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Gene Review:

LOC373362 - hyalin

Strongylocentrotus purpuratus

Wessel, G.M. et al., Adelson, D.L. et al., Davidson, L.A. et al., Vater, C.A. et al.

Davidson, Oster, Keller, Koehl,

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High impact information on LOC373362

We have generated and characterized a monoclonal antibody (McA Tg-HYL) that recognizes sea urchin hyalin as evidenced by immunofluorescence staining of the hyaline layer (HL) and immunoblot staining of the hyalin protein band [1].
McA Tg-HYL did not inhibit hyalin gelation in vitro or the reaggregation of dissociated blastula cells [1].
Sea urchin morphogenesis and cell-hyalin adhesion are perturbed by a monoclonal antibody specific for hyalin [1].
Recombinant hyalin containing the tandem repeat region of the protein was expressed in bacteria and is shown to serve as an adhesive substrate, almost equal to that of native hyalin, in cell adhesion assays [2].
The mRNA is present throughout oogenesis but is rapidly lost at oocyte maturation so that eggs and early embryos have no detectable hyalin mRNA [2].

Biological context of LOC373362

Here we provide a molecular characterization of hyalin and identify a region of the protein that is important for its function in cell adhesion [2].
These data help explain some of the classic functions ascribed to the hyalin protein in early development and now enable investigators to focus on the mechanisms of cell interactions with the hyaline layer [2].

Anatomical context of LOC373362

The major constituent of the hyaline layer is the protein hyalin, a fibrillar glycoprotein of approximately 330 kDa that multimerizes in the presence of calcium [2].
Hyalin mRNA reaccumulates in embryos beginning at the mesenchyme blastula stage; a RNA gel blot and in situ hybridization analysis of gastrulae and larvae shows a progressive confinement of hyalin mRNA to the aboral ectoderm [2].
In fertilized eggs and later-stage embryos, hyalin was observed to be located on the external surface of the embryo [3].

Associations of LOC373362 with chemical compounds

However, glycine extraction resulted in a 40 to 50% decrease in the elastic modulus along with a dramatic reduction in the hyalin protein at the apical ECM, thus implicating the apical ECM as a major mechanical component of the blastula wall [4].

References

Sea urchin morphogenesis and cell-hyalin adhesion are perturbed by a monoclonal antibody specific for hyalin. Adelson, D.L., Humphreys, T. Development (1988) [Pubmed]
A molecular analysis of hyalin--a substrate for cell adhesion in the hyaline layer of the sea urchin embryo. Wessel, G.M., Berg, L., Adelson, D.L., Cannon, G., McClay, D.R. Dev. Biol. (1998) [Pubmed]
Immunolocalization of hyalin in sea urchin eggs and embryos using an antihyalin-specific monoclonal antibody. Vater, C.A., Jackson, R.C. Mol. Reprod. Dev. (1990) [Pubmed]
Measurements of mechanical properties of the blastula wall reveal which hypothesized mechanisms of primary invagination are physically plausible in the sea urchin Strongylocentrotus purpuratus. Davidson, L.A., Oster, G.F., Keller, R.E., Koehl, M.A. Dev. Biol. (1999) [Pubmed]

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