References of "FOIDART, Jean-Michel"
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See detailExpression of basement membrane zone antigens at the dermo-epibolic junction in organ cultures of human skin.
Hintner, H.; Fritsch, P. O.; Foidart, Jean-Michel ULg et al

in Journal of Investigative Dermatology (1980), 74(4), 200-4

Using the epithelial outgrowth in organ cultures of human skin ("epiboly") as a model system for basement membrane zone neogenesis, the emergence of various antigenic determinants of the junction zone ... [more ▼]

Using the epithelial outgrowth in organ cultures of human skin ("epiboly") as a model system for basement membrane zone neogenesis, the emergence of various antigenic determinants of the junction zone (bullous pemphigoid antigen, type IV collagen and laminin) was studied and the time sequence of their appearance assessed. All 3 antigens were found at the newly built dermo-epibolic junction; their synthesis, however, followed a distinct time sequence: bullous pemphigoid antigens emerged synchronously with the advancing tip of the migrating epithelium, whereas type IV collagen and to a greater extent, laminin, appeared with considerable delay. At the ultrastructural level, the formation of basal lamina accompanied the emergence of type IV collagen and laminin. [less ▲]

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See detailSynthesis of collagen and fibronectin by glomerular cells in culture
Foidart, Jean-Michel ULg; Foidart, J. B.; Mahieu, P. R.

in Renal Physiology (1980), 3(1-6), 183-92

The biosynthesis of collagen and fibronectin molecules by cultivated glomerular epithelial or mesangial cells was studied at confluency using radioactive proline or lysine as precursors. Collagen ... [more ▼]

The biosynthesis of collagen and fibronectin molecules by cultivated glomerular epithelial or mesangial cells was studied at confluency using radioactive proline or lysine as precursors. Collagen represented 0.5% of the total protein synthesized by the glomerular epithelial cells. About 60% of this collagenous protein were associated to the cell layer, whereas about 40% were secreted into the culture medium. Two major collagenous polypeptides were observed with apparent molecular weights of 185K and 170K, and were identified as two gene products of type IV procollagen. They exhibited ratios of 3- to 4-hydroxyproline, of total hydroxyproline to proline, and of hydroxylysine to lysine characteristic of type IV procollagen. They were degraded by bacterial collagenase. The patterns of peptides obtained after digestion of the 185K and 170K chains of this type IV procollagen with pepsin and V8 protease were identical to those obtained after digestion of type IV procollagen chains purified from a murine tumor (EHS sarcoma). Finally. a purified antibody to type IV collagen specifically immunoprecipitated the collagenous protein produced by the glomerular epithelial cells. By contrast, the mesangial cells synthesized about 5% of collagenous protein. 90% of this collagen were secreted into the cultured medium, whereas about 10% remained associated to the cell layer. Type I, III and IV procollagens were synthesized by the mesangial cells. Fibronectin was found in the medium and cell layer of both epithelial and mesangial cells. Fibronectin molecules were identified by their resistance to bacterial collagenase, their susceptibility to pepsin digestion, and their specific adherence to collagen. It was composed of disulfide-linked peptides of 220K daltons. The data therefore demonstrate that: (a) the glomerular epithelial and mesangial cells synthesize fibronectin molecules and type IV procollagen in vitro; (b) the cultivated mesangial cells also synthesize type I and III collagens. The implications of these findings in certain pathological circumstances, such as diabetes mellitus, are now being investigated. [less ▲]

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See detailIdentification and culture of human bronchial epithelial cells.
Stoner, G. D.; Katoh, Y.; Foidart, Jean-Michel ULg et al

in Methods in Cell Biology (1980), 21A

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See detailUltrastructural localization of fibronectin and laminin in the basement membranes of the murine kidney
Madri, J. A.; Roll, F. J.; Furthmayr, H. et al

in Journal of Cell Biology (1980), 86(2), 682-7

Affinity-purified rabbit antibodies specific for two large noncollagenous gycoproteins--laminin and fibronectin--were used to study the distribution of these proteins in normal murine kidneys ... [more ▼]

Affinity-purified rabbit antibodies specific for two large noncollagenous gycoproteins--laminin and fibronectin--were used to study the distribution of these proteins in normal murine kidneys. Immunofluorescence staining of conventional frozen sections demonstrates fibronectin within mesangial areas of the glomerulus. Laminin is also found in mesangial areas. However, it also appears to be distributed in typical basement membranelike patterns on glomerular and tubular basement membranes and Bowman's capsule. At the ultrastructural level, by labeling 600-800-A thick frozen sections with a three-stage procedure consisting of specific antibodies, biotinyl sheep anti-rabbit IgG, and avidin-ferritin conjugates, fibronectin is present ony in the mesangial matrix and is specifically localized to areas immediately surrounding mesangial cell processes. Laminin, on the other hand, is found uniformly distributed throughout tubular basement membranes, the mesangial matrix, and Bowman's capsule. In glomerular basement membranes, laminin labeling is restricted to the lamina rara interna and adjacent regions of the lamina densa. [less ▲]

