Me. Disanto et al., NH2-TERMINAL-INSERTED MYOSIN-II HEAVY-CHAIN IS EXPRESSED IN SMOOTH-MUSCLE OF SMALL MUSCULAR ARTERIES, American journal of physiology. Cell physiology, 41(5), 1997, pp. 1532-1542
We demonstrate, using reverse transcriptase-polymerase chain reaction,
that, whereas abdominal aorta from rabbit consists almost entirely of
myosin heavy chain (MHC) mRNA with no insert at the 5'-terminal codin
g region, the distributing arteries (femoral and saphenous) begin to s
how MHC mRNA with the 21-nucleotide insert that encodes seven amino ac
ids in the ATP-binding region located in the myosin head. The femoral/
iliac artery contains >50% inserted mRNA, whereas the more distal saph
enous artery contains >80% inserted mRNA. This insert is also present
in the smooth muscle from rat tail artery but is absent in the smooth
muscle from rat aorta. The actin-activated ATPase activity of myosin f
rom the rabbit femoral/saphenous artery is 1.7-fold higher than that o
f the myosin from the aorta. A concomitant increase (about twofold) in
the maximum shortening velocity of the saphenous artery, compared wit
h that of the aorta, indicates that the preponderance of the inserted
myosin is associated with both an increase in the actin-activated ATPa
se activity and a larger maximum velocity of shortening. Furthermore,
analysis of the 17-kDa essential light chain from the aorta reveals ne
ar equal quantities of the 17-kDa light chain isoforms a and b, wherea
s the myosin from the femoral/saphenous artery contains predominantly
the 17-kDa light chain a isoform. Together, these data indicate that t
he smooth muscle cells from the small distributing arteries are simila
r to those of visceral smooth muscle with respect to the expression of
myosin isoforms, actin-activated myosin ATPase activity, and contract
ility.