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Interaction of Insulin-like Growth Factor Binding Protein-4, Miz-1, Leptin, Lipocalin-Type Prostaglandin D Synthase, and Granulin Precursor with the N-Terminal Half of Type III Hexokinase

https://doi.org/10.1006/abbi.2000.2019Get rights and content

Abstract

Insulin-like growth factor binding protein-4, Miz-1, leptin, prostaglandin D synthase, and granulin precursor were identified as proteins interacting with the N-terminal half of mammalian Type III hexokinase (HKIII) in the yeast two-hybrid method. These interactions were confirmed by in vitro binding studies. All five of these proteins, and their mRNAs, were present in PC12 cells, as shown by immunoblotting and RT-PCR, respectively. All were coimmunoprecipitated from PC12 extracts with an antibody against HKIII, but not with anti-Type I hexokinase. Moreover, all of these proteins were coimmunoprecipitated using anti-leptin as precipitating antibody, indicating the existence of a macromolecular complex including these five proteins and HKIII. Transfection of M+R 42 cells with HKIII-green fluorescent protein (GFP) reporter constructs gave a diffuse intracellular fluorescence. Cotransfection with leptin or Miz-1 resulted in distinctly different localization of the HKIII-GFP fusion protein, at intracellular sites coincident with localization of leptin-GFP or Miz-1-GFP reporter constructs.

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      2002, Archives of Biochemistry and Biophysics
      Citation Excerpt :

      “HKI”, “HKI-N”, and “HKI-C” will designate the constructs used for expression of the full length isozyme, the N-terminal half, or the C-terminal half alone (Figs. 1c–e), respectively, all driven by the CMV promoter. M + R 42 cells were grown in 100 mm plates as previously described [9,10,20,22]. When cells were approximately 80% confluent, they were transfected with the indicated plasmid construct (10 g DNA/100 mm plate), using LipofectAMINE 2000 as transfection reagent and following the protocol recommended by the manufacturer, Gibco-BRL.

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    Supported by NIH Grant NS 09910.

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