Gewählte Publikation:
Specht, B; Bartetzko, N; Hohoff, C; Kuhl, H; Franke, R; Börchers, T; Spener, F.
Mammary derived growth inhibitor is not a distinct protein but a mix of heart-type and adipocyte-type fatty acid-binding protein.
J Biol Chem. 1996; 271(33):19943-19949
Doi: 10.1074/jbc.271.33.19943
[OPEN ACCESS]
Web of Science
PubMed
FullText
FullText_MUG
Google Scholar
- Co-Autor*innen der Med Uni Graz
-
Spener Friedrich
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- Abstract:
- 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.
- Find related publications in this database (using NLM MeSH Indexing)
-
Adipose Tissue - chemistry
-
Amino Acid Sequence -
-
Animals -
-
Base Sequence -
-
Blotting, Western -
-
Carrier Proteins - chemistry Carrier Proteins - metabolism
-
Cattle -
-
DNA Primers - chemistry
-
Electrophoresis, Gel, Two-Dimensional -
-
Fatty Acid-Binding Proteins -
-
Female -
-
Fluorescent Antibody Technique, Indirect -
-
Gene Expression -
-
Humans -
-
Isoelectric Point -
-
Mammary Glands, Animal - chemistry
-
Mice -
-
Molecular Sequence Data -
-
Myelin P2 Protein - chemistry Myelin P2 Protein - metabolism
-
Myocardium - chemistry
-
Neoplasm Proteins -
-
Nerve Tissue Proteins -
-
RNA, Messenger - genetics
-
Sequence Alignment -
-
Sequence Homology, Amino Acid -
-
Tumor Suppressor Proteins -