Structure and orientation of extracellular matrix in developing chick optic tectum

Krayanek, Susan

doi:10.1002/ar.1091970109

Cited by 26 publications

(5 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There has been considerable speculation concerning the possible role of glycosaminoglycans as a component of the extracellular matrix in developing nervous tissue (1,4,6,11,14,17,21,22). It is generally agreed that one of the more likely functions of extracellular glycosaminoglycans, particularly hyaluronic acid, is to provide a readily penetrable matrix through which neuronal migration and differentiation may FIGURE 13 Elution of [3SS]sulfate-labeled proteoglycan from adult rat brain (0-----0) and 3H-labeled proteoglycan from 7-d-old brain (O ..... O) from Sepharose CL-2B (0.9 x 65 cm) using 0.2 M sodium acetate buffer, pH 5.6.3ss and 3H counts per minute were normalized as described in the legend to Fig.…”

Section: Discussionmentioning

confidence: 99%

Immunocytochemical localization of a chondroitin sulfate proteoglycan in nervous tissue. II. Studies in developing brain.

Aquino¹,

Margolis²,

Margolis³

1984

The Journal of Cell Biology

122

View full text Add to dashboard Cite

In contrast to the intracellular (cytoplasmic) localization of chondroitin sulfate proteoglycans in adult brain (Aquino, D. A., R. U. Margolis, and R. K. Margolis, 1984, J. Cell Biol. 99:940-952), immunoelectron microscopic studies in immature (7 d postnatal) rat cerebellum demonstrated almost exclusively extracellular staining in the granule cell and molecular layers. Staining was also extracellular and/or associated with plasma membranes in the region of the presumptive white matter. Axons, which are unmyelinated at this age, generally did not stain, although faint intracellular staining was present in some astrocytes. At 10 and 14 d postnatal there was a significant decrease in extracellular space and staining, and by 21 d distinct cytoplasmic staining of neurons and astrocytes appeared. This intracellular staining further increased by 33 d so as to closely resemble the pattern seen in adult brain. Analyses of the proteoglycans isolated from 7-d-old and adult brain demonstrated that they have essentially identical biochemical compositions, immunochemical reactivity, size, charge, and density. These findings indicate that the antibodies used in this study recognize the same macromolecule in both early postnatal and adult brain, and that the localization of this proteoglycan changes progressively from an extracellular to an intracellular location during brain development.In the preceding report (2) we have demonstrated by immunoelectron microscopy the intracellular (cytoplasmic) localization of a chondroitin sulfate proteoglycan in neurons and astrocytes of adult rat central nervous tissue. Its functional role in this location is still unknown, and although our immunocytochemical findings were not unexpected on the basis of previous biochemical studies of brain glycosaminoglycans, they are nevertheless quite different from the extracellular matrix or cell surface location of proteoglycans in other tissues (8,16,18,19).Since the possibility remained that during brain development this proteoglycan might be involved in extracellular processes associated with neural histogenesis and various types of cell-cell interactions, we also examined its localization in rat cerebellum during the period extending from 1 wk to l mo of postnatal age. These studies demonstrated that in contrast to the cytoplasmic localization observed in adult brain, the chondroitin sulfate proteoglycan is almost exclusively extraceUular in 7-d-old cerebellum, and progressively assumes its final intracellular location in neurons and astrocytes during the succeeding 3 wk. MATERIALS AND METHODSThe immunochemical and immunocytochcmical procedures employed were essentially as described in the preceding paper (2). However, for studies of immature brain (7-33 d postnatal), a two-step fixation procedure was used (3). After perfusion with 0.1 M sodium phosphate buffer (pH 7.4) containing 0.9% NaCl, rats were perfused with 4% freshly prepared formaldehyde and 0.1% glutaraldehyde in sodium phosphate buffer (pH 6.5), followed by the same aldehydes...

show abstract

Section: Discussionmentioning

confidence: 99%

Immunocytochemical localization of a chondroitin sulfate proteoglycan in nervous tissue. II. Studies in developing brain.

Aquino¹,

Margolis²,

Margolis³

1984

The Journal of Cell Biology

122

View full text Add to dashboard Cite

show abstract

“…However, several lines of evidence indicate that matrix components are transiently seen in the developing CNS. First, studies using ruthenium red and other markers of glycosaminoglycans show accumulations of stained, fibrillar, matrixlike material in the extracellular spaces within the developing CNS (Bork et al, 1987;Krayanck, 1980;Nakanishi, 1983). More recently, immunohistochemical studies have revealed the presence of extracellular deposits of laminin, fibronectin, and chondroitin sulfate proteoglycan during brief periods in the brains of embryonic mammals (Aquino et al, 1984b;Chun and Shatz, 1988;Gordon-Weeks et al, 1989;Liesi, 1985b;McLoon et al, 1988;Stewart and Pearlman, 1987).…”

Section: S-laminin Is Produced By Non-neuronal Cells Of the Nervous Smentioning

confidence: 99%

Laminin and s‐laminin are produced and released by astrocytes, schwann cells, and schwannomas in culture

