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Volume 271, Number 33, Issue of August 16, 1996 pp. 19943-19949
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Mammary Derived Growth Inhibitor Is Not a Distinct Protein but a Mix of Heart-type and Adipocyte-type Fatty Acid-binding Protein

(Received for publication, July 10, 1995, and in revised form, April 29, 1996)

Bernfried Specht , Norbert Bartetzko , Carsten Hohoff , Helena Kuhl , Regina Franke , Torsten Börchers and Friedrich Spener

From the  Department of Biochemistry, University of Münster, D-48149 Münster, Germany and the  Institute of Chemical and Biochemical Sensor Research, D-48149 Münster, Germany

The amino acid sequence of the mammary derived growth inhibitor (MDGI) from bovine mammary gland (Böhmer, F.-D., Kraft, R., Otto, A., Wernstedt, C., Hellman, U., Kurtz, A., Müller, T., Rohde, K., Etzold, G., Lehmann, W., Langen, P., Heldin, C.-H., and Grosse, R. (1987) J. Biol. Chem. 262, 15137-15143) revealed 95% identity to bovine heart fatty acid-binding protein (H-FABP), explaining the observed immunocross-reactivity. However, a cDNA encoding MDGI has not been found to date. Artificial MDGI cDNA was expressed in an in vitro transcription/translation assay. Analysis by isoelectric focusing of the immunoprecipitated in vitro translation products of lactating bovine mammary gland mRNA did not indicate a protein corresponding to the in vitro translation product of artificial MDGI mRNA. Moreover, two-dimensional electrophoresis of bovine mammary gland proteins confirmed the absence of a protein with the pI of the in vitro translated artificial MDGI mRNA in bovine mammary gland and instead revealed, apart from H-FABP, an unknown protein that was recognized by anti-H-FABP antibodies. From lactating bovine mammary gland the cDNA for adipocyte fatty acid-binding protein (A-FABP) was cloned. The in vitro translation of recombinant mRNA derived from this cDNA yielded a polypeptide that behaved like the unknown immunoreactive protein. Western blotting and immunofluorescence using monospecific antibodies demonstrated the coexistence of H-FABP and A-FABP in the lactating mammary gland. Taking into account that deviations of the MDGI sequence from the bovine H-FABP sequence correspond with A-FABP we attribute the structure originally reported as MDGI to a mix of these proteins.

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