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Actin constitutes a major component of the cytoskeleton of human polymorphonuclear leukocytes (PMNs). In this study, we present a comprehensive view of the organization of actin in various PMN regions and functional states. Transmission electron microscopic observations were made on whole mount, migrating, and phagocytizing PMNs. Positive identification of actin filaments was made through S-1 myosin subfragment labeling. In all PMNs studied, actin filaments were primarily organized as a three-dimensional meshwork. The density of this meshwork was greatest within the cell cortex. At peripheral regions of nonpolarized (viz., no distinct head or tail region) and polarized PMNs, actin filaments organized into parallel bundles or overlapping arcs. These bundles or arcs were oriented either perpendicular or parallel to the cell periphery. At the base of the PMN, actin filaments converged upon dense, plaquelike condensations. This latter pattern of actin organization was also observed in some pseudopods at the cell front and in phagocytic processes engulfing bacteria. In areas of internalized bacteria, the surrounding actin appeared as a loose meshwork. Treatment of PMNs with the antiactin drug, cytochalasin B, revealed shearing of the peripheral actin meshwork, condensation of the meshwork around the nuclear region, and dissolution of the basal plaquelike condensations.
Anat Rec 1984 May
PMID:The organization of actin filaments in human polymorphonuclear leukocytes. 653 75

Current evidence indicates that polymorphonuclear leukocyte (PMN) chemotaxis and phagocytosis are effected by an actin-myosin contractile system. However, the structural relationship of the contractile cytoskeleton to cell motility is still in question. In addition, while evidence suggests that microtubules are responsible for orientation during chemotaxis, the role of microtubules in degranulation is unresolved. To determine the organizational relationship between these cytoskeletal elements and phagocytosis, we examined whole-mount preparations of PMNs engulfing bacteria. These preparations were examined in the transmission electron microscope (EM) and photographed as stereo pairs. Two important observations were made. First, there was an increased density of cytoskeletal elements in the pseudopod surrounding bacteria. Second, microtubule elements were intimately associated with lysosomal granules, vesicles, and phagosomes. Lysosomal granules and vesicles aligned along microtubules and clustered around phagosomes. This suggests that the microtubules may provide a tracking mechanism whereby lysosomes are specifically parceled out to phagocytic vacuoles. These results also suggest that phagocytosis and degranulation may involve different effector mechanisms.
Anat Rec 1982 Jul
PMID:The cytoskeleton of human polymorphonuclear leukocytes: phagocytosis and degranulation. 689 Mar 21

The diaphragm of neonatal horses is significantly different from the diaphragm of adult horses in terms of histochemical fiber type composition, myosin heavy chain isoform, and native myosin isoform composition. There is a significant increase in the percentage of type I fibers present in the diaphragm with increasing age from birth through about seven months postnatal age. A possible lack of postural tone in the hiatal region of the neonatal diaphragm is suggested to account for increased incidence of vomiting or aspiration pneumonia in younger horses. The isoform data lead to rejection of the hypothesis that the diaphragm of the horse should, as an ungulate, be relatively precocial in its rate of maturation relative to other non-ungulate mammals that have been studied.
Anat Rec 1994 Mar
PMID:Neonatal development of the diaphragm of the horse, Equus caballus. 817 12

The horse provides an interesting model for study of the structure and function of the mammalian diaphragm. Multiple regions of diaphragm from seven adult horses were prepared for histochemistry, immunocytochemistry, myosin heavy chain electrophoresis, and native myosin electrophoresis. Two additional adults were dissected to demonstrate myofiber and central tendon morphology and stained for acetylcholinesterase to demonstrate motor endplates. All regions of the adult diaphragm were histochemically characterized by a preponderance of type I fibers with some type IIa fibers. Type IIb fibers were absent in all adult specimens. Myosin heavy chain electrophoresis supported the histochemical study: two isoform bands were present on SDS gels that comigrated at the same rate as rat type I and IIa myosin heavy chain isoforms. No isoform was determined to comigrate with rat type IIb heavy chain isoforms. Native myosin isoform analysis revealed two isoforms that comigrated with rat FM-4 and FM-3 (FM = fast myosin) and two isoforms that comigrated with rat SM-1 and SM-2 (SM = slow myosin) isoforms. In some samples, a third slow native myosin isoform was observed that comigrated at the same rate as the SM-3 of the equine biceps brachii muscle. This doublet (or "triplet") of slow isoforms is unique to some horse muscles compared with other adult animals studied. It is not known if these multiple slow native myosin isoforms confer some functional advantage to the equine muscles. The adult equine diaphragm also differs in its morphology by having a large central tendon compared to that in other mammals, and is predominantly slow in fiber type and myosin isoform composition.
Anat Rec 1994 Mar
PMID:Morphological, histochemical, and myosin isoform analysis of the diaphragm of adult horses, Equus caballus. 817 13

