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The distribution of actin and myosin in the rat ovary at different stages of postnatal development was studied by examination of cryostat sections treated with antibodies to chicken smooth muscle (gizzard) myosin or to chicken (pectoral muscle) actin and subsequently with fluoresceinated goat anti-rabbit gamma-globulins. Staining with either antiserum revealed several layers of intensely fluorescent elongated cells within the theca externa, forming a coherent band around the larger Graafian follicles. In smaller follicles, this band of fluorescent cells was incomplete, and ovaries of immature (6-day-old) rats were devoid of strongly fluorescent cells. Corpora lutea contained only scattered fluorescent cells at their circumference. Sections of mature ovaries incubated with antibodies raised against striated (pigeon pectoral) muscle myosin generated no significant fluorescence. Large oocytes stained with either anti-actin or anti-smooth muscle myosin showed a thin fluorescent band just beneath the zona pellucida, suggesting that actin and myosin are associated with the oolemma. The distribution of the two antigens in serial sections of follicles coincided, suggesting that the same cells contained both actin and myosin. It is suggested that follicular growth and maturation is attended by the development of a smooth muscle layer in the theca and that contraction of this layer in response to catecholamines and/or prostaglandins may play a role in the extrusion of the oocyte. The role of contractile elements in the oocyte remains to be elucidated.
Anat Rec 1977 Mar
PMID:Localization of actin and myosin in the rat oocyte and follicular wall by immunofluorescence. 32 43

Heavy meromyosin (HMM) labeling was used to identify the nature of the filaments which form bundles in the cytoplasm of the pericytes in brain tissue. Rat brain tissue pieces were incubated in glycerol solutions at 4 degrees and then transferred into buffer (pH 7.0), (1) without HMM, (2) with HMM, (3) with HMM + 5 mM ATP, and (4) with HMM + 2.5 mM Na+ pyrophosphate. In pericytes from untreated tissue, smooth-surfaced microfilaments, averaging 6 nm in diameter, appear to branch and anastomose and to anchor on the plasma membrane. After exposure to HMM, the number and the density of the microfilaments are strikingly increased. These tightly-packed microfilaments are now heavily coated with exogeneous HMM thus increasing in width to 18-20 mm. They intertwine in closely-woven networks. After incubation in HMM solutions containing ATP or Na+ phosphate, they are no longer coated with thick sidearms. It can thus be concluded that these microfilaments are of actin-like nature. In addition, after incubation in ATP, they are intermingled with, and converge onto the surfaces of, thick, tapered filaments, which we have tentatively identified as of myosin-like nature. Thus, it appears that certain of the major elements necessary for contraction are present in brain pericytes.
Anat Rec 1978 Apr
PMID:Actin- and myosin-like filaments in rat brain pericytes. 34 71

A combined ultrastructural and biochemical study of the avian oxynticopeptic cell was performed. Scanning electron microscopy demonstrates that this cell undergoes great changes in the shape of its apical pole in relation to secretory activity. These changes are confirmed by transmission electron microscopy and by freeze-fracture images. The biochemical finding of actin- and myosin-like proteins in high-speed supernatants of homogenates of these cells as well as the ultrastructural and cytochemical localization of actin-like filaments in their apical poles suggest a possible participation of these proteins in the above-mentioned changes. Thus, the study of cytoplasmic matrix elements and of their organization may be highly relevant in the search for a correlation between structure and function in these cells.
Anat Rec 1979 Jun
PMID:Muscle proteins and the changes in shape of avian oxynticopeptic cells in relation to secretion. 46 28

Muscle spindles and extrafusal fibers in the tenuissimus muscle of mature golden Syrian hamsters were studied morphologically and quantitatively using several light microscopic techniques. Muscle spindles were identified in serial-transverse frozen-sections of whole muscles stained with hematoxylin and eosin. Five tenuissimus muscles were examined from origin to insertion, and the locations of individual receptors were plotted in camera-lucida reconstructions. Spindles were found in proximity to the main neurovascular bundle in the central core of each muscle. A range of 16-20 receptors was noted per muscle. The mean muscle spindle index (the total number of spindles per gram of muscle weight) was 503 and the average spindle length was 7.5 mm. Oxidative enzyme and myosin adenosine-triphosphatase (ATPase) staining profiles were also evaluated in the intrafusal and extrafusal fibers in each muscle. Even numbers of type I and type IIA extrafusal fibers were distributed homogeneously throughout all muscle cross-sections. Histochemical staining patterns varied along the lengths of the three intrafusal fiber types. Nuclear chain fibers possessed staining properties similar to the type IIA extrafusal fibers and exhibited no regional variations. Bag1 fibers displayed staining variability, particularly when treated for myosin ATPase under acid preincubation conditions. Some spindles were isolated under darkfield illumination and then either treated with 7-nitrobenz-2-oxa-1,3-diazole (NBD)-phallacidin to detect filamentous actin by fluorescence microscopy, or prepared for conventional scanning electron microscopy (SEM). By fluorescence microscopy, a registered actin banding-pattern was observed in the sarcomeres of the intrafusal fibers, and variations in the intensity of banding were noted amongst different fibers. SEM revealed punctate sensory nerve endings that adhered intimately to the surfaces of underlying intrafusal fibers in the equatorial and juxtaequatorial regions. By transmission electron microscopy (TEM) these endings appeared crescent-shaped and were enveloped by external laminae. Each profile contained numerous mitochondria and cytoskeletal organelles. The high spindle density observed in this muscle suggests that the hamster tenuissimus may function in hindlimb proprioception.
Anat Rec 1992 Apr
PMID:Morphometry and histoenzymology of the hamster tenuissimus and its muscle spindles. 153 82

