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

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

doi:10.1074/jbc.271.33.19943

Cited by 56 publications

(42 citation statements)

References 38 publications

(28 reference statements)

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“…The mammary-derived growth inhibitor from bovine lactating mammary glands, now identified as a mixture of A-and H-FABP [9], reversibly suppresses cell multiplication in a variety of cultured epithelial cells [10][11][12]. In cultured cardiac myocytes, extracellularly added H-FABP seems to induce hypertrophy [13].…”

Section: Discussionmentioning

confidence: 99%

“…Mammary-derived growth inhibitor, which appeared to be identical with a mixture of H-FABP and adipocyte FABP (A-FABP) [9], caused specific growth inhibition and terminal differentiation of mammary epithelial cells [10,11] and modest anti-proliferative activity in human breast cancer cells [12]. The protein also appeared to be an inducer of hypertrophy of cardiac myocytes [13].…”

Section: Some Indications Of a Rolementioning

confidence: 99%

“…Growth medium (6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18) Differentiation medium (10-12) staining by Haematoxylin. Rat A-FABP-cDNA-transfected myoblasts cultured on differentiation medium remained mononuclear and were arrested in the alignment process (Figure 4c).…”

Section: Table 2 Ck and Cs Activities And H-fabp Content Of Transfectmentioning

confidence: 99%

“…No marked differences were detected in total incorporation among the four different types of clone on both media. The extent of uptake varied for different Table 6 Distribution of [1][2][3][4][5][6][7][8][9][10][11][12][13][14] …”

Section: Distribution Of [ 14 C]palmitic Acid In Neutral and Phospholmentioning

confidence: 99%

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Transfection of L6 myoblasts with adipocyte fatty acid-binding protein cDNA does not affect fatty acid uptake but disturbs lipid metabolism and fusion

Prinsen

Veerkamp

1998

Biochemical Journal

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We studied the involvement of fatty acid-binding protein (FABP) in growth, differentiation and fatty acid metabolism of muscle cells by lipofection of rat L6 myoblasts with rat heart (H) FABP cDNA or with rat adipocyte (A) FABP cDNA in a eukaryotic expression vector which contained a puromycin acetyltransferase cassette. Stable transfectants showed integration into the genome for all constructs and type-specific overexpression at the mRNA and protein level for the clones with H-FABP and A-FABP cDNA constructs. The rate of proliferation of myoblasts transfected with rat A-FABP cDNA was 2-fold higher compared with all other transfected cells. In addition, these myoblasts showed disturbed fusion and differentiation, as assessed by morphological examination and creatine kinase activity. Uptake rates of palmitate were equal for all clone types, in spite of different FABP INTRODUCTIONFatty acid-binding proteins (FABPs) belong to a conserved family of intracellular lipid-binding proteins with low molecular mass (14-15 kDa) [1][2][3]. Eight different FABP types have been described : heart, liver, adipose, myelin, intestinal, epidermal, brain and ileal. Many FABP cDNAs have been isolated, cloned and the proteins expressed in bacterial systems. In this way, large amounts of proteins have become available for three-dimensional analysis by crystallography and\or NMR (reviewed in [1,3]). All FABPs studied thus far contain a folding motif designated an up-and-down β-barrel [3].The main function of FABP is thought to be intracellular binding and targeting of fatty acids. FABPs may also modulate the effect of fatty acids on various metabolic enzymes and receptors and cellular processes such as signal transduction and gene expression [1,4]. The function significance of the different FABP types is not clear and may vary with the tissues and the physiological conditions. Adaptation may be related to metabolic requirements of the cell, ligand trafficking and\or modulatory functions.A relation has been observed between fatty acid-oxidation capacity and FABP content of various rat tissues and various human and rat muscles [5][6][7]. FABP content of muscle showed no change under various physiological conditions, except an increase in fast-twitch muscles on chronic electrostimulation and endurance training [7]. Heart FABP (H-FABP) content and fatty acid-oxidation capacity increase in skeletal and heart muscle during postnatal development [7,8]. Some indications of a role Abbreviations used : A-FABP, adipocyte fatty acid-binding protein ; CHO, Chinese hamster ovary ; CK, creatine kinase ; CS, citrate synthase ; D-PBS, Dulbecco's modified PBS ; H-FABP, heart fatty acid-binding protein ; I-FABP, intestinal fatty acid-binding protein ; L-FABP, liver fatty acid-binding protein ; PC, phosphatidylcholine ; PE, phosphatidylethanolamine ; RT, reverse transcriptase ; DMEM, Dulbecco's modified Eagle's medium ; SV40, simian virus 40 ; GAPDH, glyceraldehyde-3-phosphate dehydrogenase ; pac, puromycin acetyltransferase.1 To whom correspondence shou...