Stretch-overload has been shown to elevate muscle mass in the avian anterior latissimus dorsi (ALD) by increasing both fiber size and fiber number; however, it is not known if these adaptations result in uniform regulation of myosin isoform expression along the length of the fibers in this slow tonic muscle. When a weight was added to the left wing of 20 adult quail for 30 days, ALD mass was increased by 161%. ALDs were divided into proximal, middle, and distal portions. Tissue cross-sections from each muscle portion were reacted against monoclonal antibodies for either fast (FM) or slow myosin (SM), or processed for identification of native myosin isoforms. The number of fibers expressing FM increased by 190% in the distal region after stretch; however, most of these were small fibers. Electrophoretic analyses of stretched muscles demonstrated an upregulation of SM2 in all regions of the ALD. SM1 was only down-regulated in the proximal region of the ALD. FM isoforms had greater increases in the proximal region than other regions of the overloaded ALD. These data indicate that stretch-induced hypertrophy induces a non-uniform increase in fast myosin isoforms and SM1 along the length of the fibers of the ALD.
Anat Rec 1993 Sep
PMID:Stretch induces non-uniform isomyosin expression in the quail anterior latissimus dorsi muscle. 821 35

The compartmentalization of myosin isoforms within a muscle cell (Gauthier: J. Cell Biol. 110:693-701, 1990) suggests that myosin might be assembled directly into thick filaments at sites where it is synthesized. We therefore examined myofibrils by immunoelectron microscopy to determine whether ribosomes are associated with thick filaments under conditions in which new myosin can be identified. We used the embryonic chick anterior latissimus dorsi (ALD), a slow muscle that is induced, by curare, to synthesize a fast myosin isoform that is not normally present. Myosin was localized in situ, using a gold-labeled monoclonal antibody that recognizes the new isoform. The gold marker, as expected, was localized preferentially to the A band. There was an overall increase of fivefold in the number of gold particles per micron2 of A band in the curare-treated compared to the normal ALD, indicating that the labeled isoform was largely newly formed. There was a corresponding preferential distribution of ribosomes at the A band, especially in the H-band region, and the number of ribosomes per micron2 of A band was nearly twice as high in the curare-treated as in the normal muscle. Ribosomes were located between thick filaments, often aligned in rows. We conclude that ribosomes are located within the filament lattice, and therefore that they are available for local myosin synthesis.
Anat Rec 1993 Oct
PMID:Ribosomes in the skeletal muscle filament lattice. 823 66

The spatial distributions of two different populations of muscle fibers were measured in cross-sections taken from the mid-belly of adult 4DL muscles. Muscle fibers belonging to a single motor unit (identified by glycogen depletion) were distributed randomly in most muscles. Muscle fibers which contained slow myosin (identified immunohistochemically) were distributed nonrandomly, being evenly distributed throughout most of the muscle cross-section, but excluded from the edge of the muscle. Interpreted from a developmental perspective, the results are consistent with the proposals that slow myosin-containing fibers in the adult represent the original population of primary myotubes, and that the adult pattern of motor unit fiber type is achieved by synapse elimination from mismatched fibers rather than by conversion of fiber type.
Anat Rec 1993 Jun
PMID:Spatial distribution of muscle fibers in a lumbrical muscle of the rat. 833 41

Ectoplasmic specializations are complex actin-containing structures found at certain sites of intercellular attachment in Sertoli cells. Current evidence indicates that these structures are a form of actin-associated adhesion junction. In the turtle (Pseudemys scripta) and rooster (Gallus domesticus) ectoplasmic specializations are known to occur adjacent to sites of attachment to elongate spermatids and are characterized by a layer of "loosely" cross-linked actin filaments that lies next to the plasma membrane. In the turtle, a cistern of endoplasmic reticulum is associated with the cytoplasmic face of the filament layer. We have found that, in fixed frozen sections of turtle and rooster testes, immunological probes for myosin II react with epithelial regions that also stain with probes for filamentous actin and that are known to be sites at which ectoplasmic specializations occur. Furthermore, when exposed to standard contraction buffers, the diameters of glycerinated ectoplasmic specializations of the turtle are statistically smaller than those of the same structures exposed to control buffers. We interpret these smaller diameters as being produced by the contraction of actin bundles within the ectoplasmic specializations. Our results indicate that ectoplasmic specializations in the rooster and turtle, unlike those in mammals, possess contractile properties. We speculate that ectoplasmic specializations in eutherian mammals may have evolved from actin-associated adhesion junctions in which the actin bundles were initially contractile and from which myosin II was secondarily lost.
Anat Rec 1993 Jan
PMID:Ectoplasmic ("junctional") specializations in Sertoli cells of the rooster and turtle: evolutionary implications. 841 27