This study investigates the interaction of hormones and the cytoskeleton within the apical cytoplasm of uterine epithelial cells of the rat. The effects of the hormones estradiol-17 beta and progesterone on the microfilament configuration were studied using myosin subfragment 1 (S1) decoration of actin microfilaments (MF) and transmission electron microscopy. In control ovariectomized animals, a sparse MF distribution was found in the apical cytoplasm underlying short microvilli with S1-decorated core MF. Hormone treatment experiments consisted of injecting ovariectomized rats with either progesterone or estradiol-17 beta. For the study of the MF configuration accompanying an apical surface primed for blastocyst receptivity, progesterone treatment was immediately followed by a single dose of estradiol-17 beta. The long, regular microvilli associated with estradiol only treatment contained bundled, decorated MF with tightly bundled rootlets. Progesterone alone produced numerous short microvilli with decorated core bundle MF and pronounced rootlets that frequently appeared splayed. The irregular microvilli and luminal surface of the uterine epithelial cells associated with the receptivity hormone sequence contained variable MF configurations, including MF bundles, networks, and areas with a "felted" appearance. The results show that the various hormone regimes produce characteristically different MF configurations and that this component of the cytoskeleton appears to be under the control of a delicate hormone balance within these uterine cells. The responses of uterine MF to specific regimes of steroid hormones used in this study are not only important for the understanding of the mechanisms at work during early pregnancy, but also contribute to the body of knowledge concerning the ways in which hormones in general effect the cytoskeleton of target cells.
Anat Rec 1992 Aug
PMID:Changes in the apical microfilaments of rat uterine epithelial cells in response to estradiol and progesterone. 162 11

Changes in ultrastructure and cytoskeletal organization by avian oxyntic cells, at the onset of HCl secretion, were analysed. Cells in resting state, induced by fasting and cimetidine, were compared with histamine stimulated secreting cells. Ultrastructural studies were done by transmission electron microscopy; the distribution of prekeratin, myosin, and filamin-like protein, by immunofluorescence; and that of F-actin using FITC-phalloidin. Resting cells show short pericellular clefts. These are increasingly deepened in secreting cells by a reorganization of the lateral cell borders involving displacement of the junctional complexes toward the cell base and incorporation of the tubular system to the luminal plasma membrane. In secreting cells, the processes of the secretory surface are concentrated in a pericellular groove. Histamine stimulation induces a drastic redistribution of cytoskeletal proteins. In chicken oxyntic cells, in addition to the F-actin cytoskeleton associated with the membranes of the secretory surface, there is a cytoskeletal ring containing F-actin, myosin, and a filamin-like protein, located at the level of the junctional complexes. In resting cells, filaments and masses of cytoskeletal matrix are associated with the zonula adherens. In secreting cells, the junctional complexes maintain their association with the filamentous ring, while the amorphous matrix is replaced by microfilaments that support the processes of the luminal surface. Intermediate filaments form a peripheral ring probably associated with the zonula adherens, and project from the ring toward the cell cytoplasm. Thus, with the onset of HCl secretion, the apical cytoskeletal ring of resting cells displaces toward the cell base. A role for this cytoskeletal ring in the changes in shape parallel to HCl secretion is discussed.
Anat Rec 1990 Oct
PMID:Redistribution of membranes and cytoskeletal proteins in chicken oxyntic cells during the HCl secretory cycle: ultrastructural and immunofluorescence study. 170 Jun 49

