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Human-mouse cell hybrids: a suggestion of structural mutation for dipeptidase-2 deficiency in mouse cells
Science (New York, N.Y.)
|October 6, 1972
Abstract:
The dipeptidase-2 enzyme is inactive in certain cultured cell lines from the mouse. In somatic cell hybrids between such deficient cells and diploid human fibroblasts, the mouse deficiency was complemented when the homologous human peptidase-A was retained. The results suggested that the murine peptidase deficiency was the result of a structural mutation, rather than a regulatory one.
Insights
Murine dipeptidase-2 deficiency was complemented in somatic cell hybrids by human peptidase-A. This suggests a structural mutation, not a regulatory issue, caused the mouse enzyme inactivity.
Area of Science:
- Biochemistry
- Genetics
- Cell Biology
Background:
- Certain mouse cell lines exhibit inactive dipeptidase-2.
- Understanding the genetic basis of enzyme inactivity is crucial.
Purpose of the Study:
- To investigate the cause of dipeptidase-2 inactivity in mouse cell lines.
- To determine if the deficiency is structural or regulatory.
Main Methods:
- Creation of somatic cell hybrids between deficient mouse cells and human fibroblasts.
- Analysis of dipeptidase-2 activity and peptidase-A retention in hybrid cells.
Main Results:
- Mouse dipeptidase-2 deficiency was complemented by the presence of human peptidase-A.
- Complementation occurred when the homologous human peptidase-A gene was retained.
Conclusions:
- The murine dipeptidase-2 deficiency is likely due to a structural mutation.
- This finding distinguishes between structural and regulatory causes of enzyme inactivity.