Isolation and partial cloning of ryanodine‐sensitive Ca2+ release channel protein isoforms from human myometrial smooth muscle

FEBS Letters

Lynn, Stephen²  Morgan, Joanna M.²  Lamb, Heather K.³  Meissner, Gerhard¹  Gillespie, James I.² 

[1] Department of Biochemistry and Biophysics, School of Medicine, University of North Carolina, Chapel Hill, NC 27599-7260, USA;Department of Physiological Sciences and Biochemistry, The Medical School, University of Newcastle upon Tyne, Framlington Place, Newcastle upon Tyne, NE2 4HH, England;Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, Framlington Place, Newcastle upon Tyne, NE2 4HH, England

关键词: Ryanodine;    Myometrium;    Human;    Smooth muscle;    RyR;    ryanodine receptor;    RyR1;    skeletal ryanodine receptor;    RyR2;    cardiac ryanodine receptor;    RyR3;    brain ryanodine receptor;    SR;    sarcoplasmic reticulum;    InsP3;    inositol 1;    4;    5-trisphosphate;   

DOI  :  10.1016/0014-5793(95)00924-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Partial cDNAs of the ryanodine receptor were cloned using PCR analysis from reverse transcribed total and mRNA, extracted from freshly isolated pregnant, non-pregnant, and cultured human myometrial smooth muscle. The identity of these clones was confirmed by nucleotide sequencing of the fragments and indicate the expression of both the skeletal and brain ryanodine receptor isoforms in these preparations. In freshly isolated non-pregnant myometrial tissue, membrane fractions displaying specific [³H]ryanodine binding activities were isolated using density gradient centrifugation. SDS-PAGE of the sucrose gradient fractions indicated the specific comigration of a polypeptide with a molecular mass of ∼ 544 kDa with the ryanodine binding activity.

【 授权许可】

Unknown