Hostname: page-component-586b7cd67f-dlnhk Total loading time: 0 Render date: 2024-11-29T01:34:55.841Z Has data issue: false hasContentIssue false

What Can Epitope Specific Antibodies Tell us About the Organization of Caveolin in Cells?

Published online by Cambridge University Press:  02 July 2020

J.M. Robinson*
Affiliation:
Department of Physiology and Cell Biology, Ohio State University, Columbus, OH, 43210
Get access

Abstract

There are three members of the caveolin (CAV) gene family that give rise to four polypeptides. These polypeptides are CAV-1α, CAV-1β, CAV-2, and CAV-3. The CAV-1β isoform is a truncated form of CAV-1α that lacks 31 amino acids at the N-terminus of the molecule. The CAV- 1β molecule arises through an alternative splicing mechanism.

Caveolae are specialized plasma membrane microdomains that are expressed at high levels in some cell types (e.g., endothelium, adipocytes, fibroblasts). These specialized regions of the plasma membrane have a characteristic omega-shaped appearance with diameters ranging from 40-90 run. They are distinct from clathrin-coated pits since they lack the characteristic coated appearance in electron microscopy. Caveolae were among the first structures to be discovered by biological electron microscopy. However, biochemical characterization of these structures did not begin in earnest until a marker protein was identified. The initial marker was the 22-kDa protein known as caveolin.

Type
Labeling for Microscopy and Correlative Microscopy (Organized by R. Albrecht)
Copyright
Copyright © Microscopy Society of America 2001

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

references

1.Engelman, , et. al. 1998. Am. J. Hum. Genet. 63:15781587.CrossRefGoogle Scholar
2.Palade, G.E. 1953. J. Appl. Phys. 24:1424.Google Scholar
3.Yamada, E. 1955. Biophys. Biochem. Cytol. 1:445458.CrossRefGoogle Scholar
4.Rothberg, K.G., et al. 1992. Cell. 68:673682.CrossRefGoogle Scholar
5.Okamoto, T., Schlegel, A., et al. 1998. J. Biol. Chem. 273:54195422.CrossRefGoogle Scholar
6.Ikonen, E., Parton, R.G. 2000. Traffic. 1:212217.CrossRefGoogle Scholar
7.Gagescu, R., et al. 2000. Mol. Biol. Cell. 6:911927.Google Scholar
8.Monier, S., Parton, R.G., et al. 1995. Mol. Biol. Cell. 6:911927.CrossRefGoogle Scholar
9.Ding, M.et al. 1995. Eur. J. Cell Biol. 66:234245.Google Scholar