Abnormal proteins of shortened length are preferentially degraded in the cytosol of cultured MRC5 fibroblasts

FEBS Letters

Wharton, S.A.¹  Hipkiss, A.R.¹ 

[1] Department of Biochemistry, King's College, University of London, Strand, London WC2R 2LS, England

关键词: Puromycin;    MRC5 fibroblast;    Proteolysis;    Lysosome;   

DOI  :  10.1016/0014-5793(84)80222-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Puromycyl peptides were degraded in MRC5 fibroblasts more rapidly than normal proteins labelled for the corresponding length of time for both long and short labelling periods. The degradation of the puromycyl peptides occurred almost exclusively in the cytosol of the cells. Even when the half-lives of normal and puromycyl peptides were manipulated to be similar, proportionally more of the normal proteins were degraded in the lysosomes. The rapid degradation of the puromycyl peptides was not due to the inhibition of protein synthesis brought about by puromycin but was due to the structure of the substrates themselves. The degree and intracellular site of degradation of puromycyl peptides closely mimic those of abnormal (missense) proteins containing amino acid analogues.

【 授权许可】

Unknown