References of "Laboratory Investigation : Journal of Technical Methods & Pathology"
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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 detailThe immunohistology of glomerular antigens. V. The collagenous antigens of the glomerulus
Scheinman, J. L.; Foidart, Jean-Michel ULg; Michael, A. F.

in Laboratory Investigation : Journal of Technical Methods & Pathology (1980), 43(4), 373-81

Distinct antigenic loci are present within the human glomerulus as demonstrated by high resolution epifluorescent and phase-contrast microscopic techniques using affinity-purified antibody to ... [more ▼]

Distinct antigenic loci are present within the human glomerulus as demonstrated by high resolution epifluorescent and phase-contrast microscopic techniques using affinity-purified antibody to characterized collagens. Type IV mouse tumor procollagen and type V collagen are present within the mesangium and along the endothelial aspect of the glomerular basement membrane, demonstrating antigenic continuity between these two glomerular zones. In contrast, antiserum to type IV collagen from bovine lens capsule reacts with the full thickness of the glomerular basement membrane, as well as in the tubular basement membrane and Bowman's capsule. Types I procollagen and collagen are found within the epithelium; and types III collagen and procollagen are not detected within the glomerulus. The functional role of the multiple distinct "basement membrane" collagens in the glomerular capillary wall is unknown. A complex structure is suggested, especially in the mesangial-subendothelial continuity, and in the differential localization of two forms of type IV collagen within the glomerular basement membrane. [less ▲]

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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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