Lysosomal sulfate transport: inhibitor studies
| Autor: | Peter J. Koetters, Hsu-Fang Chou, Adam J. Jonas |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Phenylglyoxal
Arginine Membrane vesicle Biophysics Transport Biochemistry Rats Sprague-Dawley 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Anion Exchange Protein 1 Erythrocyte Cations Lysosome medicine Animals Trypsin Band 3 030304 developmental biology 0303 health sciences Ion Transport biology Sulfates Chemistry Niflumic acid Intracellular Membranes Cell Biology Sulfate Sulfate transport Rats medicine.anatomical_structure DIDS biology.protein Female Lysosomes 030217 neurology & neurosurgery medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1235(1):79-84 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/0005-2736(94)00301-5 |
| Popis: | Sulfate derived from the degradation of macromolecules is released from lysosomes via a carrier mediated process. In order to further characterize this process, recognized inhibitors of the erythrocyte band 3 anion transporter were examined for their effects on the lysosomal system. Studies with band 3 transport site inhibitors such as DIDS, SITS and phenylglyoxal indicated that, similar to the case for the band 3 protein, the llysosomal transporter has critical lysine and arginine residues. Band 3 translocation pathway or channel blocking inhibitors had mixed effects on the lysosomal system. 1,2-Cyclohexanedione, which covalently modifies a band 3 arginine residue distinct from that modified by phenylglyoxal, inhibited lysosomal sulfate transport. In contrast, the potent band 3 inhibitor dipyridamole had no effect on lysosomal sulfate transport indicating that there are some structural differences between the erythrocyte and lysosomal anion transporters. The band 3 translocation inhibitors niflumic acid and dinitrofluorobenzene were both effective inhibitors of the lysosomal system. Cupric ion inhibited sulfate transport while Ca 2+ , Co 2+ , Mg 2+ , Mn 2+ , and Zn 2+ had no inhibitory effects. Exposure of intact lysosomes to trypsin largely ablated transport of sulfate. This information should be useful in efforts to further elucidate the structure and function of the lysosomal sulfate transporter. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect