scholarly journals THE FINE STRUCTURE OF THE VENTRAL INTERSEGMENTAL ABDOMINAL MUSCLES OF THE INSECT RHODNIUS PROLIXUS DURING THE MOLTING CYCLE

1968 ◽  
Vol 37 (2) ◽  
pp. 445-461 ◽  
Author(s):  
Paul A. Toselli ◽  
Frank A. Pepe
Keyword(s):  
Fine Structure ◽  
Insect Flight ◽  
Motor Nerve ◽  
Thick Filament ◽  
Rhodnius Prolixus ◽  
Abdominal Muscles ◽  
Molting Cycle ◽  
Thin Filaments ◽  
Characteristic Structure ◽  
Thick Filaments

Rhodnius prolixus, a South American insect, molts five times in its development to an adult after emerging from the egg. Each molting cycle is triggered with a blood-meal. The ventral intersegmental abdominal muscles of Rhodnius develop during each molting cycle and are functional at molting. The fine structure of these fully developed muscles from fourth stage larval insects is studied. They have the characteristic structure of slow muscles. They have multiple motor nerve endings, and the myofibrils are poorly defined in cross-section. Longitudinal sections show long sarcomeres (8–10 µ), irregular Z-lines, and no apparent H zones. No M line is seen. Transverse sections through the A-band region show that each hexagonally arranged thick filament is surrounded by 12 thin filaments. Two thin filaments are shared by two neighboring thick filaments. The ratio of thin to thick filaments is 6:1. This structure is related to that found in vertebrate skeletal muscle and insect flight muscle.

scholarly journals THE FILAMENT LATTICE OF COCKROACH THORACIC MUSCLE

1968 ◽  
Vol 36 (3) ◽  
pp. 433-442 ◽  
Author(s):  
Martin Hagopian ◽  
David Spiro
Keyword(s):  
Fine Structure ◽  
Electron Microscope ◽  
Flight Muscle ◽  
Insect Flight ◽  
Thick Filament ◽  
Leucophaea Maderae ◽  
Thick Filaments ◽  
Femoral Muscle ◽  
Flight Muscles ◽  
Characteristic 3

The fine structure of the tergo-coxal muscle of the cockroach, Leucophaea maderae, has been studied with the electron microscope. This muscle differs from some other types of insect flight muscles inasmuch as the ratio of thin to thick filaments is 4 instead of the characteristic 3. The cockroach flight muscle also differs from the cockroach femoral muscle in thin to thick filament ratios and diameters and in lengths of thick filaments. A comparison of these latter three parameters in a number of vertebrate and invertebrate muscles suggests in general that the diameters and lengths of the thick filaments and thin to thick filament ratios are related.

scholarly journals THE FINE STRUCTURE OF THE VENTRAL INTERSEGMENTAL ABDOMINAL MUSCLES OF THE INSECT RHODNIUS PROLIXUS DURING THE MOLTING CYCLE

1968 ◽  
Vol 37 (2) ◽  
pp. 462-481 ◽  
Author(s):  
Paul A. Toselli ◽  
Frank A. Pepe
Keyword(s):  
Skeletal Muscle ◽  
Fine Structure ◽  
Chick Embryo ◽  
Muscle Cell ◽  
Cross Sections ◽  
Rhodnius Prolixus ◽  
Abdominal Muscles ◽  
Constant Ratio ◽  
Molting Cycle ◽  
Line Material

The development of the ventral intersegmental abdominal muscles of Rhodnius prolixus is triggered by feeding. The early muscle (1 day after feeding) contains essentially nonstriated fibrils. However, in cross-sections, areas indicating early I bands, Z lines, and A bands can be recognized. Interdigitating thick and thin myofilaments do not assemble into a precise lattice until sometime between 4 and 5 days after feeding. As development continues, the number of fibrils increases, the region corresponding to the Z line increases in density, and the fibrils contain more recognizable striations. The newly formed fibrils broaden as myofilaments are added peripherally. At all stages throughout development, the ratio of thin to thick myofilaments is always 6:1. The formation of fibrils in the abdominal muscles of Rhodnius is different from that in chick embryo skeletal muscle. The major differences are that at all stages in Rhodnius there are (1) a constant ratio of thin to thick myofilaments, and (2) detectable Z-line material. Other findings in Rhodnius suggest (1) that fusion of mononucleated cells with the multinucleated muscle cell occurs, (2) that microtubules develop in the tendon cell concomitantly with development of myofibrils in the associated muscle cell, and (3) that filaments 55A in diameter aggregate into microtubules.

