent technique using highly purified antibodies to the various types of collagens, fibronectin and laminin. Studying the localization of the various collagens in situ, it was observed that only type I collagen is present in the human corneal stroma. No positive immunofluorescence is obtained for type II or type III collagen. With type IV collagen, a bright immunofluorescence is observed at the level of Bowman's and Descemet's membranes. However, in vitro, the keratocyte cultures demonstrated the production of both type I and III collagens. No evidence for the production of type II or IV collagens was observed. Along with the collagens, human keratocytes in vitro also produced fibronectin. As for the non collagenous components of basement membrane (laminin), although a positive immunofluorescence was obtained the involvement of other cell-membrane glycoproteins in this reaction is not excluded. The possibility that a deregulation of type III collagen synthesis in vivo might be occurring also during certain pathologies and in corneal wound healing is postulated. [less ▲]

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See detailTissue culture of normal rat glomeruli. Basement membrane biosynthesis by homogeneous epithelial and mesangial cell lines.
Foidart, J. B.; Dubois, C. H.; Foidart, Jean-Michel ULg et al

in International Journal of Biochemistry (The) (1980), 12(1-2), 197-202

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See detailAn axial periodic fibrillar arrangement of antigenic determinants for fibronectin and procollagen on ascorbate treated human fibroblasts.
Furcht, L. T.; Wendelschafer-Crabb, G.; Mosher, D. F. et al

in Journal of Supramolecular Structure (1980), 13(1), 15-33

Fibronectin and collagens are major constituents of the cell matrix of fibroblasts. Fibronectin is a 220,000 dalton glycoprotein that mediates a variety of adhesive functions of cells examined in vitro ... [more ▼]

Fibronectin and collagens are major constituents of the cell matrix of fibroblasts. Fibronectin is a 220,000 dalton glycoprotein that mediates a variety of adhesive functions of cells examined in vitro. Fibronectin is secreted in a soluble form and interacts with collagen to form extracellular filaments. Fibronectin and procollagen type I were localized using the peroxidase anti-peroxidase method. Under standard culture conditions, fibronectin and procollagen were localized to non-periodic 10 nm extracellular fibrils, the cell membrane and plasma membrane vesicles. Ascorbate treatment of cells leads to a new larger fibril with a diameter of approximately 40 nm. Antibodies to fibronectin and procollagen I react to these native collagen fibrils with an axial periodicity of approximately 70 nm. Fibronectin is clearly associated with native collagen fibrils produced by ascorbate treated cells and there is an asymetric distribution or segregation of fibronectin on these collagen fibrils with a 70 nm axial repeat. [less ▲]

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See detailAttachment to collagen by isolated hepatocytes from rats with induced hepatic fibrosis.
Berman, M. D.; Waggoner, J. G.; Foidart, Jean-Michel ULg et al

in Journal of Laboratory & Clinical Medicine (1980), 95(5), 660-71

The attachment to and synthesis of collagen by hepatocytes isolated from rats with and without hepatic fibrosis were studied. Attachment of normal hepatocytes was enhanced fourfold in the presence of ... [more ▼]

The attachment to and synthesis of collagen by hepatocytes isolated from rats with and without hepatic fibrosis were studied. Attachment of normal hepatocytes was enhanced fourfold in the presence of serum, whereas attachment of hepatocytes from CCl4-treated rats with severely fibrotic livers was enhanced only twofold by serum. Fibronectin promoted hepatocyte attachment to collagen to the same degree as serum, whereas serum from which the fibronectin had been removed did not. Thus hepatocytes adhere to collagen via fibronectin, a known adhesion protein for fibroblasts. In the absence of serum or fibronectin, hepatocytes attached best to basement membrane collagen (type IV). This enhanced attachment was abolished by periodate oxidation of the collagen, an observation which suggested that carbohydrate residues are involved in hepatocyte attachment to this collagen. Collagen synthesis was determined after hepatocytes were cultured for 24 hr. No difference was found in the amount of collagen synthesized by cultures of hepatocytes derived from control rats and from rats with hepatic fibrosis. By immunofluorescence, the cell responsible for the synthesis of collagen appeared to have a fibroblastic morphology. [less ▲]

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See detailCollagen, factor VIII antigen, and immunoglobulins in the human aqueous drainage channels.
Rodrigues, M. M.; Katz, S. I.; Foidart, Jean-Michel ULg et al

in Ophthalmology (1980), 87(4), 337-45

Twenty-five trabeculectomy specimens from patients with primary open angle glaucoma and chronic angle closure glaucoma, and 11 age-matched controls were examined by immunofluorescence and immunoperoxidase ... [more ▼]