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Section: Discussionmentioning

confidence: 99%

Section: Some Indications Of a Rolementioning

confidence: 99%

Section: Table 2 Ck and Cs Activities And H-fabp Content Of Transfectmentioning

confidence: 99%

Section: Distribution Of [ 14 C]palmitic Acid In Neutral and Phospholmentioning

confidence: 99%

See 2 more Smart Citations

Transfection of L6 myoblasts with adipocyte fatty acid-binding protein cDNA does not affect fatty acid uptake but disturbs lipid metabolism and fusion

Prinsen

Veerkamp

1998

Biochemical Journal

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“…185 MDGI is an intracellular fatty acid binding protein known to modulate fatty acid metabolism, in addition to having tumor suppressor activity in various cancer models. [186][187][188][189] It is expressed in 40% of human breast cancers and 85% of human lung cancers; however, expression is lost in cell culture models possibly by epigenetic silencing mechanisms. 185 Experiments investigating the role of MDGI and cetuximab resistance are based on the use of cell lines stably transfected with MDGI grown in three-dimensional cell culture models, or inoculated into mouse mammary fat pads.…”

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confidence: 99%

Molecular mechanisms of resistance to the EGFR monoclonal antibody cetuximab

Brand

Iida

Wheeler

2011

Cancer Biology & Therapy

222

191

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The epidermal growth factor receptor (eGFR) is a receptor tyrosine kinase belonging to the HeR family of receptor tyrosine kinases. Receptor activation upon ligand binding leads to down stream activation of the Pi3K/AKT, RAs/RAF/MeK/ eRK and PLCγ/PKC pathways that influence cell proliferation, survival and the metastatic potential of tumor cells. increased activation by gene amplification, protein overexpression or mutations of the eGFR has been identified as an etiological factor in a number of human epithelial cancers (e.g., NsCLC, CRC, glioblastoma and breast cancer). Therefore, targeting the eGFR has been intensely pursued as a cancer treatment strategy over the last two decades. To date, five eGFR inhibitors, including three small molecule tyrosine kinase inhibitors (TKis) and two monoclonal antibodies have gained FdA approval for use in oncology. Both approaches to targeting the eGFR have shown clinical promise and the anti-eGFR antibody cetuximab is used to treat HNsCC and CRC. despite clinical gains arising from use of cetuximab, both intrinsic resistance and the development of acquired resistance are now well recognized. in this review we focus on the biology of the eGFR, the role of eGFR in human cancer, the development of

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Fatty acid binding proteins and mammary-derived growth inhibitor

Hohoff¹,

Spener²

1998

Fett/Lipid

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Fettsäurebindungsproteine und Mamma-abgeleiteter Wachstumsinhibitor. Die Superfamilie der intrazellulären Lipidbindungsproteine aus Säugetieren besteht bis heute aus 13 unterschiedlichen Proteintypen der Molekularmasse 14-15 kDa, die mit hoher Affinität vor allem Fettsäuren, Retinoide und Gallensäuren binden. Die phylogenetisch verwandten Proteine besitzen eine hoch konservierte Tertiär-struktur und werden von Genen, die aus vier Exons und drei Introns zusammengesetzt sind, kodiert. Ferner enthält der Promotorbereich der Gene Transkriptionsfaktor-Bindungsstellen, die auch in Genen vieler Lipid-metabolisierender Enzyme vorhanden sind und mit Kernrezeptoren in Wechselwirkung treten, die ihrerseits durch Peroxisomen-Proliferatoren und Fettsäuren aktiviert werden. Auf der Grundlage der Wechselwirkungen der Fettsäuren -bekanntlich Makronährstoffe -mit den Ligand-aktivierten Kernrezeptoren und den Fettsäurebindungspro-teinen (FABPs) werden in einer fokussierten Schau die Regulation der FABP-Expression und die Funktionen der einzelnen FABP-Typen in zellulärer Lipid-Homöostase, Signaltransduktion und Wachstumsregulation diskutiert.

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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

Cited by 56 publications

References 38 publications

Transfection of L6 myoblasts with adipocyte fatty acid-binding protein cDNA does not affect fatty acid uptake but disturbs lipid metabolism and fusion

Transfection of L6 myoblasts with adipocyte fatty acid-binding protein cDNA does not affect fatty acid uptake but disturbs lipid metabolism and fusion

Molecular mechanisms of resistance to the EGFR monoclonal antibody cetuximab

Fatty acid binding proteins and mammary-derived growth inhibitor

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