Duchenne dystrophy: alteration in muscle plasma membrane structure

Science ◽  
1977 ◽  
Vol 196 (4293) ◽  
pp. 1005-1007 ◽  
Author(s):  
D. Schotland ◽  
E Bonilla ◽  
M Van Meter
Keyword(s):  
Plasma Membrane ◽  
Membrane Structure ◽  
Duchenne Dystrophy ◽  
Muscle Plasma Membrane

Duchenne dystrophy: Reduced density of orthogonal array subunit particles in muscle plasma membrane

Neurology ◽  
1984 ◽  
Vol 34 (10) ◽  
pp. 1313-1313 ◽  
Author(s):  
Y. Wakayama ◽  
H. Okayasu ◽  
S. Shibuya ◽  
T. Kumagai
Keyword(s):  
Plasma Membrane ◽  
Orthogonal Array ◽  
Duchenne Dystrophy ◽  
Muscle Plasma Membrane ◽  
Reduced Density

A modified liquid-mosaic model of plasma membrane structure

1998 ◽  
Vol 30 (4-5) ◽  
pp. 328-329 ◽  
Author(s):  
V. K. Rybal'chenko
Keyword(s):  
Plasma Membrane ◽  
Membrane Structure ◽  
Mosaic Model

Muscle Plasma Membrane Changes in Dystrophin Gene Exon 52 Knockout Mouse

2001 ◽  
Vol 197 (6) ◽  
pp. 441-447 ◽  
Author(s):  
Seiji Shibuya ◽  
Yoshihiro Wakayama ◽  
Makoto Murahashi ◽  
Hiroko Kojima ◽  
Hiroaki Oniki ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Knockout Mouse ◽  
Dystrophin Gene ◽  
Muscle Plasma Membrane ◽  
Membrane Changes ◽  
Gene Exon

Interpretation of yeast plasma membrane structure

Micron (1969) ◽  
1980 ◽  
Vol 11 (3-4) ◽  
pp. 359-364 ◽  
Author(s):  
S. Bullivant
Keyword(s):  
Plasma Membrane ◽  
Membrane Structure ◽  
Yeast Plasma Membrane

The effects of acetylcholine and atropine on the 22Na+ permeability of intestinal smooth muscle vesicles

1978 ◽  
Vol 56 (6) ◽  
pp. 921-925
Author(s):  
L. Spero
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Intestinal Smooth Muscle ◽  
Erythrocyte Ghosts ◽  
Muscarinic Agonists ◽  
Plasma Membrane Vesicles ◽  
Muscle Plasma Membrane ◽  
Whole Muscle ◽  
Kinetics Of

A technique is described which has enabled us to measure changes in 22Na+ efflux from smooth muscle plasma membrane vesicles. The resting 22Na+ efflux from these sealed vesicles showed a concentration-dependent increase in response to acetylcholine and other muscarinic agonists, in similar concentrations to those which increased 42K+ efflux in whole muscle. The kinetics of this efflux were complex and could not be described by less than three exponential processes. The response to agonists has, therefore, been characterized by measurement of the half-life of 22Na+ efflux (t1/2). The acetylcholine effect was inhibited by atropine, but unlike the situation in the whole muscle, this inhibition was noncompetitive. Tubocuraine (a nicotinic antagonist) had no effect on this acetylcholine response. Atropine has no effect by itself on the resting 22Na+ efflux, neither did tetrodotoxin or ouabain. 22Na+ efflux from erythrocyte ghosts and liposomes, prepared from lipid extracts of the smooth muscle plasma membrane, was not modified by acetylcholine or atropine.

