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Changing protein patterns during lens cell aging in vitro.

F C Ramaekers, M W Hukkelhoven, A Groeneveld

Biochimica Et Biophysica Acta

|June 29, 1984

Summary

Lens cell culture alters protein synthesis, with alpha-crystallin decreasing and cytoskeletal proteins like actin and vimentin changing. Protein expression shifts significantly during cell aging and elongation in vitro.

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Area of Science:

Cell Biology
Biochemistry
Ophthalmology

Background:

Lens cells in culture provide a model to study protein expression changes.
Understanding lens protein biosynthesis is crucial for eye research.

Purpose of the Study:

To investigate alterations in lens protein biosynthesis during in vitro cell culture.
To characterize changes in crystallin and cytoskeletal protein synthesis and their regulation.

Main Methods:

One- and two-dimensional gel electrophoresis were employed to analyze protein synthesis.
Primary lens cells were cultured and subcultured to observe changes over time.

Main Results:

Alpha-crystallin synthesis decreased significantly as cells detached from the capsule.

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Actin and vimentin synthesis increased with subculturing, while tubulin synthesis ceased.

Cell elongation correlated with increased synthesis of a 26 kDa polypeptide and a 130 kDa glycoprotein, alongside decreased overall glycosylation.

Conclusions:

Lens cell culture induces significant changes in protein biosynthesis, affecting both crystallins and cytoskeletal components.
Cellular aging and elongation in vitro lead to distinct alterations in protein expression profiles and glycosylation patterns.