The continuity of thick filaments between sarcomeres in honey bee flight muscle

Nature ◽  
1979 ◽  
Vol 281 (5729) ◽  
pp. 319-320 ◽  
Author(s):  
K. Trombitas ◽  
A. Tigyi-Sebes
Keyword(s):  
Honey Bee ◽  
Flight Muscle ◽  
Thick Filaments

scholarly journals Characterization of components of Z-bands in the fibrillar flight muscle of Drosophila melanogaster.

1989 ◽  
Vol 109 (5) ◽  
pp. 2157-2167 ◽  
Author(s):  
J D Saide ◽  
S Chin-Bow ◽  
J Hogan-Sheldon ◽  
L Busquets-Turner ◽  
J O Vigoreaux ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Flight Muscle ◽  
Cross Reactivity ◽  
Antigenic Determinants ◽  
Immunogold Staining ◽  
Thick Filaments ◽  
The Matrix ◽  
Flight Muscles

Twelve monoclonal antibodies have been raised against proteins in preparations of Z-disks isolated from Drosophila melanogaster flight muscle. The monoclonal antibodies that recognized Z-band components were identified by immunofluorescence microscopy of flight muscle myofibrils. These antibodies have identified three Z-disk antigens on immunoblots of myofibrillar proteins. Monoclonal antibodies alpha:1-4 recognize a 90-100-kD protein which we identify as alpha-actinin on the basis of cross-reactivity with antibodies raised against honeybee and vertebrate alpha-actinins. Monoclonal antibodies P:1-4 bind to the high molecular mass protein, projectin, a component of connecting filaments that link the ends of thick filaments to the Z-band in insect asynchronous flight muscles. The anti-projectin antibodies also stain synchronous muscle, but, surprisingly, the epitopes here are within the A-bands, not between the A- and Z-bands, as in flight muscle. Monoclonal antibodies Z(210):1-4 recognize a 210-kD protein that has not been previously shown to be a Z-band structural component. A fourth antigen, resolved as a doublet (approximately 400/600 kD) on immunoblots of Drosophila fibrillar proteins, is detected by a cross reacting antibody, Z(400):2, raised against a protein in isolated honeybee Z-disks. On Lowicryl sections of asynchronous flight muscle, indirect immunogold staining has localized alpha-actinin and the 210-kD protein throughout the matrix of the Z-band, projectin between the Z- and A-bands, and the 400/600-kD components at the I-band/Z-band junction. Drosophila alpha-actinin, projectin, and the 400/600-kD components share some antigenic determinants with corresponding honeybee proteins, but no honeybee protein interacts with any of the Z(210) antibodies.

scholarly journals Molecular and ultrastructural defects in a Drosophila myosin heavy chain mutant: differential effects on muscle function produced by similar thick filament abnormalities.

1988 ◽  
Vol 107 (6) ◽  
pp. 2601-2612 ◽  
Author(s):  
P T O'Donnell ◽  
S I Bernstein
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Function ◽  
Flight Muscle ◽  
Thick Filament ◽  
Differential Sensitivity ◽  
Indirect Flight Muscle ◽  
Molecular Defect ◽  
Thick Filaments ◽  
Nuclease Mapping

We have determined the molecular defect of the Drosophila melanogaster myosin heavy chain (MHC) mutation Mhc and the mutation's effect on indirect flight muscle, jump muscle, and larval intersegmental muscle. We show that the Mhc1 mutation is essentially a null allele which results in the dominant-flightless and recessive-lethal phenotypes associated with this mutant (Mogami, K., P. T. O'Donnell, S. I. Bernstein, T. R. F. Wright, C. P. Emerson, Jr. 1986. Proc. Natl. Acad. Sci. USA. 83:1393-1397). The mutation is a 101-bp deletion in the MHC gene which removes most of exon 5 and the intron that precedes it. S1 nuclease mapping indicates that mutant transcripts follow two alternative processing pathways. Both pathways result in the production of mature transcripts with altered reading frames, apparently yielding unstable, truncated MHC proteins. Interestingly, the preferred splicing pathway uses the more distal of two available splice donor sites. We present the first ultrastrutural characterization of a completely MHC-null muscle and show that it lacks any discernable thick filaments. Sarcomeres in these muscles are completely disorganized suggesting that thick filaments play a critical role in sarcomere assembly. To understand why the Mhc1 mutation severely disrupts indirect flight muscle and jump muscle function in heterozygotes, but does not seriously affect the function of other muscle types, we examined the muscle ultrastructure of Mhc1/+ heterozygotes. We find that these organisms have a nearly 50% reduction in the number of thick filaments in indirect flight muscle, jump muscle, and larval intersegmental muscle. In addition, aberrantly shaped thick filaments are common in the jump muscle and larval intersegmental muscle. We suggest that the differential sensitivity of muscle function to the Mhc1 mutation is a consequence of the unique myofilament arrays in each of these muscles. The highly variable myofilament array of larval intersegmental muscle makes its function relatively insensitive to changes in thick filament number and morphology. Conversely, the rigid double hexagonal lattice of the indirect flight muscle, and the organized lattice of the jump muscle cannot be perturbed without interfering with the specialized and evolutionarily more complex functions they perform.

