Deposition of fibronectin and laminin in the basement membrane of the rat parietal yolk sac: immunohistochemical and biosynthetic studies.

Amenta, Peter S.; Clark, Charles C.; Martínez-Hernández, Antonio

doi:10.1083/jcb.96.1.104

Cited by 65 publications

(24 citation statements)

References 34 publications

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“…Interestingly, the transcription of laminin is severely reduced throughout the vertebral fusion process, and any possible anchoring might have been weakened. In zebrafish and mice, laminin1ß 0-mutants have a disrupted formation of the basal lamina, which seems to result in the disorganization of both the notochordal sheath and elastic membrane (Miner et al 2004;Smyth et al 1999;Amenta et al 1983;Hogan et al 1980). Furthermore, if Perlecan is not expressed in zebrafish, the basement membrane around the notochord fails to form, and notochordal cells fail to differentiate (Parsons et al 2002).…”

Section: Discussionmentioning

confidence: 95%

Remodeling of the notochord during development of vertebral fusions in Atlantic salmon (Salmo salar)

et al. 2010

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Histological characterization of spinal fusions in Atlantic salmon (Salmo salar) has demonstrated shape alterations of vertebral body endplates, a reduced intervertebral space, and replacement of intervertebral cells by ectopic bone. However, the significance of the notochord during the fusion process has not been addressed. We have therefore investigated structural and cellular events in the notochord during the development of vertebral fusions. In order to induce vertebral fusions, Atlantic salmon were exposed to elevated temperatures from fertilization until they attained a size of 15g. Based on results from radiography, intermediate and terminal stages of the fusion process were investigated by immunohistochemistry and real-time quantitative polymerase chain reaction. Examination of structural extracellular matrix proteins such as Perlecan, Aggrecan, Elastin, and Laminin revealed reduced activity and reorganization at early stages in the pathology. Staining for elastic fibers visualized a thinner elastic membrane surrounding the notochord of developing fusions, and immunohistochemistry for Perlecan showed that the notochordal sheath was stretched during fusion. These findings in the outer notochord correlated with the loss of Aggrecan- and Substance-P-positive signals and the further loss of vacuoles from the chordocytes in the central notochord. At more progressed stages of fusion, chordocytes condensed, and the expression of Aggrecan and Substance P reappeared. The hyperdense regions seem to be of importance for the formation of notochordal tissue into bone. Thus, the remodeling of notochord integrity by reduced elasticity, structural alterations, and cellular changes is probably involved in the development of vertebral fusions.

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Section: Discussionmentioning

confidence: 95%

Remodeling of the notochord during development of vertebral fusions in Atlantic salmon (Salmo salar)

et al. 2010

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“…On the other hand, laminin has been noted in the lamina lucida of the epidermal basal lamina , or on the side facing yolk sac cells (i.e. endodermal cells lining the yolk) of the Reichert membrane (AMENTA et al, 1983). These studies indicate that laminin might mediate the attachment of epithelial as well as endothelial cells to the basal laminae.…”

Section: Lamininmentioning

confidence: 85%

“…It has been noticed that macromolecules, including laminin, fibronectin and heparan sulfate proteoglycan, are constituents of the basement membranes of various tissues (LINDER et al, 1978;STENMAN and VAHERI, 1978;TIMPL et al, 1979;MADRI et al, 1980;COURTOY et al, 1982;LAURIE et al, 1982;ODERMATT et al, 1982;SANES, 1982;WARTIOVAARA and LEIVo., 1982;AMENTA et al, 1983;GULATI et al, 1983). It is thought that laminin is involved in the attachment of epithelial cells to the basement membrane (TERRANOVA et al, 1980) or of carcinoma cells to the culturing substrate (VLODAVSKY and GOSPODAROwICz, 1981).…”

Section: Discussionmentioning

confidence: 99%

The localization of laminin and fibronectin on the Schwann cell basal lamina.