The anatomical structure as well as the smooth muscle cell (SMC1) composition of the ductus arteriosus (DA) were studied in rabbits ranging in age from 29 days of gestation to 20 days after birth. Computer-assisted, three-dimensional reconstructions of hematoxylin-eosin stained serial cryosections from ductus arteriosus-aorta (DA-AO) junctures revealed that DA in animals near term is separated from the aorta by a "septumlike" structure that is continuous with the aortic wall. Two days after birth, obliteration of DA is almost complete, and a small "pocketlike" cavity appears in the pre-existing site in which DA merged into the aorta. This small cavity in the aortic arch was still evident in the large majority of animals examined even 20 days after birth, as also demonstrated by scanning electron microscopy. At this time period DA consisted of a central, fibrotic region surrounded by several layers of SMC (the ligamentum arteriosum, LA) and ended within the aortic media just above the small cavity, forming a round "scar." Vascular SMC composition of DA during closure was examined by means of indirect and double immunofluorescence procedures, using a panel of monoclonal antibodies against some cytoskeletal and cytocontractile proteins (vimentin, desmin, smooth muscle (SM), and nonmuscle (NM) myosin isoforms). "Intimal cushions" were particularly evident from 5 hr after birth and were found to be desmin-negative, homogenously reactive for vimentin and NM myosin, and heterogeneously stained with anti-SM myosin antibody. In SMC subjacent to the "intimal cushions," distribution of vimentin and SM myosin was homogeneous, whereas the one of desmin and NM myosin content was heterogeneous. The cytoskeletal and cytocontractile protein content displayed by SMC during the closure of DA is similar to that of "intimal thickening" found in some pathological conditions of the arterial wall in adult rabbits. Completation of DA closure (day 2) was accompanied by the disappearance of cellular heterogeneity in myosin isoform distribution in both the "intimal cushions" and the underlying media. These results give new insights into: (1) the structure of DA-AO juncture, which can be relevant to the physiology of blood circulation in the fetus, and (2) the phenotypic similarity of vascular SMC populations involved in the formation of "intimal cushions" and "intimal thickening."
Anat Rec 1993 Jan
PMID:Rabbit ductus arteriosus during development: anatomical structure and smooth muscle cell composition. 841 32

The South American opossum, Monodelphis domestica, is very immature at birth, and we wished to assess its potential for studies of jaw muscle development. Given the lack of prior information about any Monodelphis fiber types or spindles, our study aimed to identify for the first time fiber types in both adult and neonatal muscles and the location of spindles in the jaw muscles. Fiber types were identified in frozen sections of adult and 6-day-old jaw and limb muscles by using myosin ATPase and metabolic enzyme histochemistry and by immunostaining for myosin isoforms. The distribution of fiber types and muscle spindles throughout the jaw-closer muscles was identified by immunostaining of sections of methacarnoy-fixed, wax-embedded heads. Most muscles contained one slow (type I) and two fast fiber types (equivalent to types IIA and IIX), which were similar to those in eutherian muscle, and an additional (non-IIB) fast type. In jaw-closer muscles, the main extrafusal fiber type was IIM (characteristic of these muscles in some eutherians), and almost all spindles were concentrated in four restricted areas: one in masseter and three in temporalis. Six-day neonatal muscles were very immature, but future spindle-rich areas were revealed by immunostaining and corresponded in position to the adult areas. Extrafusal and spindle fiber types in Monodelphis share many similarities with eutherian mammalian muscle. This finding, along with the immaturity of myosin isoform expression observed 6 days postnatally, indicates that Monodelphis could provide a valuable model for studying early developmental events in the jaw-closer muscles and their spindles.
Anat Rec 1998 08
PMID:Skeletal fiber types and spindle distribution in limb and jaw muscles of the adult and neonatal opossum, Monodelphis domestica. 971 89


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