Thick filaments of striated muscle are laterally interconnected.
Earlier reports from this and other laboratories indicated that thick filaments may be interconnected along their length by rung-like structures. This study was carried out to test whether these interconnections are genuine structures; whether they appear in different muscle types; and whether they arise from myosin cross-bridges. We studied insect flight muscles because of their well-known ultrastructure, and frog heart and rabbit psoas muscles secondarily. Ultrastructure was examined with freeze-fracture; with conventionally prepared thin sections; and with negative stain. All three methods showed rung-like interconnections between thick filaments. The interconnections spanned the length of the cross-bridge zone, i.e., along all but the central bare zone of the thick filament. They were observed consistently in relaxed, activated, and rigor states. We considered potential artifacts that might cause apparent interconnections where none existed in vivo, but were unable to identify a source of artifact common to all methods. Several features of the interconnections imply that for the most part they may be composed of S-1 heads from adjacent thick filaments binding to one another at their tips.
Baatsen
P H
PH
Center for Bioengineering, University of Washington, Seattle 98195.
Trombitás
K
K
Pollack
G H
GH
D000818:Animals; D001516:Bees; D005614:Freeze Fracturing; D006430:Hemiptera; D008854:Microscopy, Electron; D009119:Muscle Contraction; D009126:Muscle Relaxation; D009132:Muscles / Q000648:ultrastructure*; D009206:Myocardium / Q000648:ultrastructure*; D011817:Rabbits; D011896:Rana temporaria