NDLI: Affinity of PIP-aquaporins to sterol-enriched domains in plasma membrane of the cells of etiolated pea seedlings

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Affinity of PIP-aquaporins to sterol-enriched domains in plasma membrane of the cells of etiolated pea seedlings

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Affinity of PIP-aquaporins to sterol-enriched domains in plasma membrane of the cells of etiolated pea seedlings

Content Provider	Springer Nature Link
Author	Belugin, B. V. Zhestkova, I. M. Trofimova, M. S.
Copyright Year	2011
Abstract	The hypothesis that sterol-enriched domains represent sites of preferred localization of PIP-aquaporins was tested in experiments on plasma membranes isolated from cells of etiolated pea (Pisum sativum L.) seedlings. Plasma membranes were isolated from microsomes by the partition in the aqueous two-phase polymer system and separated into vesicle fractions of different buoyant density by flotation in discontinuous OptiPrep gradient. Two types of plasma membrane preparations were used: one was treated with cold 1% Triton X-100 and the other was not. In untreated preparations, three populations of plasma membrane vesicles were obtained, while in the case of treated preparations, fractions of detergent-resistant membranes (DRM) and solubilized membrane proteins were obtained. In all membrane fractions collected after OptiPrep flotation, the amounts of proteins, sterols, and PIP-aquaporins were determined. The highest sterol content was detected in the membrane fraction with buoyant density 1.098 g/cm$^{3}$ and in the DRM fraction (1.146 g/cm$^{3}$). These fractions contained much more PIP-aquaporins than the other ones. Phase state of the lipid bilayer was determined by measuring generalized polarization excitation of fluorescence (GPEX) of laurdan incorporated into the membranes of different fractions. It was revealed that the lipid bilayer of the membranes with density of 1.098 g/cm$^{3}$ had a higher extent of ordering than that of the fractions with density of ∼1.146 g/cm$^{3}$. The results indicated that uppermost local concentrations of PIP-aquaporins were associated with tightly packed sterol-enriched domains. Moreover, upon solubilization of plasma membrane with Triton X-100, PIP-aquaporins mainly resided in DRM, thus exhibiting a high affinity to sterols.
Starting Page	56
Ending Page	63
Page Count	8
File Format	PDF
ISSN	19907478
Journal	Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology
Volume Number	5
Issue Number	1
e-ISSN	19907494
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2011-03-05
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Pisum sativum L. plasma membrane buoyant density detergent-resistant membranes sterols PIP-aquaporins laurdan Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Biophysics

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