Immunochemical Characterization of the Hyaluronic Acid‐Hyaluronectin Interaction

Delpech, Bertrand

doi:10.1111/j.1471-4159.1982.tb05338.x

Cited by 36 publications

(4 citation statements)

References 13 publications

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“…An antiserum against an extracellular matrix glycoprotein called hyaluronectin outlined approximately 10% of the neurons in a number of rat brain regions, including the cerebral cortex (Delpech et al, 1982). Hyaluronectin from human brain was composed of 2 forms with molecular weights of 66,000 and of 100,000, as determined by gel-permeation chromatography (Delpech, 1982). An antibody raised against cat spinal cord, Cat30 1, preferentially labeled subpopulations of neurons in area 17 of the cat and monkey, as well as subpopulations in a variety of other CNS regions.…”

Section: Discussionmentioning

confidence: 99%

Molecular markers of neuronal subpopulations in layers 4, 5, and 6 of cat primary visual cortex

Arimatsu¹,

Naegele²,

Barnstable³

1987

J. Neurosci.

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Cat primary visual cortex has been used as an immunogen to produce monoclonal antibodies that detect subpopulations of neurons. When tested by immunofluorescence on tissue sections of areas 17 and 18, 2 of these antibodies, VC1.1 and VC5.1, outlined a rare subpopulation of neurons located mainly in layer 4 but also in layers 5 and 6. Double-labeling immunofluorescence experiments in area 17 revealed that all VC1.1-reactive cells were also VC5.1-reactive and 83% of VC5.1-reactive cells were VC1.1-reactive, suggesting that the antibodies were reacting with the same subpopulation of cells. Both antibodies labeled similar or identical subpopulations of cells in other areas of the cat CNS, including the superior colliculus, parts of hippocampus, cerebellar deep nuclei, and rostral spinal cord. Neither antibody labeled cell bodies in the lateral geniculate nucleus. In the retina, VC1.1 labeled cell bodies and processes of some horizontal and amacrine cells, whereas VC5.1 labeled only ganglion cell axons. In the cerebellar cortex, the most prominent labeling of VC1.1 was of Purkinje cells, whereas that of VC5.1 was of Lugaro cells. Immunoblotting analyses of cat cortical homogenates demonstrated that VC1.1 recognized a major polypeptide band of Mr 95,000-105,000 and additional bands of Mr 145,000 and Mr 170,000. VC5.1 recognized bands of Mr 97,000 and Mr 150,000. Subcellular fractionation and extraction studies showed that the VC1.1 antigens were integral membrane proteins preferentially located in a synaptosomal plasma membrane fraction. The VC5.1 antigens were preferentially located in a soluble cytoplasmic or extracellular fraction. The results indicate that antibodies VC1.1 and VC5.1 recognize unique epitopes in the cat CNS and define a previously unrecognized subpopulation of cells in cat visual cortex.

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Section: Discussionmentioning

confidence: 99%

Molecular markers of neuronal subpopulations in layers 4, 5, and 6 of cat primary visual cortex

Arimatsu¹,

Naegele²,

Barnstable³

1987

J. Neurosci.

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“…Purified HA from human umbilical cord and hyaluronidase from bovine testes were obtained from Sigma (St. Louis, MO, USA). Sheep brain HN was prepared as previously described [12, 15]. Briefly, a sheep brain was homogenized in 0.2 M glycine HCl pH 2.2.…”

Section: Methodsmentioning

confidence: 99%

Hyaluronectin blocks the stimulatory effect of hyaluronan‐derived fragments on endothelial cells during angiogenesis in vitro

et al. 1997

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Hyaluronic acid (HA) is a glycosaminoglycan of the extracellular matrix. Its fragmentation by the hyaluronidase, secreted by tumor cells, facilitates tumor invasion and the HA degradation products generated stimulate angiogenesis. We report here that the HA-binding protein hyaluronectin (HN) inhibits the stimulatory effect of HA-derived fragments on the proliferation and migration of endothelial cells in vitro, and hampers the organization of endothelial cells into capillary-like structures. Since HN strongly inhibits endothelial cell adhesion to immobilized HA, it is postulated that HN acts by impairing the binding to endothelial cells of HA fragments generated by hyaluronidase, thereby neutralizing the effect of HA degradation products on angiogenesis. Our results reveal a new mechanism by which the angiogenesis induced by HA fragments is modulated by HN.

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“…Hyaluronectin was isolated from human brain as reported (9,15). Samples of cerebral hemispheres were obtained within [4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] NaDodSO4/PAGE was run as reported (18) in 8% gels with 0.1% NaDodSO4. Samples were reduced with dithiothreitol.…”

Section: Methodsmentioning

confidence: 99%

Brain-specific hyaluronate-binding protein: an immunohistological study with monoclonal antibodies of human and bovine central nervous system.

Bignami¹,

Dahl²

1986

Proc. Natl. Acad. Sci. U.S.A.

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Hyaluronectin is a protein isolated from acid extracts of human brain by affinity chromatography on immobilized hyaluronate. With polyclonal antibodies, it was immunohistologically localized in the rat at the nodes of Ranvier of central and peripheral myelinated fibers and in mesenchymal tissues. Compared to adult rat, hyaluronectinimmunoreactive material was more abundant in embryonal rat brain and mesenchyma. We report a different localization in human and bovine tissues with monoclonal antibodies reacting with human hyaluronectin by NaDodSO4/PAGE and immunoblotting but not staining rat tissues by immunohistology. In human and calf the antigen reacting with hyaluronectin monoclonal antibodies was brain specific, while several peripheral tissues were stained by the polyclonal antibodies. In human and bovine central nervous system monoclonal antibodies stained white matter and tissues formed predominantly by glial fibers (e.g., subependymal glia). In white matter hyaluronectin-immunoreactive material formed a delicate mesh surrounding individual myelinated fibers, a pattern compatible with the distribution of fine astroglial processes in this location. Gray matter did not stain with monoclonal antibodies, the granular layer of the cerebellum excepted. The findings suggest that human hyaluronectin is heterogeneous and comprises at least two fractions. The main fraction is a brain-speciflic protein, probably produced by white matter astrocytes. Another fraction cross-reacting with rat is more abundant in embryonal tissues, including mesenchyma and brain.

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Immunochemical Characterization of the Hyaluronic Acid‐Hyaluronectin Interaction

Cited by 36 publications

References 13 publications

Molecular markers of neuronal subpopulations in layers 4, 5, and 6 of cat primary visual cortex

Molecular markers of neuronal subpopulations in layers 4, 5, and 6 of cat primary visual cortex

Hyaluronectin blocks the stimulatory effect of hyaluronan‐derived fragments on endothelial cells during angiogenesis in vitro

Brain-specific hyaluronate-binding protein: an immunohistological study with monoclonal antibodies of human and bovine central nervous system.

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