Tohyama

Idé

1984

Arch. Histol. Jap., Arch. Histol. Jpn

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Summary.The localization of laminin and fibronectin was examined on the basal laminae of Schwann cells. Basal laminae from sciatic nerves were isolated by sonication, and the localization of laminin and fibronectin on such isolated basal laminae was studied by immunoferritin histochemistry.Laminin was localized mainly on the cellular side (i.e. the side originally facing the Schwann cell plasma membrane) of the basal laminae.On the other hand, fibronectin was found to be present as aggregates only on the interstitial side (i.e., the side originally facing the endoneurial connective tissue) of the basal laminae.Thus, the locations of laminin and fibronectin were distinctly different. It is presumed that laminin might be involved in the attachment of axons and Schwann cells to the basal laminae, while fibronectin mediates the adhesion of the basal laminae to connective tissue elements, including the collagen fibrils.These findings are discussed from a standpoint of nerve regeneration through the basal laminae scaffolds of Schwann cells.Schwann cells are surrounded by basement membranes.As the pathways of their elongation regenerating axons utilize the Bungner's bands which are formed by Schwann cell processes with the basement membranes after denervation.It has been demonstrated that Schwann cells in grafted nerves, which have been killed by repetitive freezing and thawing, are phagocytized by macrophages, leaving the basement membranes, or more exactly, the basal laminae in a tube or scaffold, and that regenerating nerves always extend through such basal lamina scaffolds (IDE, 1983;IDE et al., 1983). This fact suggests that unlike the outer surface, the inner or adluminal surface of the basal lamina scaffolds has some particular constituents favorable to the attachment of axons and Schwann cells to the basal laminae.The basement membrane of Schwann cells, as that of epithelial and muscle cells, can be divided into three layers: the basal lamina, the lamina lucida and the reticular layer (lamina) (KEFALIDES et al., 1979). The basal lamina is the electron dense region which corresponds to the lamina densa of the glomerular basement membrane, the lamina lucida is in contact with the cell plasma membranes, and the reticular lamina faces the connective tissues. The glomerular basement membrane, which also consists of three layers, i.e. the lamina densa, the lamina rara interna and the externa, differs from that of other tissues in being devoid of reticular lamina having originated by the fusion of two basement membranes of different tissues belonging to the endothelium and the epitelium (FARQUHAR,1981).

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“…This was rather surprising, especially since, in the mouse, fibronectin is present in Reichert's membrane at the egg cylinder stage (Wartiovaara et al, 1979). It has, however, been suggested that fibronectin in Reichert's membrane is derived from the maternal circulation and not from the embryo (Amenta et al, 1983).…”

Section: Organization Of Fibronectin Fibrils In the Developing Blastomentioning

confidence: 94%

Basement membrane and fibronectin matrix are distinct entities in the developing mouse blastocyst

Þorsteinsdóttir

1992

Anat. Rec.

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Immunocytochemical techniques were used to study the distribution of fibronectin, type IV collagen (collagen-IV), and laminin in four different stages of mouse blastocyst development. Immunoreactivity for collagen-IV and laminin is present in a granular pattern inside the inner cell mass (ICM) cells in stage 1 blastocysts, while these blastocysts are negative for fibronectin. Fibronectin immunoreactivity appears extracellularly under the trophectoderm (TE) in stage 2 blastocysts, in the form of homogeneously distributed dots, and/or fibrils located preferentially close to cell boundaries. It is followed by the appearance of both collagen-IV and laminin immunoreactivity in patches on the basal side of the TE in stage 3 blastocysts. These patches are initially localized under the central region of TE cells, thus in a location clearly different from that of fibronectin-positive fibrils. As development proceeds the collagen-IV- and laminin-positive patches become larger, covering, by stage 4, an extensive portion of the inner lining of the blastocoel. Fibronectin-positive material is still present in a fibrillar form in stage 3 blastocysts, but is generally reduced to thin strands by stage 4. These results indicate that fibronectin is independent of the mouse blastocyst basement membrane, but may play a transient role in cell adhesion during its deposition. In addition, the results suggest that the ICM plays a major role in the production of collagen-IV and laminin, while the basal surface of TE cells is the primary site of basement membrane assembly.

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Deposition of fibronectin and laminin in the basement membrane of the rat parietal yolk sac: immunohistochemical and biosynthetic studies.

Cited by 65 publications

References 34 publications

Remodeling of the notochord during development of vertebral fusions in Atlantic salmon (Salmo salar)

Remodeling of the notochord during development of vertebral fusions in Atlantic salmon (Salmo salar)

The localization of laminin and fibronectin on the Schwann cell basal lamina.

Basement membrane and fibronectin matrix are distinct entities in the developing mouse blastocyst

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