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On the ultrastructure of hyalin, a cell adhesion protein of the sea urchin embryo extracellular matrix.

Publication ,  Journal Article
Adelson, DL; Alliegro, MC; McClay, DR
Published in: The Journal of cell biology
March 1992

Hyalin is a large (ca. 350 x 10(3) kD by gel electrophoresis) molecule that contributes to the hyalin layer surrounding the sea urchin embryo. In previous work a mAb (McA Tg-HYL), specific for hyalin, was found to inhibit cell-hyalin adhesion and block morphogenesis of whole embryos (Adelson, D. L., and T. D. Humphreys. 1988. Development. 104:391-402). In this report, hyalin ultrastructure was examined via rotary shadowing. Hyalin appeared to be a filamentous molecule approximately 75-nm long with a globular "head" about 12 nm in diameter that tended to form aggregates by associating head to head. Hyalin molecules tended to associate with a distinct high molecular weight globular particle ("core"). In fractions containing the core particle often more than one hyalin molecule were seen to be associated with the core. The core particle maintained a tenacious association with hyalin throughout purification procedures. The site(s) of McA Tg-HYL binding to the hyalin molecule were visualized by decorating purified hyalin with the antibody and then rotary shadowing the complex. In these experiments, McA Tg-HYL attached to the hyalin filament near the head region in a pattern suggesting that more than one antibody binding site exists on the hyalin filament. From the ultrastructural data and from the cell adhesion data presented earlier we conclude that hyalin is a filamentous molecule that binds to other hyalin molecules and contains multiple cell binding sites. Attempts were made to demonstrate the existence of lower molecular weight hyalin precursors. Whilst no such precursors could be identified by immunoprecipitation of in vivo labeled embryo lysates, immunoprecipitation of in vitro translation products suggested such precursors (ca 40 x 10(3) kD) might exist.

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Published In

The Journal of cell biology

DOI

EISSN

1540-8140

ISSN

0021-9525

Publication Date

March 1992

Volume

116

Issue

5

Start / End Page

1283 / 1289

Related Subject Headings

  • Sea Urchins
  • Morphogenesis
  • Molecular Structure
  • Hyalin
  • Fractional Precipitation
  • Developmental Biology
  • Cell-Free System
  • Cell Adhesion Molecules
  • Blotting, Southern
  • Animals
 

Citation

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Adelson, D. L., Alliegro, M. C., & McClay, D. R. (1992). On the ultrastructure of hyalin, a cell adhesion protein of the sea urchin embryo extracellular matrix. The Journal of Cell Biology, 116(5), 1283–1289. https://doi.org/10.1083/jcb.116.5.1283
Adelson, D. L., M. C. Alliegro, and D. R. McClay. “On the ultrastructure of hyalin, a cell adhesion protein of the sea urchin embryo extracellular matrix.The Journal of Cell Biology 116, no. 5 (March 1992): 1283–89. https://doi.org/10.1083/jcb.116.5.1283.
Adelson DL, Alliegro MC, McClay DR. On the ultrastructure of hyalin, a cell adhesion protein of the sea urchin embryo extracellular matrix. The Journal of cell biology. 1992 Mar;116(5):1283–9.
Adelson, D. L., et al. “On the ultrastructure of hyalin, a cell adhesion protein of the sea urchin embryo extracellular matrix.The Journal of Cell Biology, vol. 116, no. 5, Mar. 1992, pp. 1283–89. Epmc, doi:10.1083/jcb.116.5.1283.
Adelson DL, Alliegro MC, McClay DR. On the ultrastructure of hyalin, a cell adhesion protein of the sea urchin embryo extracellular matrix. The Journal of cell biology. 1992 Mar;116(5):1283–1289.

Published In

The Journal of cell biology

DOI

EISSN

1540-8140

ISSN

0021-9525

Publication Date

March 1992

Volume

116

Issue

5

Start / End Page

1283 / 1289

Related Subject Headings

  • Sea Urchins
  • Morphogenesis
  • Molecular Structure
  • Hyalin
  • Fractional Precipitation
  • Developmental Biology
  • Cell-Free System
  • Cell Adhesion Molecules
  • Blotting, Southern
  • Animals