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See detailSynthesis of fibronectin, laminin, and several collagens by a liver-derived epithelial line
Foidart, Jean-Michel ULg; Berman, J. J.; Paglia, L. et al

in Laboratory Investigation : Journal of Technical Methods & Pathology (1980), 42(5), 525-32

We have investigated the ability of ARL-6 cells, a cell line derived from rat liver, to synthesize various collagens and two glycoproteins of the extracellular matrix, fibronectin, and laminin. Using ... [more ▼]

We have investigated the ability of ARL-6 cells, a cell line derived from rat liver, to synthesize various collagens and two glycoproteins of the extracellular matrix, fibronectin, and laminin. Using immunofluorescence, we detected types I, II, and IV collagen plus laminin and fibronectin. Antibodies to types I and III collagen and to fibronectin were associated with most cells and showed a similar distribution. Type IV collagen and laminin were found in thin filaments associated with a small proportion of the cells. Chemical studies showed that ARL-6 cells synthesize predominantly types I and III collagens. The level of collagen synthesis was greatly affected by the presence of exogenous fibronectin added to the cells in the media. Cells maintained in fibronectin-free serum synthesized much less collagen. These studies indicate that liver-derived cells can synthesize a variety of connective tissue proteins and that collagen synthesis by these cells is enhanced by the presence of fibronectin. [less ▲]

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See detailDistribution and immunoelectron microscopic localization of laminin, a noncollagenous basement membrane glycoprotein.
Foidart, Jean-Michel ULg; Bere, EW Jr; Yaar, M. et al

in Laboratory Investigation : Journal of Technical Methods & Pathology (1980), 42(3), 336-42

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See detailAscorbate-induced fibroblast cell matrix: reaction of antibodies to procollagen I and III and fibronectin in an axial periodic fashion.
Furcht, L. T.; Wendelschafer-Crabb, G.; Mosher, D. F. et al

in Progress in Clinical & Biological Research (1980), 41

Fibronectin and procollagen types I and III are constituents of the extracellular matrix of human fibroblasts. Ultrastructural immunocytochemistry using the peroxidase anti-peroxidase method showed ... [more ▼]

Fibronectin and procollagen types I and III are constituents of the extracellular matrix of human fibroblasts. Ultrastructural immunocytochemistry using the peroxidase anti-peroxidase method showed fibronectin and procollagen antibodies reacting in continuous fashion on 10 nm diameter extracellular fibrils on human fibroblasts. Intracellular localization showed an intense accumulation of procollagen within cells cultured under routine conditions. This accumulation appeared almost as if there were a blockade in secretion of procollagen under routine culture conditions. Cells treated with ascorbic acid do not have the dense intracellular accumulation of procollagens seen with the apparent blockade of secretion in cells cultured under routine conditions. Ascorbate treated cells also have a more pronounced extracellular accumulation of matrix fibronectin and procollagen constituents. At the electromicroscopic level a new 40 nm diameter fibril is formed after ascorbic acid treatment of human fibroblasts. Antibody to fibronectin and procollagen I and III are seen binding to the 40 nm diameter fibrils in a periodic or stuttered appearance. The fibronectin and procollagen antibodies react with a 70 nm axial repeat along these 40 nm fibrils formed after ascorbate treatment. These studies suggest that under routine culture conditions "precursor" fibrils of fibronectin and procollagen are formed. Ascorbic acid treatment leads to enhanced matrix formation. Ultrastructural studies clearly show antibodies to fibronectin bind to fibronectin on native collagen fibrils formed by human fibroblasts cultured with ascrobic acid. Lastly there is an asymmetric or 70 nm axial periodic distribution of fibronectin along these definitive or mature collagen fibrils formed after ascorbic acid treatment. [less ▲]

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See detailFibronectin presence in native collagen fibrils of human fibroblasts: immunoperoxidase and immunoferritin localization.
Furcht, L. T.; Smith, D.; Wendelschafer-Crabb, G. et al

in Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society (1980), 28(12), 1319-33

Fibronectin is a major constituent of the fibroblast extracellular matrix. Fibronectin binds to collagen, mediates fibroblast adhesion to collagen, and is synthesized and secreted into the medium of ... [more ▼]