Cytoskeletal proteins of insect muscle: location of zeelins in Lethocerus flight and leg muscle

1994 ◽  
Vol 107 (5) ◽  
pp. 1115-1129 ◽  
Author(s):  
C. Ferguson ◽  
A. Lakey ◽  
A. Hutchings ◽  
G.W. Butcher ◽  
K.R. Leonard ◽  
...  
Keyword(s):  
Insect Flight ◽  
Regular Structure ◽  
Thick Filament ◽  
Cytoskeletal Proteins ◽  
Stretch Activation ◽  
Insect Muscle ◽  
Thick Filaments ◽  
Flight Muscles ◽  
Leg Muscle ◽  
Low Ionic Strength

Asynchronous insect flight muscles produce oscillatory contractions and can contract at high frequency because they are activated by stretch as well as by Ca2+. Stretch activation depends on the high stiffness of the fibres and the regular structure of the filament lattice. Cytoskeletal proteins may be important in stabilising the lattice. Two proteins, zeelin 1 (35 kDa) and zeelin 2 (23 kDa), have been isolated from the cytoskeletal fraction of Lethocerus flight muscle. Both zeelins have multiple isoforms of the same molecular mass and different charge. Zeelin 1 forms micelles and zeelin 2 forms filaments when renatured in low ionic strength solutions. Filaments of zeelin 2 are ribbons 10 nm wide and 3 nm thick. The position of zeelins in fibres from Lethocerus flight and leg muscle was determined by immunofluorescence and immunoelectron microscopy. Zeelin 1 is found in flight and leg fibres and zeelin 2 only in flight fibres. In flight myofibrils, both zeelins are in discrete regions of the A-band in each half sarcomere. Zeelin 1 is across the whole A-band in leg myofibrils. Zeelins are not in the Z-disc, as was thought previously, but migrate to the Z-disc in glycerinated fibres. Zeelins are associated with thick filaments and analysis of oblique sections showed that zeelin 1 is closer to the filament shaft than zeelin 2. The antibody labelling pattern is consistent with zeelin molecules associated with myosin near the end of the rod region. Alternatively, the position of zeelins may be determined by other A-band proteins. There are about 2.0 to 2.5 moles of myosin per mole of each zeelin. The function of these cytoskeletal proteins may be to maintain the ordered structure of the thick filament.

Comparison of slow larval and fast adult muscle innervated by the same motor neurone

1980 ◽  
Vol 84 (1) ◽  
pp. 103-118
Author(s):  
M. B. Rheuben ◽  
A. E. Kammer
Keyword(s):  
Developmental Stages ◽  
Neuromuscular Junctions ◽  
Motor Nerve ◽  
Thick Filament ◽  
Motor Neurone ◽  
Muscle Fibre Types ◽  
Thin Filaments ◽  
Adult Muscle ◽  
Motor Neurones ◽  
Two Stages

1. Muscles innervated by an identified set of motor neurones were compared between larval and adult stages. 2. The structure of the larval muscle is typically tonic: long sarcomeres, irregular Z-bands, and 10-12 thin filaments around each thick filament. The structure of the adult muscle is phasic: 3-4 micrometers sarcomeres, regular Z-bands, 6-8 thin filaments around each thick filament, and large mitochondrial volume. 3. The tensions produced by these muscles were correspondingly different. The larval twitch was about 7 times slower and the tetanus/twitch ratio 10 times greater than those of the adult. 4. No structural or physiological differences were observed in the neuromuscular junctions of the two stages. 5. The relatively unchanging functional relationship of a single motor neurone with two different muscle fibre types during two developmental stages is compared with the converse situation in which it has been reported that implantation of a different type of motor nerve into a muscle modifies contractile properties.

