Synthesis of basement membrane components by differentiated thyroid cells

Wadeleux, P.; Nusgens, Betty; Foidart, Jean‐Michel; Lapière, Charles M.; Winand, René

doi:10.1016/0167-4889(85)90073-4

Cited by 27 publications

(11 citation statements)

References 15 publications

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“…The ability of thyrocytes to synthesize extracellular matrix proteins such as TSP and basement membrane components such as type IV collagen and heparan-sulfate containing proteoglycan was previously evidenced (Wadeleux et al, 1985;Garbi et al, 1988;Prabakaran et al, 1993). In a previous report, we have already shown that TSH increased the synthesis of heparan sulfate associated with the cell layer and the amount of hyaluronic acid in the culture medium whereas TPA increased the synthesis of glycosaminoglycan in the culture medium and had no effect on cell layer-associated glycosaminoglycans (Wegrowski et al, 1989).…”

Section: Discussionmentioning

confidence: 90%

“…Depending on the culture conditions, thyroid epithelial cells can organize themselves either into vesicle or follicle-like structures that mimic the in viva state (Mauchamp et al, 1979a,b;Verrier et al, 1980; entiated pig thyroid cells cultured on poly (L-1ysine)-treated surfaces has been previously demonstrated (Wadeleux et al, 1985;Garbi et al, 1988). Chemical and immunological studies have revealed the presence of type IV collagen and heparan-sulfate containing proteoglycan in thyroid cells differentiated into follicularlike structures (Wadeleux et al, 1984).…”

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confidence: 99%

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Differential expression of thrombospondin, collagen, and thyroglobulin by thyroid‐stimulating hormone and tumor‐promoting phorbol ester in cultured porcine thyroid cells

Bellon

Chaqour

Antonicelli

et al. 1994

Journal Cellular Physiology

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In the present study, we have investigated the potential regulation of thyroglobulin (Tg) and extracellular matrix components synthesis by thyroid-stimulating hormone (TSH) and tetradecanoyl phorbol-13-acetate (TPA) on thyroid cells. Porcine thyroid cells isolated by trypsin-EGTA digestion of thyroid glands were maintained in serum containing medium on poly (L-lysine)-coated dishes. Cells differentiated into follicular or vesicular-like structures were distinguished by their ability to organify Na[125I] and to respond to TSH stimulation. After an incubation of the cells with radiolabeled proline or methionine, two major proteins were identified, p450-480 and p290 (so named because of their molecular masses). Tg (p290) synthesis was demonstrated by the synthesis of [131I]-labeled polypeptides with electrophoretic properties identical to those of authentic Tg molecules. P450-480 resolved to M(r) 190,000 under reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) conditions. It was identified as thrombospondin by its reactivity with a monoclonal anti-human thrombospondin and by peptide sequencing of some of its tryptic fragments that displayed identity to thrombospondin I. Collagen synthesis was demonstrated by the formation of radioactive hydroxyproline and by the synthesis of pepsin-resistant polypeptides ranging from M(rs) 120,000 to 200,000. When the cells were cultured in the presence of 100 nM TPA, the culture medium contents of thrombospondin and collagen were increased by 2.7 and 1.6-fold, respectively, whereas Tg content was decreased by a factor 3.9. In contrast, the acute treatment of control cells with TPA induced a decrease in both Tg and collagen content by factors 3.0 and 1.5, respectively, and an increase in thrombospondin content by a factor 2.5. In the presence of 100 nM TPA, TSH (1 mU/ml) did not counteract the stimulating effect of TPA on extracellular matrix components synthesis. In contrast, when cells were cultured in the presence of TSH alone at concentrations higher than 0.1 mU/ml, collagen and thrombospondin in the medium were decreased by a factor 2.0 and 1.9, respectively, and TSH preferentially activated Tg synthesis. However, no acute response to TSH was observed in cells incubated for 2 days without effectors (control cells). On TSH differentiated cells, TPA decreased both collagen and Tg accumulation by factors 1.2 and 1.8, respectively, whereas it increased the one of thrombospondin by a factor 2. These results, together with the stimulating effect of TPA on TSH mediated cell proliferation, argue for a role of thrombospondin in cell adhesion and migration events within the thyroid epithelium.

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Section: Discussionmentioning

confidence: 90%

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confidence: 99%

Differential expression of thrombospondin, collagen, and thyroglobulin by thyroid‐stimulating hormone and tumor‐promoting phorbol ester in cultured porcine thyroid cells

Bellon

Chaqour

Antonicelli

et al. 1994

Journal Cellular Physiology

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“…Thyrotropin effects have been investigated in primary cultures of thyroid porcine cells. Synthesis of fibronectin (Giraud et al, 1981), type IV collagen (Wadeleux et al, 1985), and the total fraction of glycosaminoglycans (Giraud and Bouchilloux, 1983) do not seem to be influenced by the presence of thyroid-stimulating hormone (TSH). No data are available for laminin.…”

Section: Discussionmentioning

confidence: 99%

Synthesis of extracellular matrix glycoproteins by a differentiated thyroid epithelial cell line

