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Cell surface marker proteins during mouse spermatogenesis: two-dimensional electrophoretic analysis.

C F Millette, C T Moulding

    Journal of Cell Science
    |April 1, 1981
    PubMed
    Summary
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    This study identifies unique proteins in mouse spermatogenic cell membranes, confirming that purified membranes are suitable for analyzing surface proteins during spermatogenesis.

    Area of Science:

    • Reproductive Biology
    • Cell Biology
    • Biochemistry

    Background:

    • Spermatogenesis involves complex cellular differentiation.
    • Understanding plasma membrane protein changes is crucial for reproductive research.
    • Specific markers for spermatogenic cell stages are not well-defined.

    Purpose of the Study:

    • To identify stage-specific proteins in mouse spermatogenic cell plasma membranes.
    • To assess the suitability of purified cell membranes for biochemical analysis.
    • To investigate the impact of cell purification on membrane integrity.

    Main Methods:

    • Isolation of highly homogenous populations of mouse pachytene spermatocytes, round spermatids, and residual bodies.
    • Comparison of plasma membranes using 2D polyacrylamide gel electrophoresis.

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  • Short-term in vitro culture and [3H]leucine incorporation to assess cell viability and protein synthesis.

    • Main Results:

    • Identified two unique polypeptides (Pa, Pb) in pachytene spermatocytes.
    • Identified four unique polypeptides (RSa, RSb, RSc, RSd) in round spermatids.
    • Demonstrated that separated spermatogenic cells survive and synthesize proteins in vitro.
    • Showed minimal degradation of plasma membrane constituents during cell purification.

    Conclusions:

    • Purified plasma membranes from mouse spermatogenic cells are suitable for detailed biochemical analysis.
    • Specific protein markers for pachytene spermatocytes and round spermatids were identified.
    • The cell separation procedure minimally affects the integrity of plasma membrane proteins.