Fibronectin is a major constituent of the fibroblast extracellular matrix. Fibronectin binds to collagen, mediates fibroblast adhesion to collagen, and is synthesized and secreted into the medium of cultured fibroblasts. Affinity-purified antibodies to fibronectin and collagen were localized using the peroxidase-antiperoxidase method or with ferritin-coupled secondary antibodies. Using human fibroblasts cultured under routine conditions, fibronectin and procollagen I react in a nonperiodic manner with: 1) approximately 10 nm extracellular fibrils, 2) cell membrane, and 3) membrane-associated vesicles. All fibrils react with both antibodies, suggesting some form of codistribution of fibronectin and collagen in these fibrils. Treatment with ascorbate leads to the development of a larger diameter extracellular fibril, approximately 40 nm in diameter. These large diameter fibrils are clearly collagen fibrils as documented by the procollagen antibody reaction. Importantly, fibronectin is bound to or a constituent of these "native" or cellular made collagen fibrils. Fibronectin and procollagen antibodies localized with the peroxidase-antiperoxidase method have a 70 nm axial repeat of reaction product on ascorbate-treated fibroblasts. Localization of antibodies with ferritin-labeled secondary antibodies is less satisfactory, but supports the basic observations made with the unlabeled antibody enzyme method. This observation rules out any potential criticisms. Although it is more difficult to observe with immunoferritin, there is an indication that antibodies to fibronectin react with an axial periodicity on cellular produced collagen fibrils. [less ▲]

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See detailAssay for radiolabeled type IV collagen in the presence of other proteins using a specific collagenase.
Garbisa, S.; Tryggvason, K.; Foidart, Jean-Michel ULg et al

in Analytical Biochemistry (1980), 107(1), 187-92

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See detailSynthesis of collagen by rat liver epithelial cultures
Berman, J. J.; Foidart, Jean-Michel ULg

in Annals of the New York Academy of Sciences (1980), 349

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See detailThe epidermal cell which selectively adheres to a collagen substrate is the basal cell.
Stanley, J. R.; Foidart, Jean-Michel ULg; Murray, J. C. et al

in Journal of Investigative Dermatology (1980), 74(1), 54-8

In order to determine whether a specific subpopulation of epidermal cells selectively attaches to collagen substrates in vitro, epidermal cell suspensions, obtained by trypsinization of guinea pig skin ... [more ▼]

In order to determine whether a specific subpopulation of epidermal cells selectively attaches to collagen substrates in vitro, epidermal cell suspensions, obtained by trypsinization of guinea pig skin, were incubated on type I or type IV collagen-coated glass cover slips. It was noted, morphologically and by electronic volume measurements, that small round cells, as opposed to the larger angulated flat cells, adhered to the collagen substrates. To further characterize the attached cells, the percentage of basal cells was determined in the attached cell population and in the initial epidermal cell suspension. Basal cells were identified by indirect immunofluorescence in 2 ways: (1) by the presence of pemphigoid antigen and (2) by the absence of upper cytoplasmic antigen, which is present in all keratinocytes except the basal cells. Whereas in the initial guinea pig epidermal cell suspensions about 50% of the cells were basal cells using either of these 2 criteria, 86-97% of the cells which adhered to the collagen substrates were basal cells. Human basal cells, as defined by pemphigoid antigen, also selectively adhered to the collagen substrates. [less ▲]

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See detailThe immunohistology of glomerular antigens. IV. Laminin, a defined noncollagen basement membrane glycoprotein.
Scheinman, J. L.; Foidart, Jean-Michel ULg; Gehron-Robey, P. et al

in Clinical Immunology and Immunopathology (1980), 15(2), 175-89

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See detailLaminin--a glycoprotein from basement membranes.
Timpl, R.; Rhode, H.; Robey, P. G. et al

in Journal of Biological Chemistry (1979), 254(19), 9933-7

We have isolated a large noncollagenous glycoprotein, laminin, from a mouse tumor that produces basement membrane. The protein consists of at least two polypeptide chains (Mr = 220,000 and Mr = 440,000 ... [more ▼]

We have isolated a large noncollagenous glycoprotein, laminin, from a mouse tumor that produces basement membrane. The protein consists of at least two polypeptide chains (Mr = 220,000 and Mr = 440,000) joined to each other by disulfide bonds. Laminin and type IV collagen are major constituents of the tumor. Laminin is distinctly different from fibronectin, another component of basement membranes, in amino acid composition and immunological reactivity. Pepsin digestion of laminin releases a large, cystine-rich fragment which retains most of the antigenicity of the original protein. Immunological studies using purified antibody against laminin show that it is produced by a variety of cultured cells. In addition, these antibodies react with the basement membranes of normal tissues, suggesting that this protein or an immunologically related protein is a constituent of the basement membranes of these tissues. [less ▲]

