Ma. Carrasco et al., CHARACTERIZATION AND SUBCELLULAR-DISTRIBUTION OF G-PROTEINS IN HIGHLYPURIFIED SKELETAL-MUSCLE FRACTIONS FROM RABBIT AND FROG, Archives of biochemistry and biophysics, 310(1), 1994, pp. 76-81
The presence of G-proteins in highly purified fractions from frog and
rabbit skeletal muscles was analyzed by Bordetella pertussis toxin-cat
alyzed ADP-ribosylation and by immunoblots. Two B. pertussis toxin sub
strates were present in transverse tubules and sarcoplasmic reticulum
from frog and rabbit skeletal muscle. Immunoblot analysis suggested th
at the two B. pertussis toxin substrates present in rabbit sarcoplasmi
c reticulum are possibly alphai2 and alphai3, but the corresponding su
bstrates in sarcoplasmic reticulum from frog are still unidentified. T
ransverse tubules isolated from both rabbit and frog also contained al
phai2 and alphai3; additionally, beta35, beta36, alphao (weak immunore
activity), alphai1 (and/or alphai3 in frog), as (short form only in fr
og), and alphaq were found. Sarcoplasmic reticulum from rabbit also co
ntained alphas (predominantly alphas short), beta36, and alphaq. The p
resence of alphaq in sarcoplasmic reticulum, in addition to transverse
tubules, is potentially a very important finding since this G-protein
has been described only in plasma membranes so far. Also, this study
describes the candidate G-proteins for the control of excitation-contr
action coupling in skeletal muscle. (C) 1994 Academic Press, Inc.