Tubular aggregates (TAs) originate from the sarcoplasmic reticulum (SR) and
form polymorphic double (or single) -walled structures in cross section. T
As are involved in various human skeletal muscle disorders including period
ic paralysis, congenital myasthenic syndromes, inflammatory myopathies, and
malignant hyperthermias. Horse lumbrical muscle (LM) is a slender fusiform
muscle that shows varying degrees of regression due to its limited activit
y in the limb. Double-walled TAs were found in degenerating spindle fibers
and with a range of 80-116 nm (average 92 nm, n=135) for outer layer and 50
-78 nm (average 59 nm, n=135) for the inner layer. TAs exhibit degradation
of myofibrillar proteins, disruption of mitochondria with cristae lost, gly
cogen accumulation, electron-dense metabolic products, blebbing appearance
of sarcolemma, and presence of various vacuoles. LM fibers also show a simi
larly degenerative state. The disassembly of the SR structure probably prod
uces a large accumulation of SR proteins which remain as molecules without
being further degraded and which could aggregate to form the orderly struct
ure of TAs. We believe that TA formation may be an adaptation to store unba
lanced extra proteins by forming ordered aggregates in degeneration caused
by stress in cells.