Pisoni R L, Thoene J G, Lemons R M, Christensen H N
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor 48109-0606.
J Biol Chem. 1987 Nov 5;262(31):15011-8.
Superficial similarities led us to extend our designation for the transport of the plasma membrane for cationic amino acids, y+, to the lysosomal system also serving for such amino acids. Further study on the purified lysosomes of human skin fibroblasts leads us now to redesignate the lysosomal system as c (for cationic), rather than y+, to emphasize important contrasts. Lysosomal uptake of arginine at pH 7.0 was linear during the first 2 min, but attained a steady state in 6 min. This arginine uptake was Na+-independent and was tripled in rate when the lysosomes had first been loaded with the cationic amino acid analog, S-2-aminoethyl-L-cysteine. Uptake was slowed to one-third when 2 mM MgATP was added to the incubation mixture. The following differences in cationic amino acid influx between lysosomal System c and the plasma membrane System y+ became apparent: 1) arginine influx is increased 10-fold by raising the external pH from 5.0 to 7.0. This effect favors net entry of cationic amino acids under the H+ gradient prevailing in vivo. In contrast, arginine uptake across the plasma membrane is insensitive to pH changes in this range. 2) The Km of arginine uptake by lysosomal System c, 0.32 mM, is eight times that for System y+ arginine uptake by the fibroblast. 3) Certain neutral amino acids in the presence of Na+ are accepted as surrogate substrates by System y+, but not by lysosomal system c. 4) Cationic amino acids in which the alpha-amino group is monomethylated or the distal amino group is quaternary, also D-arginine, are recognized by lysosomal System c, whereas System y+ has little affinity for these analogs. This broader substrate specificity of lysosomal system c led us to discover that thiocholine serves to deplete accumulated cystine from cystinotic fibroblasts as effectively as does the therapeutic agent, cysteamine. The quaternary nitrogen of thiocholine renders the mixed disulfide formed when it reacts with cystine unsatisfactory as a substrate for System y+.
表面上的相似性使我们将用于阳离子氨基酸转运的质膜命名(y+)扩展到同样用于此类氨基酸的溶酶体系统。对人皮肤成纤维细胞纯化溶酶体的进一步研究,使我们现在将溶酶体系统重新命名为c(代表阳离子),而不是y+,以强调重要的差异。在pH 7.0时,精氨酸在溶酶体中的摄取在最初2分钟内呈线性,但在6分钟时达到稳态。这种精氨酸摄取不依赖于Na+,并且当溶酶体首先装载阳离子氨基酸类似物S-2-氨基乙基-L-半胱氨酸时,摄取速率增加两倍。当向孵育混合物中加入2 mM MgATP时,摄取速率减慢至三分之一。溶酶体系统c和质膜系统y+在阳离子氨基酸流入方面的以下差异变得明显:1)通过将外部pH从5.0提高到7.0,精氨酸流入增加10倍。这种效应有利于在体内普遍存在的H+梯度下阳离子氨基酸的净进入。相比之下,质膜上的精氨酸摄取对该范围内的pH变化不敏感。2)溶酶体系统c摄取精氨酸的Km为0.32 mM,是成纤维细胞系统y+摄取精氨酸的Km的八倍。3)在Na+存在下,某些中性氨基酸被系统y+接受为替代底物,但不被溶酶体系统c接受。4)α-氨基被单甲基化或远端氨基为季铵化的阳离子氨基酸,还有D-精氨酸,被溶酶体系统c识别,而系统y+对这些类似物几乎没有亲和力。溶酶体系统c这种更广泛的底物特异性使我们发现,硫代胆碱与治疗剂半胱胺一样有效地从胱氨酸病成纤维细胞中消耗积累的胱氨酸。硫代胆碱的季铵氮使得它与胱氨酸反应形成的混合二硫键作为系统y+的底物不理想。