Natural Variability in the Length of Thin and Thick Filaments in Single Fibres From a Crab, Portunus Depurator

1970 ◽  
Vol 6 (2) ◽  
pp. 559-592
Author(s):  
CLARA FRANZINI-ARMSTRONG
Keyword(s):  
Thick Filament ◽  
Natural Variability ◽  
Thin Filaments ◽  
Thick Filaments ◽  
Striation Spacing ◽  
Free Region ◽  
Cross Striation ◽  
Single Fibres ◽  
Length Changes ◽  
Medium Type

The carpopodite flexor of the walking legs of the crab Portunus depurator contains fibres belonging to 3 groups. These are characterized by differences in the cross-striation spacing. Fibres having sarcomeres of approximately 4, 5 and 7 µm are here called short, medium and long sarcomere types, respectively. Within individual fibres belonging to any of the groups the length of the A band is not constant. Up to 25 % length differences have been measured in A bands belonging even to the same fibril. The bridge-free regions of the thick filaments are not always in the centre, so that the filaments are often asymmetric. Analogally, the L line, resulting from the alignment of the bridge-free regions of the thick filaments, may be asymmetrically placed in the Z band. The length of the bridge-free region in crab thick filaments is 60 nm, while the corresponding region in vertebrate thick filaments is 120 nm. This is discussed in terms of a possible model of the filament. The length of the thin filaments is proportional to that of the thick filaments in the corresponding portion of the sarcomere. When two A bands of different length occur in adjacent positions along the fibril, the Z line is not a centre of symmetry. The ratio of thin to thick filament number is variable in individual fibrils. In general, the ratio is higher in the medium sarcomere type fibres than in the short sarcomere type. Stretched and shorter portions of single fibres of the medium type have been examined and the A-band length populations compared. From such a study it can be deduced that passive length changes occur in crab fibres by sliding of thin and thick filaments.

scholarly journals LOCALIZATION OF MYOSIN FILAMENTS IN SMOOTH MUSCLE

1968 ◽  
Vol 37 (1) ◽  
pp. 105-116 ◽  
Author(s):  
Robert E. Kelly ◽  
Robert V. Rice
Keyword(s):  
Smooth Muscle ◽  
Cross Section ◽  
Striated Muscle ◽  
Thick Filament ◽  
Longitudinal Axis ◽  
Thin Filaments ◽  
Chicken Gizzard ◽  
Thick Filaments ◽  
Myosin Filaments ◽  
Muscle Myosin

Thick myosin filaments, in addition to actin filaments, were found in sections of glycerinated chicken gizzard smooth muscle when fixed at a pH below 6.6. The thick filaments were often grouped into bundles and run in the longitudinal axis of the smooth muscle cell. Each thick filament was surrounded by a number of thin filaments, giving the filament arrangement a rosette appearance in cross-section. The exact ratio of thick filaments to thin filaments could not be determined since most arrays were not so regular as those commonly found in striated muscle. Some rosettes had seven or eight thin filaments surrounding a single thick filament. Homogenates of smooth muscle of chicken gizzard also showed both thick and thin filaments when the isolation was carried out at a pH below 6.6, but only thin filaments were found at pH 7.4. No Z or M lines were observed in chicken gizzard muscle containing both thick and thin filaments. The lack of these organizing structures may allow smooth muscle myosin to disaggregate readily at pH 7.4.

scholarly journals Changes in thick filament length in Limulus striated muscle.

1977 ◽  
Vol 75 (2) ◽  
pp. 366-380 ◽  
Author(s):  
M M Dewey ◽  
B Walcott ◽  
D E Colflesh ◽  
H Terry ◽  
R J Levine
Keyword(s):  
Horseshoe Crab ◽  
Striated Muscle ◽  
Thick Filament ◽  
Filament Length ◽  
Thin Filaments ◽  
Thick Filaments ◽  
Wide Range ◽  
The Difference

Here we describe the change in thick filament length in striated muscle of Limulus, the horseshoe crab. Long thick filaments (4.0 microns) are isolated from living, unstimulated Limulus striated muscle while those isolated from either electrically or K+-stimulated fibers are significantly shorter (3.1 microns) (P less than 0.001). Filaments isolated from muscle glycerinated at long sarcomere lengths are long (4.4 microns) while those isolated from muscle glycerinated at short sarcomere lengths are short (2.9 microns) and the difference is significant (P less than 0.001). Thin filaments are 2.4 microns in length. The shortening of thick filaments is related to the wide range of sarcomere lengths exhibited by Limulus telson striated muscle.

scholarly journals Structure and paramyosin content of tarantula thick filaments.

