Regional distribution of the enzymes and substrates mediating the action of cAMP in the mammalian lens.

Regional distribution of the enzymes and substrates mediating the action of cAMP in the mammalian lens.
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哺乳动物晶状体中介导 cAMP 作用的酶和底物的区域分布。

DOI:
10.1016/0167-4889(89)90184-5
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发表时间:
1989
期刊:
Biochimica et biophysica acta
影响因子:
--
通讯作者:
Louis,CF
Louis,CF
中科院分区:
--
文献类型:
--
作者:
Hur,KC;Louis,CF

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Localization of adenylate cyclase activity in the outer cortical regions of the bovine lens correlates with the restriction of the G8and G1guanine nucleotide regulatory subunits of this enzyme to these same regions of the lens. In contrast, the major membrane substrates for cAMP-dependent protein kinase (cAMP-PK) (molecular masses of 18, 26 and 28 kDa) were identified in both the inner nuclear and the outer cortical regions of the lens. However, there were differences in the relative amounts of Piincorporated into the 18 kDa and 28 kDa components in different lens regions. The three major membrane substrates for cAMP-PK were also phosphorylated when homogenates of lens cortex were incubated with [γ-32P]ATP plus activators of the lens adenylate cyclase. In contrast, there was no incorporation of32P into these substrates when homogenates of lens nucleus were used. When exogenous cAMP was added to homogenates of lens nucleus or cortex,32P was incorporated into the membrane substrates for cAMP-PK in both regions of the lens, indicating that cAMP-PK was present in both regions. Interestingly, cAMP phosphodiesterase activity was at least 10-times greater in lens cortex than in the lens nucleus. These results indicate that while the major membrane substrates for cAMP-PK could be phosphorylated in all regions of the lens, there is a restriction of those enzymes that synthesize and degrade cAMP to the outer cortical regions of this organ.
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