Membrane lipid a-crystallin interaction and membrane Ca2+-ATPase activities

Abstract

Alpha-Crystallin-lens membrane binding does not protect the Ca2+ -ATPase pump from thermal derangement or oxidation by H2O2.

Sphingolipids in human lens membranes: an update on their composition and possible biological implications

“…The binding between human lens lipids and alpha-crystallin aggregates of high-molecular weight has been documented. These associations increase with age and opacification Petrash, 2000, 2002a,b;Duindam et al, 1998;Ifeanyi and Takemoto, 1989, 1990a,b, 1991Kodama and Takemoto, 1988;Takehana and Takemoto, 1987;Takemoto et al, 1984;Tang et al, 1998Tang et al, , 1999Zhang et al, 1999;Zigman et al, 1984). It is also possible that the unexpected absence of non-sedimenting bands in membranes from cataractous tissues may reflect an even greater enhancement in the density of the otherwise floating clusters.…”

Regulation of Sarco/Endoplasmic Ca2+-ATPase Expression by Calcium in Human Lens Cells

“…SERCA3 is expressed in tissues actively involved in secretion (Wu et al, 1995;Poch et al, 1998). Lens SERCA is inhibited by oxidation (Ahuja et al, 1999;Borchman et al, 1989;Zhang et al, 1999) and by lipid order Zeng et al, 1999).…”

Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding

“…In contrast to GroEL, however, shown to be located on the surface of lipid bilayers (22), the deeply membrane embedded DPH probe reported significant pene- tration of HSP17 into the membrane hydrophobic core. It should be noted that this effect is unique to HSP17, because saturating amounts of ␣-crystallin were reported to interact only with the external surfaces of membranes (27).…”