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See detailReversal by glucocorticoid hormones of the loss of a fibronectin and probollagen matrix around transformed human cells.
Furcht, L. T.; Mosher, D. F.; Wendelschafer-Crabb, G. et al

in Cancer Research (1979), 39(6Pt 1), 2077-83

Confluent cultured human skin fibroblasts had an extracellular fibrillar matrix of fibronectin and procollagen. Human skin fibroblasts transformed by SV40 did not have such a matrix. Treatment of ... [more ▼]

Confluent cultured human skin fibroblasts had an extracellular fibrillar matrix of fibronectin and procollagen. Human skin fibroblasts transformed by SV40 did not have such a matrix. Treatment of transformed fibroblasts with 10(-5) to 10(-8) M dexamethasone and 10(-5) to 10(-7) M cortisol, but not testosterone or progesterone, caused partial restoration of the matrix. Glucocorticoid-treated transformed human fibroblasts can serve as a model for partial reversion toward normal or differentiation of transformed human fibroblasts. [less ▲]

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See detailDexamethasone-induced accumulation of a fibronectin and collagen extracellular matrix in transformed human cells.
Furcht, L. T.; Mosher, D. F.; Wendelschafer-Crabb, G. et al

in Nature (1979), 277(5695), 393-5

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See detailEffects of culture conditions on the synthesis of human chorionic gonadotropin by placental organ cultures.
Huot, R. I.; Foidart, Jean-Michel ULg; Stromberg, K.

in In Vitro (1979), 15(7), 497-502

Culture conditions for maintaining first trimester human placenta in organ culture, which enhance the secretion of human chorionic gonadotropin (hCG), are described. Nutrient medium, oxygen tension and ... [more ▼]

Culture conditions for maintaining first trimester human placenta in organ culture, which enhance the secretion of human chorionic gonadotropin (hCG), are described. Nutrient medium, oxygen tension and Gelfoam support matrix influence the synthesis of hCG by these cultures. Placental tissue remained viable for the duration of experiments (12 days) as judged by the incorporation of tritiated thymidine into DNA and the lack of release of incorporated [125I]iododeoxyuridine. Optimal conditions for hCG synthesis in placental organ culture included an atmosphere of 95% air and 5% Co2 (approximately 20% O2), CMRL 1066 medium containing fetal human or bovine serum, insulin, hydrocortisone and retinal acetate. Multiple pieces of placenta could be cultured in the same dish with an additive effect on hCG secretion. The functional responsiveness of these placental cultures was demonstrated by modulation of hCG synthesis with theophylline and 3'5' dibutyryl cyclic AMP. [less ▲]

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See detailIdentification of micrometastasis of breast carcinomas by presence of basement membrane collagen.
Liotta, L. A.; Foidart, Jean-Michel ULg; Gehron Robey, P. et al

in Lancet (1979), 2(8134), 146-7

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See detailSubtle clues to diagnosis by immunopathology. Relapsing polychondritis.
Foidart, Jean-Michel ULg; Katz, S. I.

in American Journal of Dermatopathology (1979), 1(3), 257-60

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See detailHormonal requirements for basement membrane collagen deposition by cultured rat mammary epithelium.
Liotta, L. A.; Wicha, M. S.; Foidart, Jean-Michel ULg et al

in Laboratory Investigation : Journal of Technical Methods & Pathology (1979), 41(6), 511-8

Alveoli and ducts isolated from virgin rat mammary glands synthesize basement membrane collagen (typeIV) in primary culture. Using purified antibodies to type IV collagen, prominent intracellular and ... [more ▼]

Alveoli and ducts isolated from virgin rat mammary glands synthesize basement membrane collagen (typeIV) in primary culture. Using purified antibodies to type IV collagen, prominent intracellular and extracellular fluorescence is observed in the epithelium. No fluorescence is observed with antibodies to collagen type I and III. From quantitation of the incorporation of [14c]proline-labeled proteins, 1.5 to 2.5 per cent of the newly synthesized proteins are collagen. Type IV collagen from these cultures was biochemically identified on the basis of (1) the high ratio of labeled 3-hydroxyproline to 4-hydroxyproline (1:10), (2) the gel electrophoretic pattern of the collagenase-sensitive proteins precipitated with 1.7 M NaCl, (3)the failure of the collagen to bind to diethylaminoethyl-cellulose, and(4)the immunologic cross-reactivity with mouse tumor type IV is identical with that of type IV collagen from other sources. When the supportive hormones, insulin, prolactin, hydrocortisone, progesterone, and estradiol are removed from the cultures, there is a 90 per cent reduction in the amount of [3H]proline recovered in collagen synthesis coincides with only a 30 percentdrop in the growht rate and a 20 per cent drop in total protein synthesis of the sells over the 24-hour period without hormones. Pulse-chase experimout hormones. Pulse-chase experiments revealed an enhanced turnover of collagen following hormone withdrawal. This system may be an in vitro model of collagen turnover in mammary gland in involution. [less ▲]

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