Twenty-five trabeculectomy specimens from patients with primary open angle glaucoma and chronic angle closure glaucoma, and 11 age-matched controls were examined by immunofluorescence and immunoperoxidase techniques to determine the types of collagen, immunoglobulins, and the presence of factor VIII-related antigen in the human aqueous drainage channels. In the glaucoma cases and in controls, we demonstrated that the electron dense basement membrane-like material in the peripheral portion of the trabecular beams and in the juxtacanalicular meshwork, consists at least in part, of type IV collagen, a noncollagenous protein ("laminin") and fibronectin. Factor VIII-related antigen was demonstrated in conjunctival vessels of the control eyes. Schlemm's canal and the trabecular endothelial cells did not stain for factor VIII-related/antigen in any of the specimens examined. No deposits of IgA, IgM, IgG, and the C3 component of complement were detected in the aqueous drainage channels. [less ▲]

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See detailSome properties of marrow derived adherent cells in tissue culture.
Bentley, S. A.; Foidart, Jean-Michel ULg

in Blood (1980), 56(6), 1006-12

It has previously been shown that monolayer cultures derived adherent cells (MDAC), apparently consisting of fibroblasts, macrophages, epithelioid cells, and fat cells, can support long-term stem cell ... [more ▼]

It has previously been shown that monolayer cultures derived adherent cells (MDAC), apparently consisting of fibroblasts, macrophages, epithelioid cells, and fat cells, can support long-term stem cell proliferation in vitro. In the present study, the hematopoietic support capability of murine MDAC monolayers was confirmed and the cultured cells further characterized with respect to the following properties: esterase I activity, complement (C3) receptors, IgG (Fc) receptors, colony stimulating activity (csa) production, and collagen synthesis. The cultures were also examined immunohistochemically to localize fibronectin, laminin, and collagen synthesis and to identify the collagen subtypes synthesized. MDAC morphology was as described in previous studies, although fat cells were few in number. It was found that MDAC included some cells with esterase I activity and C3 receptors. Fc receptors were not, however, detected, nor did the cultures produce csa, indicating that mononuclear phagocytes were not present. MDAC synthesized collagen types I and III and also fibronectin. Staining for epithelial basement membrane proteins (collagen types IV and V and laminin) was negative. The results indicate that the vast majority of these cultured MDAC were fibroblasts. [less ▲]

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See detailCollagen synthesis in cultures of differentiating neural crest cells
Greenberg, J. H.; Foidart, Jean-Michel ULg; Greene, R. M.

in Cell Differentiation (1980), 9(3), 153-63

Neural crest cells from the cranial region of chick embryos were cultured in the presence of fetal calf serum in which they differentiate into melanocytes or in the presence of horse serum in which they ... [more ▼]

Neural crest cells from the cranial region of chick embryos were cultured in the presence of fetal calf serum in which they differentiate into melanocytes or in the presence of horse serum in which they differentiate into neuron-like cells. Undifferentiated cultures, as well as pigmented and neuronal cultures, incorporated [14C]proline into types I and III collagen and into non-collagenous proteins. When cells differentiated into melanocytes, the ratio of collagen to non-collagenous protein did not change. In contrast, in cultures where a portion of the cells differentiated into neuron-like cells, the ratio of collagen to non-collagenous protein was reduced. Indirect immunofluorescence studies using specific antibodies against collagen or procollagen types I, II, III, and IV demonstrated that undifferentiated neural crest cells, melanocytes and neuron-like cells stained only with antibody to type III procollagen, while fibroblastic cells present in some cultures stained only with antibody to type I procollagen. Our results demonstrate that although the types of collagen synthesized by neural crest cells do not change with time in culture, the relative amounts of collagen may reflect the pathway of differentiation of the cells. [less ▲]

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See detailModifications of vascular reactivity. 1. Structural alterations of the utero-placental arteries
Foidart, Jean-Michel ULg; Rorive, G.; Lambotte, R.

in Journal de Gynécologie, Obstétrique et Biologie de la Reproduction (1980), 9(1), 48-9

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See detailHyperplasia of rat arteries smooth muscle cells associated with development and reversal of renal hypertension.
Rorive, G. L.; Carlier, P. J.; Foidart, Jean-Michel ULg

in Clinical Science (1980), 59(suppl 6), 335-338

1. Renal hypertension produces a marked and rapidly detectable hypertrophy of the rat aorta, due to smooth muscle cell hyperplasia and connective tissue deposition. 2. As we described previously for ... [more ▼]

1. Renal hypertension produces a marked and rapidly detectable hypertrophy of the rat aorta, due to smooth muscle cell hyperplasia and connective tissue deposition. 2. As we described previously for collagen synthesis, cell hyperplasia is a very early event which reaches a maximum at a time when the blood pressure is far from its highest level, and thereafter progressively decreases. 3. Reserpine prevents the vascular wall changes on the arterial as well as the venous side of the circulation. On the other hand, captopril although effective in preventing the blood pressure rise does not suppress the hyperplastic response. 4. The arterial hypertensive disease appears to be reversible, when renal ischaemia is corrected. The smooth muscle cell hyperplasia is, however, only partly and slowly reversible. 5. These data suggest that blood pressure is not the only determinant of the vascular wall response, and that the effect of a drug on the blood pressure does nt necessarily predict the vascular wall response. [less ▲]

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