Basal lamina glycoproteins are produced by neuroblastoma cells

Alitalo, Kari; Kurkinen, Markku; Vaheri, Antti; Virtanen, Ismo; Rohde, Heilwig; Timpl, Rupert

doi:10.1038/287465a0

Cited by 65 publications

(26 citation statements)

References 33 publications

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“…Neuroblastoma cells are known to produce both laminin [19] and PA [20], which at least in some cell lines is t-PA (unpublished). Interestingly, cellassociated PA of tumorigenic rat neuroblastoma cells was suppressed by substratum-attached matrix material of nontumorigenic neuroblastoma cells with little or no PA activity 1201.…”

Section: Resultsmentioning

confidence: 99%

Laminin interacts with plasminogen and its tissue‐type activator

Salonen¹,

Zitting

Vaheri³

1984

FEBS Letters

111

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Section: Resultsmentioning

confidence: 99%

Laminin interacts with plasminogen and its tissue‐type activator

Salonen¹,

Zitting

Vaheri³

1984

FEBS Letters

111

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“…The sections were incubated ovemight at +40C with nonral sheep serum diluted 1/30. Laminin antiserum was raised in rabbit against mouse EHS-tumor laminin obtained from Dr. R.Timpl, and its specificity confirmed (Alitalo et al, 1980;Liesi, 1983). The rndbit vimentin antiserum (Hynes and Destree, 1978), mouse antibodies GFAP (Raju et al, 1981), and rabbit anti-fibronectin antiserum (Hedman et al, 1978) were antisera of high specificity.…”

Section: Methodsmentioning

confidence: 99%

Do neurons in the vertebrate CNS migrate on laminin?

Liesi¹

1985

The EMBO Journal

239

135

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In adult rat brain the extracellular matrix glycoprotein, laminiin, is found only in basement membranes, but is transiently expressed by astrocytes after brain injury. Here, I show that lanminin also appears in immature brain cells during CNS development, and that its presence coincides with phases of neuronal migration. In early embryos, laninin is seen throughout the whole thickness of the forniing brain, and is apparently synthesized by the cells, as judged by its intracytoplasmic localization. As development proceeds, intracellular laminin becomes restricted to the periventricular regions while punctate deposits of laminin follow the course of vimentin-positive radial glial fibers. In most brain regions, the adult pattern of laminin expression is achieved by birth. In the post-natal rat cerebellum, however, lamniin is detected in external granule cells, in Purkinje cells, and in punctate deposits along the radial Bergmann glial fibers. By day 24 after birth, when the migration of external granule cells is complete, all laminin immunoreactivity disappears from these structures. The transient expression of laniinin in regions where neurons are migrating raises the possibility that lanin plays a role in neuronal migration during CNS development.

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“…Then the cell layers were rinsed in PBS overnight at +4°C and permeabilized with cold methanol (-20°C) before they were stained for laminin. Rabbit antibodies against laminin were those used previously and their specificity was confirmed (20,21). 1 They were used at a dilution of 1:100 and applied for 1 h at room temperature.…”

Section: Monensin Treatment Of the Culturesmentioning

confidence: 99%

“…It is also produced by mouse neuroblastoma Cells (20), in which its pattern of localization suggests a role for laminin as their adhesion protein) In adult mouse brain, laminin has been found only in connection with blood vessel wails (21), but little is known about the expression of laminin in normal developing cells of neuroectodermal origin. Fibronectin, the other major noncollagenous matrix glycoprotein, important in normal development of several types of cells (22,23), has been demon- Liesi, P. 1983.…”

mentioning

confidence: 99%

Laminin is produced by early rat astrocytes in primary culture.

Liesi¹,

Dahl²,

Vaheri³

1983

The Journal of Cell Biology

364

127

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The production of laminin by early rat astrocytes in primary culture was investigated by double immunoffuorescence staining for laminin and the gliat fibrillary acidic protein (GFAP), a defined astrocyte marker. In early cultures (3 d in vitro; 3 DIV) cytoplasmic laminin was detected in all the GFAP-positive cells which formed the major population (80%) of the nonneuronal cells present in cultures from 20-21-d embryonic, newborn, or 5-d-old rat brains. Monensin treatment (10 #M, 4 h) resulted in accumulation of laminin in the Golgi region, located using labeled wheat germ agglutinin. Laminin started gradually to disappear from the cells with the time in culture, was absent in starshaped, apparently mature astrocytes, but remained as pericellular matrix deposits. The disappearance of cellular laminin was dependent on the age of the animal and the time in culture so that it started earlier in cultures from 5-d-old rat brains (5 DIV) and approximately following the in vivo age difference in cultures from newborn (12 DIV) and embryonic (14 DIV) rat brains.Our results indicate that laminin is a protein of early astrocytes and also deposited by them in primary culture, thus suggesting a role for this glycoprotein in the development of the central nervous system.The development and migration of brain cells have been extensively studied (1-3), and the timing for the appearance of the glial fibriUary acidic protein, a defined astrocyte marker (4-6) both in brain and in primary culture, has been well documented (4,(7)(8)(9).In several studies on primary cultures the development of neurons and glial cells have been shown to closely follow the pattern of the in vivo development (8-13); tissue culture systems may thus serve as experimental models for central development and cell interactions (14,15).Laminin, one of the matrix glycoproteins (16), is present in all basement membranes so far investigated (16-18) and is produced by various epithelial cells in culture (16,19). It is also produced by mouse neuroblastoma Cells (20), in which its pattern of localization suggests a role for laminin as their adhesion protein) In adult mouse brain, laminin has been found only in connection with blood vessel wails (21), but little is known about the expression of laminin in normal developing cells of neuroectodermal origin. Fibronectin, the other major noncollagenous matrix glycoprotein, important in normal development of several types of cells (22, 23), has been demonLiesi, P. 1983. Laminin in cultured mouse C 1300 neuroblastoma cells: immunocytochemical localization by pre-and postembedding electron microscope procedures. J. Histochem. Cytochem. In press. 920 strated to be present in vessel walls in developing and adult rat brain (24). In primary brain cell cultures, fibronectin is thought to be due to mesenchymal cell contamination (25).In the present study, we used primary cultures from early rat brain to study the possible role of laminin for development of central cells of neuroectodermal origin. We demonstrate that lamin...

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Basal lamina glycoproteins are produced by neuroblastoma cells

Cited by 65 publications

References 33 publications

Laminin interacts with plasminogen and its tissue‐type activator

Laminin interacts with plasminogen and its tissue‐type activator

Do neurons in the vertebrate CNS migrate on laminin?

Laminin is produced by early rat astrocytes in primary culture.

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