Cholesterol sulphate sulphohydrolase of human placenta lysosomal membrane.

In this paper we report that the activity of cholesterol sulphate sulphohydrolase (CHS-ase) is associated with the lysosomal membranes. The procedure of purification of CHS-ase from human placenta lysosomes was elaborated. The purified enzyme is highly specific to cholesterol sulphate (specific activity 2126.

Dehydroepiandrosterone sulphate sulphohydrolase [correction of sulphoydrolase] from human placenta microsomes--properties of the purified enzyme.

A form of steroid sulphate sulphohydrolase (EC 3.1.6.

[Lysosomal membrane glycoprotein lamp2a--receptor for chaperone-mediated degradation of cytosolic proteins].

The structure of several lysosomal membrane glycoproteins (lamp1, lamp2, limpI and limpII) has been described. The significance of the receptor glycoprotein lamp2a in the chaperone-mediated autophagy of cytosolic proteins with KFERQ motif has been described in details as well as the chaperone protein Hsc73 and other chaperones involved in this process. Several modulatory mechanisms of the chaperone-mediated autophagy, which is activated in condition of stress and starvation, were also outlined.

[Nongenomic action of aldosterone on cellular metabolism].

In addition to the well-known genomic action of aldosterone, resulting in delayed effect (1-2 h), a very rapid nongenomic effect (1-2 min) of aldosterone has been recognized recently. The nongenomic action pathway of aldosterone involves: signal perception by protein membrane receptors, induction of the synthesis of messenger molecules such as cAMP, IP3, and DAG, and a change of Ca2+ concentration in the cell cytosol. The target of these rapid responses are also ion channels and exchangers.

Sterolsulphate sulphohydrolase from human placenta microsomes--30 kDa molecular weight form of cholesterol sulphate sulphohydrolase.

The cholesterol sulphate sulphohydrolase (CHS-ase) exhibiting molecular weight of 30 kDa was purified from human placenta microsomes. The microsomal proteins were extracted with 0.5% Triton X-100.