Cell proliferation-associated expression of a recently evolved isozyme of triosephosphate isomerase

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Abstract
An electrophoretically unique, thermolabile isozyme of triosephosphate isomerase (TPI; EC 5.3.1.1) accounts for 10–30% of the enzymatic activity in a range of mitotically active human cells and tissues. This type 2 form (subunit) of human TPI appears in two isozymes, an anodally migrating, relative to the constitutive TPI-1/1 homodimer, TPI-2/2 homodimer and the TPI-1/2 heterodimer with an intermediate mobility. Human cell types expressing the induced isozyme, which is the product of the same structural locus as the constitutive isozyme, include mitogen-stimulated lymphocytes, virally transformed B-lymphoblastoid cells, leukemia-derived T-lymphoblastoid cells, HeLa cells, both normal and transformed fibroblasts, and placental tissue. Extracts of nondividing or terminally differentiated human cells/tissues, such as erythrocytes, striated muscle, peripheral lymphocytes, and platelets, contain high levels of the constitutive TPI-1/1 isozyme but little or undetectable levels of the TPI-1/2 or TPI-2/2 isozyme. The cell division-associated TPI-1/2 and -2/2 isozymes are distinct in electrophoretic mobility from the deamidated forms of the constitutive isozyme. Extracts of dividing gorilla fibroblasts display an isozyme pattern identical to that of proliferating human cells, but various proliferating cells derived from the African green monkey, rabbit, and chicken express only the constitutive isozyme. Thus, expression of the cell division-associated isozyme of TPI is restricted to the hominoids, suggesting a recently evolved modification mechanism which is specifically activated in proliferating cells.