Chiu

Cole

Loera

et al. 1991

Glia

View full text Add to dashboard Cite

Components of the extracellular matrix (ECM) have been implicated in the regulation of neuronal migration, axonal growth, and synaptogenesis. We have examined cultures of glial cells, Schwann cells, and schwannomas for the expression of two components of the ECM, laminin and s-laminin, using immunohistochemical and Western blot techniques. Laminin is a potent promotor of neurite outgrowth in cultures of both central and peripheral neurons, and is present in all ECMs. In contrast, s-laminin (for synaptic laminin), a recently described homolog of laminin, is highly localized at the neuromuscular synaptic cleft (Sanes and Chiu, Cold Spring Harbor Symp. Quant. Biol. 1983;48:667-678; Chiu and Sanes, Dev. Biol. 1984;103:456-467) and shows selective adhesivity for motor neurons (Hunter et al. Cell 1989;59:905-913). While the distribution of these ECM components have been well documented in situ, the sources of these extracellular molecules are unclear. We report that astrocytes cultured in serum-free medium maintain an organized ECM that only bears laminin immunoreactivity; s-laminin appears to be sequestered intracellularly. However, both molecules are found in the astrocyte conditioned medium. Thus, under these growth conditions, astrocytes produce and release laminin and s-laminin, but only incorporate the former into an ECM. In contrast, neither molecule is present in comparable cultures of oligodendrocytes. Although no established ECM is seen in cultures of Schwann cells or schwannomas, laminin and s-laminin immunoreactivity are present within cells and in the conditioned media. These results indicate that certain populations of non-neuronal support cells and cell lines can produce and release both synaptic and extrasynaptic components of the ECM. The assembly of these different molecules into an organized basal lamina may require the presence of additional factors or interaction with neurons.

show abstract

“…Although a matter of controversy for many years, it now seems clear that ECM components are involved in development of the CNS as well (Sanes, 1989;Reichardt and Tomaselli, 199 1). Glycosaminoglycans, defined by labeling with cationic dyes, are present in the cerebral cortex of the mouse (Derer and Nakanishi, 1983;Nakanishi, 1983;Bruckner et al, 1985) and in the chick's optic tectum just ahead of arriving optic nerve axons (Krayanek, 1980). Immunolabeling with antibodies against fibronectin (IN;Hatten et al, 1982;Stewart and Pearlman, 1987;Chun and Shatz, 1988;Stallcup et al, 1989) proteoglycans (Aquino et al, 1984;Margolis and Margolis, 1989;Snow et al, 1990b), hyaluronectin (Delpech and Delpech, 1984;Bignami and Delpech, 1985), laminin (Liesi, 1985;Letoumeau et al, 1988;Liesi and Silver, 1988;McLoon et al, 1988;Hagg et al, 1989), tenascin (Crossin et al, 1989;Steindler et al, 1989), and thrombospondin (O'Shea et al, 1990) has been demonstrated in the developing CNS of the rodent, and extracellular material that has not been characterized with antibody markers is evident with electron microscopy in the cortical subplate and marginal zones (Derer and Nakanishi, 1983;Nakanishi, 1983;Hankin and Silver, 1988).…”

mentioning

confidence: 99%

Changes in the distribution of extracellular matrix components accompany early morphogenetic events of mammalian cortical development

1991

View full text Add to dashboard Cite

As a step in defining the molecular environment for development of the mammalian cerebral cortex, we have used immunohistochemistry to analyze the distribution and remodeling of three major extracellular matrix (ECM) components, fibronectin, chondroitin sulfate proteoglycan (CSPG), and tenascin, during embryonic and early postnatal stages in the mouse. Fibronectin and CSPG are distributed throughout the proliferative zone that initially comprises the thin wall of the telencephalic vesicle, but their distribution changes as newly generated cells form the preplate just beneath the pia. Immunolabeling for CSPG becomes most prominent in the preplate, and fibronectin becomes restricted to that layer. Just after this change occurs, processes of preplate neurons, visualized with antibodies to neurofilaments, become evident within the matrix-rich preplate zone. The association of fibronectin and CSPG with preplate cells persists as cortical plate neurons divide the preplate; both ECM components are now most prominent in the marginal zone and subplate, the layers above and below the cortical plate that are preplate derived. Within the preplate and its derivatives, immunolabeling of fibronectin is punctate and closely associated with radial glial processes, while labeling of CSPG is more intense and diffuse. Labeling of fibronectin and CSPG declines rapidly as the cortical plate begins to differentiate into cortex; labeling for tenascin first appears at this stage in the most mature layers, the marginal zone and subplate, then gradually becomes widespread throughout all of cortex and subcortical white matter. In early postnatal life, tenascin is eliminated from the hollows of the vibrissal barrels in the somatosensory region; it then declines rapidly throughout cortex. The association of both fibronectin and CSPG with preplate cells and the distribution of fibronectin along radial glia during early cortical development suggest that one or both of these transient cell types might produce specific ECM components or induce their local deposition. The spatial and temporal distribution of fibronectin and CSPG suggests a role in defining a destination for migrating neurons that form the cortical plate and in delineating the pathway for early axonal extension. In contrast, the relatively late appearance of tenascin correlates best with the formation of astrocytes and their processes rather than with the establishment of cortical layers or major axonal pathways. These events are well underway before labeling of tenascin is evident.

show abstract

Structure and orientation of extracellular matrix in developing chick optic tectum

Cited by 26 publications

References 40 publications

Immunocytochemical localization of a chondroitin sulfate proteoglycan in nervous tissue. II. Studies in developing brain.

Immunocytochemical localization of a chondroitin sulfate proteoglycan in nervous tissue. II. Studies in developing brain.

Laminin and s‐laminin are produced and released by astrocytes, schwann cells, and schwannomas in culture

Changes in the distribution of extracellular matrix components accompany early morphogenetic events of mammalian cortical development

Contact Info

Product

Resources

About