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  • COA 111148

    Tipo de documento:
    Certificado de análisis
    Referencia del producto:
    111148

  • Regulation of RCK1 currents with a cAMP analog via enhanced protein synthesis and direct channel phosphorylation. 7782324

    We have recently shown that the rat brain Kv1.1 (RCK1) voltage-gated K+ channel is partially phosphorylated in its basal state in Xenopus oocytes and can be further phosphorylated upon treatment for a short time with a cAMP analog (Ivanina, T., Perts, T., Thornhill, W. B., Levin, G., Dascal, N., and Lotan, I. (1994) Biochemistry 33, 8786-8792). In this study, we show, by two-electrode voltage clamp analysis, that whereas treatments for a short time with various cAMP analogs do not affect the channel function, prolonged treatment with 8-bromoadenosine 3',5'-cyclic monophosphorothioate ((Sp)-8-Br-cAMPS), a membrane-permeant cAMP analog, enhances the current amplitude. It also enhances the current amplitude through a mutant channel that cannot be phosphorylated by protein kinase A activation. The enhancement is inhibited in the presence of (Rp)-8-Br-cAMPS, a membrane-permeant protein kinase A inhibitor. Concomitant SDS-polyacrylamide gel electrophoresis analysis reveals that this treatment not only brings about phosphorylation of the wild-type channel, but also increases the amounts of both wild-type and mutant channel proteins; the latter effect can be inhibited by cycloheximide, a protein synthesis inhibitor. In the presence of cycloheximide, the (Sp)-8-Br-cAMPS treatment enhances only the wild-type current amplitudes and induces accumulation of wild-type channels in the plasma membrane of the oocyte. In summary, prolonged treatment with (Sp)-8-Br-cAMPS regulates RCK1 function via two pathways, a pathway leading to enhanced channel synthesis and a pathway involving channel phosphorylation that directs channels to the plasma membrane.
    Tipo de documento:
    Referencia
    Referencia del producto:
    14-111

  • ApoB-54.8, a truncated apolipoprotein found primarily in VLDL, is associated with a nonsense mutation in the apoB gene and hypobetalipoproteinemia. 1940616

    A new, large kindred with hypobetalipoproteinemia and a previously undescribed truncated form of apolipoprotein B (apoB) has been identified. The asymptomatic, Caucasian male proband (CK, aged 37 years) has total plasma cholesterol, triglyceride, low density lipoprotein-(LDL) cholesterol, high density lipoprotein- (HDL) cholesterol, and apoB concentrations of 108, 131, 32, 50, and 16 mg/dl, respectively. Plasma samples of 11 family members spanning three generations, which had less than 5th percentile concentrations of LDL-cholesterol, contained three apoB bands detected on immunoblots: the normal apoB-100 and apoB-48 and an unusual band of apparent molecular mass of 299,356 +/- 9580 daltons (approximately 54% the molecular weight of apoB-100). Additional immunoblotting experiments using several different anti-apoB monoclonal antibodies showed that the carboxyl terminal of apoB-100 had been deleted somewhere between amino acid residues 2148-2488. A segment of genomic DNA from the proband was amplified by polymerase chain reaction (PCR) between nucleotides 7491-7791 of Exon 26 of the apoB gene. The DNA segment was cloned into pGEM3Zf(-) and sequenced. A C----T transition was found at nucleotide 7665, resulting in a premature stop codon at amino acid residue 2486 corresponding to apoB-54.8. These results were confirmed by direct sequencing of PCR products from three apoB-54.8 positive and three apoB-54.8 negative kindred members. Allele-specific oligonucleotides were used to identify other affected family members. Cosegregation of apoB-54.8 with the C----T transition occurred in all cases. Based on haplotypes constructed from restriction fragment length polymorphism, variable number of tandem repeats, and 5' insertion/deletion analyses and from the presence or absence of apoB-54.8, it was possible to assign a single allele of apoB to the mutation throughout the family. In contrast with other shorter truncations such as apoB-31, apoB-40, and apoB-46, which are found with particles in the HDL density range, and apoB-89 that is found primarily with LDL, apoB-54.8 was found primarily in very low density lipoproteins, much less in LDL, and was virtually absent in HDL. This suggests that the length of the truncation may significantly affect the metabolism of the associated lipoprotein particles.
    Tipo de documento:
    Referencia
    Referencia del producto:
    17-111
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