SOLUBILITY IN NONIONIC DETERGENTS DISTINGUISHES BETWEEN SLOWLY AND RAPIDLY DEGRADED PLASMA-MEMBRANE PROTEIN

Citation
Jf. Hare et A. Holocher, SOLUBILITY IN NONIONIC DETERGENTS DISTINGUISHES BETWEEN SLOWLY AND RAPIDLY DEGRADED PLASMA-MEMBRANE PROTEIN, The Journal of biological chemistry, 269(8), 1994, pp. 5981-5988
Citations number
38
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
269
Issue
8
Year of publication
1994
Pages
5981 - 5988
Database
ISI
SICI code
0021-9258(1994)269:8<5981:SINDDB>2.0.ZU;2-N
Abstract
Four cell surface-exposed, integral membrane proteins from H4-II-E-3 h epatoma monolayer cultures, derivatized by the membrane-impermeant rea gent sulfosuccinimidyl 2-(biotin-amido)ethyl-1,3-dithioproprionate, we re resistant to extraction with Triton X-100 at 0 degrees C. Thirty-th ree other similarly derivatized proteins were solubilized under these same conditions. Antisera were prepared that reacted only with Triton X-100-insoluble proteins. All four Triton X-100-insoluble proteins pre cipitated with the antibody were slowly degraded (t(1/2) > 100 h). By contrast, all but four Triton X-100-soluble proteins were rapidly degr aded (t(1/2) = 24 h). The detergent-insoluble proteins did not possess glycosylphosphatidylinositol anchors nor were they solubilized by Tri ton X-100 after disruption of the cytoskeleton. In addition, they were insoluble in Triton X-100 in isolated membrane preparations but solub le when isolated on streptavidin-agarose and removed from other membra ne proteins. We conclude that protein-protein interactions within the membrane itself result in insolubility in non-ionic detergents for a s mall cohort of plasma membrane proteins and that this may be directly related to the increased metabolic stability for this class of protein s.