Garbi

Zurzolo

Bifulco

et al. 1988

Journal Cellular Physiology

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We examined the synthesis of extracellular matrix macromolecules by the differentiated rat thyroid epithelial cell line FRTL-5. As shown by electron microscopy, the extracellular material produced by these cells is deposited at the basolateral surface and focally organized in the form of a basement membrane. Biochemical and biosynthetic studies demonstrated that laminin, type IV collagen, and fibronectin are synthesized and deposited in the culture monolayer. Secretion of fibronectin into the culture medium also occurred. By immunofluorescence we observed some peculiarities in the distribution patterns of the basement membrane glycoproteins; while fibronectin and laminin had an almost superimposable distribution, type IV collagen displayed a rather different pattern. Type IV collagen and laminin localization at sites where extracellular material was detected was confirmed by immuno electronmicroscopy using the protein A-colloidal gold technique. The results indicate that under appropriate culture conditions the differentiated thyroid epithelial cell line FRTL-5 synthesizes, secretes and organizes an extracellular matrix where some basement membrane glycoproteins are present.

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“…So far, much less but nevertheless fascinating research has been done on the structure and metabolism of ECM of thyroid tissue (Garbi & Wollman 1982, Alquier et al 1983, Garbi et al 1984, Wadeleux et al 1985, Demeure et al 1992, Prabakaran et al 1993, Vitale et al 1993, 1994, Andre et al 1994, Lemansky et al 1994, Tognella et al 1995, Arvan et al 1997, Bürgi-Saville et al 1997, 1998. Ultrastructural studies indicate that BM formation or maintenance can be achieved in cultures of thyroid cells (Alquier et al 1983, Garbi & Wollman 1982, Garbi et al 1988.…”

Section: Introductionmentioning

confidence: 99%

“…Ultrastructural studies indicate that BM formation or maintenance can be achieved in cultures of thyroid cells (Alquier et al 1983, Garbi & Wollman 1982, Garbi et al 1988. Cultured porcine cells have been shown to synthesize type I, II and IV collagens as well as a heparan sulfate glycosaminoglycan (Wadeleux et al 1985) and also a laminin variant containing an 2-chain (merosin) (Andre et al 1994). Synthesis of laminin, CoIV and fibronectin has been demonstrated in the thyroid epithelial cell line FRTL5 (Ambesi-Impiombato et al 1980, Ambesi-Impiombato & Perrild 1989 and also the deposition of the extracellular material at the basolateral surface of the cells and its organization into a BM (Garbi et al 1988).…”

Section: Introductionmentioning

confidence: 99%

Follicle-forming cat thyroid cell lines synthesizing extracellular matrix and basal membrane components: a new tool for the study of thyroidal morphogenesis

Tognella

Marti²,

Peter³

et al. 1999

Journal of Endocrinology

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Interactions between follicular epithelial cells and extracellular matrix (ECM) are supposed to play an important role in the development and maintenance of thyroid tissue architecture. In the present study we have therefore investigated the synthesis of ECM components by a feline thyroid cell line which is able to form follicle-like structures in vitro, and also in v-ras-transfected and controltransfected sublines. Transfections were performed by lipofection with pZSR (viral Harvey ras gene; neo) and pSV2-neo (control, neo only) plasmids. We have adapted a semisolid culture system composed exclusively of polymerized alginate and therefore devoid of ECM components. Feline cells embedded in alginate gels as single cells and cultured for up to 90 days formed cell clusters within 10 days. Follicle-like structures were formed in the original cell lines and also in the v-ras-and controltransfected cells. Differences in proliferation rates were observed, the v-ras-transfected cells growing up to two to three times faster than the non-transfected cells. Immunostaining was done using rabbit first antibodies directed against mouse collagen IV, human fibronectin, laminin (tumor Engelbreth-Holm-Swarm laminin), perlecan and other ECM components. For comparison, immunostaining was also performed on cryosections of nodular goiters of six hyperthyroid cats. The cell lines and their transfected clones stained strongly positive for collagen IV and fibronectin, and positively but less strongly for laminin and perlecan. The cat goiter tissue stained positively for collagen IV, laminin, perlecan, and fibronectin, and positive staining for S-laminin (containing the 2-chain) was seen in blood vessel walls in this tissue.In conclusion, cat cell lines grow three-dimensionally in alginate beads over several weeks, they form follicle-like structures and express the same ECM components as the native cat goiter tissue. Transfection with v-ras does increase proliferation rate, but does not fundamentally alter formation of follicle-like structures and ECM expression. Alginate gel culture is a promising new tool for the study of follicular morphogenesis, polarity, the expression pattern of ECM components and of the interaction between thyrocytes and ECM. It avoids interference caused by gels composed of ECM components.

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Synthesis of basement membrane components by differentiated thyroid cells

Cited by 27 publications

References 15 publications

Differential expression of thrombospondin, collagen, and thyroglobulin by thyroid‐stimulating hormone and tumor‐promoting phorbol ester in cultured porcine thyroid cells

Differential expression of thrombospondin, collagen, and thyroglobulin by thyroid‐stimulating hormone and tumor‐promoting phorbol ester in cultured porcine thyroid cells

Synthesis of extracellular matrix glycoproteins by a differentiated thyroid epithelial cell line

Follicle-forming cat thyroid cell lines synthesizing extracellular matrix and basal membrane components: a new tool for the study of thyroidal morphogenesis

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