Microridges produce a characteristic fingerprint-like pattern on the surface of fish oral mucosa. The cytoskeleton in these microridges was examined by immunofluorescence microscopy and transmission electron microscopy after detergent extraction and decoration with myosin subfragment 1. The effect of cytochalasin B on microridges was probed with scanning electron microscopy. Immunofluorescence microscopy revealed that actin filaments were present throughout the periphery of the epithelial cells and were especially localized beneath the free surface of the epithelium. In thin sections treated with Triton X-100, the majority of filaments in the microridges and their bases were found to be actin filaments and a plexus of keratin filaments that underlay the network of actin filaments. A part of the plexus of keratin filaments entered the microridges. After extraction with Triton X-100 and decoration with myosin subfragment 1, decorated actin filaments were found in the microridge cores, connected to the keratin filaments. The keratin filaments aggregated in the pattern of microridges and a few of them protruded into the microridges. Treatment with cytochalasin B caused microridges to disappear or to become thinner and lower or to change short or microvillus-like microridges. When most microridges disappeared, the surface of the superficial cells was prominently swollen, but the cell boundaries were fastened, and the microridges in the periphery were preserved. On the basis of these observations, the possible roles of actin and keratin filaments in the maintenance and the formation of microridges are discussed.
Anat Rec 1991 Jun
PMID:Cytoskeleton in microridges of the oral mucosal epithelium in the carp, Cyprinus carpio. 171 56

In situ hybridization (ISH) of myosin heavy chain (MHC) mRNA, immunofluorescent detection of MHC protein, and oxidative enzyme histochemistry were performed on the same fibers in serially sectioned rabbit skeletal muscle. By combining these three techniques quantitatively, on a fiber-by-fiber basis, fibers that expressed mRNA complementary to a fast MHC cDNA pMHC24-79 of unknown subtype (Maeda et al., 1987) were classified into fiber types with respect to slow myosin expression and oxidative capacity. As expected, slow fibers had low hybridization to pMHC24-79. Fast fibers were divided into three subtypes. mRNA from the low oxidative fibers (fast-glycolytic, IIB) did not hybridize with pMHC24-79. Fast fibers whose mRNA hybridized best to pMHC24-79 were mainly in the intermediate range of oxidative capacity (probably IIX). The fast fibers with the highest oxidative capacity had low hybridization to this MHC mRNA (probably IIA). Thus, pMHC24-79 was identified as a clone of a fast isomyosin, tentatively designated as the fast IIX with intermediate oxidative capacity. The expression of more than a single species of fast and slow isomyosin mRNAs in classically defined fiber type was considered in interpreting these results.
Anat Rec 1991 May
PMID:Expression of a fast myosin heavy chain mRNA in individual rabbit skeletal muscle fibers with intermediate oxidative capacity. 182 91

A procedure has been developed for the three-dimensional immunoelectron microscopic localization of cytoskeletal filaments by a deep-etching replica method in combination with immunogold labeling and/or myosin subfragment 1 (S1) decoration techniques. Neonatal hamster heart cells grown on glass coverslips were extracted with Triton X-100 or physically permeabilized by breaking open the cell membranes. S1 decoration was performed on some specimens immediately after the permeabilization. After prefixation in formaldehyde, samples were immunostained with poly- or monoclonal antibodies to desmin or vimentin, and indirectly tagged with colloidal gold probes by the biotin-streptavidin method. After postfixation with glutaraldehyde, tannic acid and osmium tetroxide, the cells were freeze-etched and rotary-replicated with platinum and carbon in a freeze-fracture apparatus. Replicas were viewed with a transmission electron microscope using a tilting specimen stage to obtain stereo images. The procedure made it possible to identify the specific filaments within the complex cytoskeletal networks in cultured hamster heart muscle and nonmuscle cells at high resolution and in three dimensions. The method has advantages in its three-dimensionality and feasibility to evaluate the data by comparing them with those obtained by alternative light microscopic methods. Details of the protocol and a description of the results of using three different antibodies are given.
Anat Rec 1991 Mar
PMID:Deep-etching immunogold replica electron microscopy of cytoskeletal elements in cultured hamster heart cells. 202 81

Three-dimensional (3-D) distribution of atrial and ventricular isomyosins is analysed immunohistochemically during the formation of the tubular chicken heart (stage 7 to 12 [H/H]) using antibodies specific for adult chicken atrial and ventricular myosin heavy chains, respectively. This analysis revealed that both types of isomyosins can be first detected at stage 8 (H/H, possessing four pairs of somites), i.e., when the heart primordium still exists as two separate cardiogenic plates. The ventricular type of isomyosin is initially expressed in those areas of cardiogenic plates in the vicinity of the anterior intestinal portal. The atrial type of isomyosin is initially expressed in zones caudal and lateral to the areas of ventricular isomyosin expression. Medial to the atrial isomyosin-expressing areas, cardiogenic plate areas exist that initially lack myosin expression. Those parts of the cardiogenic plates that fuse in front of the anterior intestinal portal, thereby forming the heart tube, are characterized by the expression of both isomyosins; however, the caudolateral parts of the heart primordium maintain their single atrial isomyosin expression during further development. Cardiac contractions are therefore first observed at stage 10 (H/H, possessing ten pairs of somites) in myocardium that coexpresses both isomyosins.
Anat Rec 1990 Feb
PMID:Isomyosin expression pattern during formation of the tubular chicken heart: a three-dimensional immunohistochemical analysis. 213 8


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