References of "FOIDART, Jean-Michel"
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See detailBasement membrane components and galactosylhydroxylysyl glucosyltransferase in suction blisters of human skin.
Oikarinen, A.; Savolainen, E. R.; Tryggvason, K. et al

in British Journal of Dermatology (1982), 106(3), 257-66

Basement membrane components and collagen biosynthesis were studied in suction blisters in human skin. The basement membrane components were characterized by immunofluorescence using specific antibodies ... [more ▼]

Basement membrane components and collagen biosynthesis were studied in suction blisters in human skin. The basement membrane components were characterized by immunofluorescence using specific antibodies to type IV collagen, laminin and fibronectin, and collagen biosynthesis was studied by assaying galactosylhydroxylysyl glucosylatransferase. In suction blisters, the separation of epidermis and dermis occurred above the lamina lucida, indicating that the basement membrane, composed of lamina lucida and lamina densa, forms a mechanically strong entity. During the regeneration phase of blisters, type Iv collagen and laminin were not observed in the old epidermal blister roof. This indicates that keratinocytes when separated from the underlying basement membrane or connective tissue do not synthesize laminin or type IV collagen. Galactosylhydroxylysyl glucosyltransferase activity could be demonstrated in blister fluid and was about the same as in serum when expressed on the basis of protein in fresh blisters. It increased by 2-3 fold during the repair of blisters, indicating that there was local production of this enzyme. Further studies revealed that pure epidermis contained galactosylyhdroxylysyl glucosyltransferase and hydroxyprolineand this suggests that epidermis may synthesize some collagen type which, according to these studies, is not type IV (basement memebrane) collagen. [less ▲]

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See detailImmunolocalization of laminin, fibronectin, and collagens I to V in the normal and mastotic breast
Gordenne, W.; Foidart, Jean-Michel ULg; Lapière, C. M.

in Journal de Gynécologie, Obstétrique et Biologie de la Reproduction (1982), 11(5), 549-54

Our study tries by immunofluorescence to specify the nature of the connective tissue of the breasts, and especially of the scaffolding of the fatty tissue and the matrix of the lobules and of the ... [more ▼]

Our study tries by immunofluorescence to specify the nature of the connective tissue of the breasts, and especially of the scaffolding of the fatty tissue and the matrix of the lobules and of the lactiferous ducts. In consists of a study of 35 samples which were taken from 13 women whose ages ranged from 40 to 75 and whose breasts were considered on clinical examination and on radiography as normal or abnormal. We have analyzed the distribution of anti-collagen types I, III, IV and V and anti-fibronectin and anti-laminin antibodies in certain sites in the breast which were chosen because of the diversity of forms they could take from one woman to another. In each case of the distribution of protein markers seemed to be regular without, as can be found in certain cases of scar or tumour formation, a change in the distribution of the matrix proteins. Therefore, as already suggested by certain histologists, benign abnormal breast conditions (fibrosis) should be considered as simple variations from the normal. This conclusion agrees with classical histological findings. [less ▲]

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See detailDifferential modulation of human chorionic gonadotropin secretion by epidermal growth factor in normal and malignant placental cultures.
Huot, R. I.; Foidart, Jean-Michel ULg; Nardone, R. M. et al

in Journal of Clinical Endocrinology and Metabolism (1981), 53(5), 1059-63

The ability of epidermal growth factor (EGF) to modulate the secretion of human chorionic gonadotropin (hCG) in both normal and malignant placental cells was compared. Receptors for EGF were present on ... [more ▼]

The ability of epidermal growth factor (EGF) to modulate the secretion of human chorionic gonadotropin (hCG) in both normal and malignant placental cells was compared. Receptors for EGF were present on the JAr line of choriocarcinoma cells and were localized to the trophoblast cells of normal placental organ cultures as detected by immunofluorescence. Despite the presence of EGF receptors, the normal placenta did not respond to EGF by significantly increasing its levels of hCG production. The JAr line of choriocarcinoma exhibited a 2-fold increase in hCG secretion after the addition of EGF. EGF stimulated growth in the JAr cells, as measured by the protein content of the cultures, but did not elevate the incorporation of [methyl-3H]thymidine in either the JAr cells or placental organ cultures. [less ▲]

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See detailSpecificity of antibodies to heterologous glomerular and tubular basement membranes in various strains of mice with different H-2 types.
Moulonguet-Doleris, D.; Erard, D.; Auffredou, M. T. et al

in Clinical & Experimental Immunology (1981), 46(1), 35-43

C3H, CBA (H-2k) and NZB (H-2d) mice were immunized with dog insoluble glomerular (GBM) or tubular basement membrane (TBM). The titre of circulating antibodies was sequentially determined and their ... [more ▼]

C3H, CBA (H-2k) and NZB (H-2d) mice were immunized with dog insoluble glomerular (GBM) or tubular basement membrane (TBM). The titre of circulating antibodies was sequentially determined and their specificity was analysed using various soluble antigenic fractions. Glomerular and tubular deposits were studied on serial biopsies by direct immunofluorescence. After elution from whole kidneys, IgG fixation on normal mouse kidney sections was analysed by indirect immunofluorescence. After immunization with insoluble GBM, animals from all three strains develop antibodies mainly directed against collagenous antigenic determinants shared by GBM and TBM. After immunization with insoluble TBM, the antibodies are directed in NZB mice against non-collagenous TBM-specific determinants, in C3H mice against collagenous determinants and in CBA mice against both types of antigenic determinants. Thus the ability to respond to the various antigens of GBM and TBM is genetically determined and does not depend only on the major histocompatibility complex. [less ▲]

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See detailCultured human bronchial epithelial cells: blood group antigens, keratin, collagens, and fibronectin
Stoner, G. D.; Katoh, Y.; Foidart, Jean-Michel ULg et al

in In Vitro (1981), 17(7), 577-87

Immunofluorescence and immunoperoxidase methods were used to identify constituents and products of cultured human bronchial epithelial cells and fibroblasts. Epithelial cells, but not fibroblasts, from ... [more ▼]

Immunofluorescence and immunoperoxidase methods were used to identify constituents and products of cultured human bronchial epithelial cells and fibroblasts. Epithelial cells, but not fibroblasts, from patients with blood Types A or B reacted to the respective antisera to either the A or B blood group antigens. However, neither the epithelial cells nor the fibroblasts from patients with blood type O[H] reacted with the anti-H antisera. Epithelial cells in primary culture reacted with antibody to prekeratin proteins from human stratum corneum and fibroblasts did not react. Moreover, keratin filaments were assembled in vitro from proteins isolated from the epithelial cells. These immunological and biochemical data support previous morphological observations that human bronchial epithelial cells in primary culture shift progressively from a mucociliary epithelium to a keratinizing epithelium. Epithelial cells and fibroblasts could also be identified by their reactivity to anti-collagen antibodies. Fibroblasts reacted strongly with antibodies to Types I and III collagens and epithelial cells did not. On the other hand, epithelial cells reacted weakly with antibodies to Type IV collagen and fibroblasts were completely negative. Both epithelial cells and fibroblasts reacted with antibody to fibronectin; however, the distribution of fibronectin differed in the two cell types. In epithelial cells, fibronectin was restricted to the cell surface, whereas in fibroblasts it was found on the cell surface and in the extracellular matrix where fibrils of fibronectin were both cell associated and deposited on the surface of the dish where the fibroblasts had migrated. [less ▲]

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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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