1983 ◽  
Vol 97 (1) ◽  
pp. 186-195 ◽  
Author(s):  
R J Levine ◽  
R W Kensler ◽  
M C Reedy ◽  
W Hofmann ◽  
H A King
Keyword(s):  
Evolutionary Relationship ◽  
Radial Distance ◽  
Thick Filament ◽  
Optical Diffraction ◽  
Thin Filaments ◽  
Biochemical Characteristics ◽  
Thick Filaments ◽  
Cross Bridges ◽  
Centers Of Mass ◽  
Relationship Of

Muscle fibers of the tarantula femur exhibit structural and biochemical characteristics similar to those of other long-sarcomere invertebrate muscles, having long A-bands and long thick filaments. 9-12 thin filaments surround each thick filament. Tarantula muscle has a paramyosin:myosin heavy chain molecular ratio of 0.31 +/- 0.079 SD. We studied the myosin cross-bridge arrangement on the surface of tarantula thick filaments on isolated, negatively stained, and unidirectionally metal-shadowed specimens by electron microscopy and optical diffraction and filtering and found it to be similar to that previously described for the thick filaments of muscle of the closely related chelicerate arthropod, Limulus. Cross-bridges are disposed in a four-stranded right-handed helical arrangement, with 14.5-nm axial spacing between successive levels of four bridges, and a helical repeat period every 43.5 nm. The orientation of cross-bridges on the surface of tarantula filaments is also likely to be very similar to that on Limulus filaments as suggested by the similarity between filtered images of the two types of filaments and the radial distance of the centers of mass of the cross-bridges from the surfaces of both types of filaments. Tarantula filaments, however, have smaller diameters than Limulus filaments, contain less paramyosin, and display structure that probably reflects the organization of the filament backbone which is not as apparent in images of Limulus filaments. We suggest that the similarities between Limulus and tarantula thick filaments may be governed, in part, by the close evolutionary relationship of the two species.

scholarly journals Myosin motors that cannot bind actin leave their folded OFF state on activation of skeletal muscle

2021 ◽  
Vol 153 (11) ◽  
Author(s):  
Massimo Reconditi ◽  
Elisabetta Brunello ◽  
Luca Fusi ◽  
Marco Linari ◽  
Vincenzo Lombardi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Binding Sites ◽  
Muscle Activation ◽  
Sarcomere Length ◽  
Rapid Change ◽  
Thick Filament ◽  
Actin Binding ◽  
Thin Filaments ◽  
Thick Filaments ◽  
Myosin Motors

The myosin motors in resting skeletal muscle are folded back against their tails in the thick filament in a conformation that makes them unavailable for binding to actin. When muscles are activated, calcium binding to troponin leads to a rapid change in the structure of the actin-containing thin filaments that uncovers the myosin binding sites on actin. Almost as quickly, myosin motors leave the folded state and move away from the surface of the thick filament. To test whether motor unfolding is triggered by the availability of nearby actin binding sites, we measured changes in the x-ray reflections that report motor conformation when muscles are activated at longer sarcomere length, so that part of the thick filaments no longer overlaps with thin filaments. We found that the intensity of the M3 reflection from the axial repeat of the motors along the thick filaments declines almost linearly with increasing sarcomere length up to 2.8 µm, as expected if motors in the nonoverlap zone had left the folded state and become relatively disordered. In a recent article in JGP, Squire and Knupp challenged this interpretation of the data. We show here that their analysis is based on an incorrect assumption about how the interference subpeaks of the M3 reflection were reported in our previous paper. We extend previous models of mass distribution along the filaments to show that the sarcomere length dependence of the M3 reflection is consistent with <10% of no-overlap motors remaining in the folded conformation during active contraction, confirming our previous conclusion that unfolding of myosin motors on muscle activation is not due to the availability of local actin binding sites.

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