Premium
Isolation and partial cloning of ryanodine‐sensitive Ca 2+ release channel protein isoforms from human myometrial smooth muscle
Author(s) -
Lynn Stephen,
Morgan Joanna M.,
Lamb Heather K.,
Meissner Gerhard,
Gillespie James I.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00924-x
Subject(s) - ryanodine receptor , gene isoform , microbiology and biotechnology , messenger rna , cloning (programming) , centrifugation , receptor , biology , chemistry , differential centrifugation , myometrium , biochemistry , endocrinology , gene , uterus , computer science , programming language
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 [ 3 H]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.