Abstract
The variation in thin filament length was investigated in slow and fast muscle from adult and neonatal rats. Soleus (slow) muscle from adult, 3-, 7-, and 9-d-old rats, and extensor digitorum longus (EDL; fast) muscle from adult rats were serially cross-sectioned. The number of thin filaments per 0.06 microns2 (TF#) was counted for individual myofibrils followed from the H zone of one sarcomere, through the I-Z-I region, to the H zone of an adjacent sarcomere TF# was pooled by distance from the Z band or AI junction. In both adult muscles, thin filament length varied from 0.18 to 1.20 microns, with approximately 25% of the thin filaments less than 0.7 microns in length. In 7- and 9-d soleus, thin filament length ranged from 0.18 to 1.08 microns; except for the longest (0.18 to 1.20 microns) filaments, the distribution of thin filament lengths was similar to that in adult muscle. In 3-d soleus, thin filament length was more uniform, with less than 5% of the filaments shorter than 0.7 microns. In all neonatal muscles, there were approximately 15% fewer thin filaments per unit area as compared to adult muscles. We conclude: (a) In rat skeletal muscle, thin filaments are not of uniform length, ranging in length from 0.18 to 1.20 microns. (b) There may be two stages of thin filament assembly in neonatal muscle: between 3 and 7 d when short thin filaments may be preferentially or synthesized or inserted near the Z-band, and between 9 d and adult when thin filaments of all lengths may be synthesized or inserted into the myofibril.
MeSH Terms
Animals
Cytoskeleton/metabolism,ultrastructure
Male
Muscle Contraction
Muscle Development
Muscles/ultrastructure
Myofibrils/ultrastructure
Rats
Rats, Inbred Strains
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Traeger L
Goldstein M A
References (17)
17 references, click to expand
-
Sarcomere length during post-natal growth of mammalian muscle fibres.
J Cell Sci. 1968 Dec;3(4):539-48
PMID: 5707851
-
Dynamic properties of mammalian skeletal muscles.
Physiol Rev. 1972 Jan;52(1):129-97
PMID: 4256989
-
Hindlimb muscle fiber populations of five mammals.
J Histochem Cytochem. 1973 Jan;21(1):51-5
PMID: 4348494
-
Compositional studies of myofibrils from rabbit striated muscle.
J Cell Biol. 1976 Jan;68(1):123-41
PMID: 1245543
-
Actinins, regulatory proteins of muscle.
Adv Biophys. 1976;:157-85
PMID: 797241
-
Polarity of actin filaments at the initial stage of myofibril assembly in myogenic cells in vitro.
J Cell Biol. 1977 Mar;72(3):777-85
PMID: 557043
-
Variation of thin filament length in heart muscles.
Nature. 1977 May 5;267(5606):74-5
PMID: 859640
-
The polymerization reaction of muscle actin.
Mol Cell Biochem. 1977 Nov 25;18(1):3-13
PMID: 340937
-
The existence of an insoluble Z disc scaffold in chicken skeletal muscle.
Cell. 1978 Dec;15(4):1253-68
PMID: 729000
-
Desmin and vimentin coexist at the periphery of the myofibril Z disc.
Cell. 1979 Dec;18(4):1053-63
PMID: 391403
-
Protein turnover in muscle cells as visualized by autoradiography.
Int Rev Cytol. 1980;67:215-57
PMID: 6450192
-
Trabecular network in adult skeletal muscle.
J Ultrastruct Res. 1980 Oct;73(1):21-6
PMID: 6970269
-
Structural changes in muscle during contraction; interference microscopy of living muscle fibres.
Nature. 1954 May 22;173(4412):971-3
PMID: 13165697
-
Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation.
Nature. 1954 May 22;173(4412):973-6
PMID: 13165698
-
ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE.
J Mol Biol. 1963 Sep;7:281-308
PMID: 14064165
-
FILAMENT LENGTHS IN STRIATED MUSCLE.
J Cell Biol. 1963 Nov;19:369-90
PMID: 14086763
-
Tension development in highly stretched vertebrate muscle fibres.
J Physiol. 1966 May;184(1):143-69
PMID: 5921535