scholarly journals Effects of Flight on Gene Expression and Aging in the Honey Bee Brain and Flight Muscle

Insects ◽  
2012 ◽  
Vol 4 (1) ◽  
pp. 9-30 ◽  
Author(s):  
Joseph Margotta ◽  
Georgina Mancinelli ◽  
Azucena Benito ◽  
Andrew Ammons ◽  
Stephen Roberts ◽  
...  
Keyword(s):  
Gene Expression ◽  
Honey Bee ◽  
Flight Muscle

scholarly journals Structure of Thick Filaments from Drosophila Indirect Flight Muscle by Cryo-EM

2019 ◽  
Vol 116 (3) ◽  
pp. 404a
Author(s):  
Nadia Daneshparvar ◽  
Dianne Taylor ◽  
Hamidreza Rahmani ◽  
Kenneth A. Taylor
Keyword(s):  
Flight Muscle ◽  
Indirect Flight Muscle ◽  
Thick Filaments

Cytochrome changes during honey bee flight muscle development

1963 ◽  
Vol 8 (1) ◽  
pp. 67-79 ◽  
Author(s):  
Richard C. Herold ◽  
Hans Borei
Keyword(s):  
Honey Bee ◽  
Muscle Development ◽  
Flight Muscle

scholarly journals Antagonistic effects of hexose 1,6-bisphosphates and fructose 2,6-bisphosphate on the activity of 6-phosphofructokinase purified from honey-bee flight muscle

1986 ◽  
Vol 236 (3) ◽  
pp. 925-928 ◽  
Author(s):  
G Wegener ◽  
H Schmidt ◽  
A R Leech ◽  
E A Newsholme
Keyword(s):  
Honey Bee ◽  
Adenylate Kinase ◽  
Flight Muscle ◽  
Antagonistic Effects ◽  
Fructose 1,6 Bisphosphate ◽  
Low Activity

6-Phosphofructokinase purified from honey-bee flight muscle is inhibited by ATP and, unusually, by glucose 1,6-bisphosphate and fructose 1,6-bisphosphate. The inhibition by either of the bisphosphates is not relieved by AMP, but is relieved by fructose 6-phosphate and especially by fructose 2,6-bisphosphate. Lack of effect by AMP is consistent with a low activity of adenylate kinase in this muscle.

scholarly journals THE STRUCTURE OF INTERSEGMENTAL MUSCLE FIBERS IN AN INSECT, PERIPLANETA AMERICANA L

1966 ◽  
Vol 29 (3) ◽  
pp. 449-459 ◽  
Author(s):  
David S. Smith
Keyword(s):  
Periplaneta Americana ◽  
Flight Muscle ◽  
Muscle Fibers ◽  
Structural Features ◽  
Mitochondrial Content ◽  
Thin Filaments ◽  
Transverse Tubular System ◽  
Thick Filaments ◽  
Tubular System ◽  
Contraction And Relaxation

The organization of intersegmental muscle fibers associated with the dorsal abdominal sclerites of the cockroach is described. These fibers correspond closely, in the disposition and derivation of the membranes of the transverse tubular system and sarcoplasmic reticulum cisternae, with insect synchronous flight muscle fibers, but differ markedly from these in their fibrillar architecture and mitochondrial content. The mitochondria are small and generally aligned alongside the prominent I bands of the sarcomere, and, in the best-oriented profiles of the A bands, thick filaments are associated with orbitals of twelve thin filaments, a configuration that has also been observed in striated fibers of insect visceral muscle. These structural features of insect muscles are compared and discussed in terms of possible variations in the control of contraction and relaxation, and in the nature of their mechanical role.

scholarly journals The Structure of the Relaxed Thick Filaments from Lethocerus Asynchronous Flight Muscle

2016 ◽  
Vol 110 (3) ◽  
pp. 300a
Author(s):  
Zhongjun Hu ◽  
Dianne W. Taylor ◽  
Michael K. Reedy ◽  
Robert J. Perz-Edwards ◽  
kenneth A. Taylor
Keyword(s):  
Flight Muscle ◽  
Thick Filaments
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