An unusual cell surface modification: a double plasma membrane

1979 ◽  
Vol 39 (1) ◽  
pp. 355-372
Author(s):  
N.J. Lane ◽  
J.B. Harrison
Keyword(s):  
Plasma Membrane ◽  
Membrane Structure ◽  
Cell Layer ◽  
Peritrophic Membrane ◽  
Thin Sections ◽  
Double Membrane ◽  
Freeze Fracturing ◽  
Blood Sucking ◽  
Great Pressure ◽  
Insertion Sites

The occurrence of an unusual double plasma membrane structure is reported; it has been studied in conventional thin sections, after lanthanum-impregnation and with freeze-fracturing. This modification of the plasmalemma is found where the luminal cell membrane (I membrane) of gut microvilli in the haematophagous insect, Rhodnius prolixus, is surrounded by a second, outer membrane (O membrane), the 2 separated from one another by a highly regular I-O space of about 10 nm. Lanthanum impregnation reveals the presence of columns inclined at an angle, within this I-O space; as in the continuous junctions which link the lateral borders of these cells, these columns may maintain the very precise I-O distance. From the outer microvillar membranes radiate short spoke-like fibrils or sheets which encounter another more extensive system of myelin-like sheets. Freeze-fracturing reveals that the spoke-like sheets and the other ones which lie like a tube, around and parallel to the microvilli, contain linear ridges composed of particles, lying at random within layers of the myelin-like material which also extends into the lumen of the gut. The microvillar membanes, both O and I, fracture into faces containing rows of either PF particles or EF pits arranged as spiral ridges or grooves around the sides and across the tip of each microbillus. These could be the insertion sites of one or both of the I-O columns and spoke-like sheets while the sheets could represent a variant of peritrophic membrane. The double membrane may be a cellular device to increase the strength of the microvillar layer in these blood-sucking animals, since the cell layer must withstand great pressure owing to a sudden massive extension of the gut during a blood meal.

Calcium pump, high-affinity Ca2+-ATPase, and other ATPases in dog antrum smooth muscle plasma membrane

1985 ◽  
Vol 248 (5) ◽  
pp. C449-C456 ◽  
Author(s):  
A. K. Grover ◽  
C. Y. Kwan ◽  
P. J. Oakes
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Maximal Activity ◽  
Calcium Pump ◽  
Disulfonic Acid ◽  
Calmodulin Antagonists ◽  
High Affinity ◽  
Chelex 100 ◽  
Muscle Plasma Membrane ◽  
Absolute Requirement

The plasma membrane-enriched fraction from dog antrum smooth muscle is enriched in ATP-dependent azide-insensitive Ca2+ uptake (0.3-0.4 microM Ca2+ required for half-maximal activity), a high-affinity Ca2+-ATPase (Km of 0.3-0.8 microM for Ca2+), a low-affinity Ca2+-ATPase (Km for 250-400 microM for Ca2+), and a Mg2+-ATPase. Studies using membranes washed with EDTA and assay media treated with Chelex 100 showed that the high-affinity Ca2+-ATPase did not depend on contaminating Mg2+. Thus, whereas the ATP-dependent Ca2+ uptake had an absolute requirement for Mg2+, the Ca2+-ATPases did not. Studies using gamma-irradiation showed that the protein responsible for the ATP-dependent Ca2+ uptake was inactivated at significantly lower doses of radiation than the three ATPases. The Ca2+ uptake and the high-affinity Ca2+-ATPase also differed in their inhibition by calmodulin antagonists and 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid. Thus it is unlikely that the high-affinity Ca2+-ATPase by itself is responsible for the ATP-dependent Ca2+ uptake.

Preferential support of Ca 2+ uptake in smooth muscle plasma membrane vesicles by an endogenous glycolytic cascade

1989 ◽  
Vol 3 (11) ◽  
pp. 2298-2301 ◽  
Author(s):  
Richard J. Paul ◽  
Christopher D. Hardin ◽  
Luc Raeymaekers ◽  
Frank Wuytack ◽  
Rik Casteels
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Muscle Plasma Membrane

Synaptic Plasma Membrane Structure and Polarity of Long-Sleep and Short-Sleep Mice

1994 ◽  
Vol 309 (2) ◽  
pp. 369-376 ◽  
Author(s):  
F. Schroeder ◽  
S.M. Colles ◽  
G.P. Kreishman ◽  
C.E. Heyliger ◽  
W.G. Wood
Keyword(s):  
Plasma Membrane ◽  
Membrane Structure ◽  
Synaptic Plasma Membrane ◽  
Short Sleep ◽  
Long Sleep
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