Breakdown of aberrant protein in rabbit reticulocytes decreases with cell age

Author:

McKay M J,Daniels R S,Hipkiss A R

Abstract

Rabbit reticulocytes, separated into ten cell age groups by bovine serum albumin density-gradient sedimentation, were pulse-labelled with [14C]leucine in the presence of either puromycin dihydrochloride or aminoethyl-L-cysteine (a lysine analogue). Intracellular proteolysis of both the puromyucinyl-peptides and analogue-containing protein decreased with cell maturity.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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1. Proteins and aging;Reviews in Clinical Gerontology;1996-02

2. Gene Expression and Protein Degradation;Comprehensive Physiology;1995-12

3. The unstable haemoglobins;Blood Reviews;1993-09

4. Bovine lens epithelial cells have a ubiquitin-dependent proteolysis system;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1993-01

5. Effects of aging in vitro on intracellular proteolysis in cultured rabbit lens epithelial cells in the presence and absence of serum;In Vitro Cellular & Developmental Biology - Animal;1991-04

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