Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Microfibrils”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 613 records · Page 34Linked to original sources

Nematopsis gigas n. sp. (Apicomplexa), a parasite of Nerita ascencionis (Gastropoda, Neritidae) from Brazil.

A new species of Nematopsis (Apicomplexa, Porosporidae) is described from the mantle tissues of the seawater gastropod, Nerita ascencionis (Neritidae), collected in the Atlantic North off the coast of "Fernando de Noronha" Island (3 degrees 47' 57'' S, 32 degrees 25' 12'' W) situated about 350 km from the northeast coast of Brazil. Numerous oocysts, each contained in a parasitophorous vacuole, were found in the cytoplasm of phagocytes in the mantle tissue of the host. The phagocytes were surrounded by a thin wall composed of lucent material. The phagocyte cytoplasm contained a nucleus surrounded by numerous vesicles and some dense masses. The oocysts were 21.9 +/- 0.5 microm long, and 11.5 +/- 0.6 microm wide. The oocyst wall was 0.18-0.25 microm thick, and the apical zone contained a micropyle, 1.0-1.2 microm in diameter, covered by a canopy-like operculum about 0.25 microm thick. Externally, the oocyst wall was surrounded by numerous anastomosing microfibrils attached to the wall and extending towards the periphery of the parasitophorous vacuole. Some microfibrils formed a dense complex network that surrounded the oocyst in the middle of the parasitophorous vacuole, which opened only at the apical zone near the external region of the opercular system. On the basis of the data obtained by light and transmission electron microscopy and host specificity, the gregarine Nematopsis gigas is distinguished from the nearest species as a new species. The taxonomic affinities and morphological comparisons with other similar species of the same genus are discussed.

Animals↗

Phenotypic alteration of vascular smooth muscle cells precedes elastolysis in a mouse model of Marfan syndrome.

Marfan syndrome is associated with early death due to aortic aneurysm. The condition is caused by mutations in the gene (FBN1) encoding fibrillin-1, a major constituent of extracellular microfibrils. Prior observations suggested that a deficiency of microfibrils causes failure of elastic fiber assembly during late fetal development. Mice homozygous for a targeted hypomorphic allele (mgR) of Fbn1 revealed a predictable sequence of abnormalities in the vessel wall including elastic fiber calcification, excessive deposition of matrix elements, elastolysis, and intimal hyperplasia. Here we describe previously unrecognized concordant findings in elastic vessels from patients with Marfan syndrome. Furthermore, ultrastructural analysis of mgR mice revealed cellular events that initiate destructive changes. The first detectable abnormality was an unusually smooth surface of elastic laminae, manifesting the loss of cell attachments that are normally mediated by fibrillin-1. Adjacent cells adopted alteration in their expression profile accompanied by morphological changes but retained expression of vascular smooth muscle cell markers. The abnormal synthetic repertoire of these morphologically abnormal smooth muscle cells in early vascular lesions included elastin, among other matrix elements, and matrix metalloproteinase 9, a known mediator of elastolysis. Ultimately, cell processes associated with zones of elastic fiber thinning and fragmentation. These data suggest that the loss of cell attachments signals a nonproductive program to synthesize and remodel an elastic matrix. This refined understanding of the pathogenesis of vascular disease in Marfan syndrome will facilitate the development of therapeutic strategies.

Actins↗

Collagen degradation in endodontically treated teeth after clinical function.

Endodontically treated teeth restored with posts are susceptible to coronal leakage after long-term function. We hypothesize that demineralized collagen matrices (DCMs) created in dentin by acidic zinc phosphate cement within the dowel spaces degrade with time. Forty-two post-restored teeth were extracted after three periods of clinical service and were examined, by means of scanning and transmission electron microscopy, for the status of the DCMs. SEM revealed a progressive degradation of the DCMs, becoming less dense after 3 to 5 years, losing structural integrity after 6 to 9 years, and partially disappearing after 10 to 12 years. TEM revealed evidence of collagenolytic activity within the DCMs, with loss of cross-banding and unraveling into microfibrils, and gelatinolytic activity that resulted in disintegration of the microfibrils. Bacterial colonization and the release of bacterial enzymes and of host-derived matrix metalloproteinases may contribute to the degradation of collagen fibrils in root dentin after clinical function.

Bacteria↗

Fibrillin-1 and fibrillin-2 show temporal and tissue-specific regulation of expression in developing elastic tissues.

The recent characterization of multiple fibrillin genes raises the question of whether each of the fibrillin proteins is a component of elastic fiber microfibrils and whether their expression during development of elastic tissues is consistent with a function associated with elastogenesis. To address these possibilities, the expression of fibrillin-1 and fibrillin-2 was compared with expression of MAGP and tropoelastin in two elastogenic tissues that undergo different developmental programs. For both fibrillins, the greatest increase in expression occurred during the last half of fetal development when elastin production is highest. In fetal bovine nuchal ligament, mRNA levels for fibrillin-1 and fibrillin-2 increased approximately threefold during this period, whereas tropoelastin increased 20-fold. Although the relative increase in expression of both fibrillins was equivalent, the basal level of fibrillin-1 expression was greater than fibrillin-2. In developing bovine aorta, fibrillin mRNA levels again paralleled tropoelastin expression although, compared to ligament, elastin synthesis began at an earlier fetal age in this tissue. Furthermore, the relative increase in aortic fibrillin-2 expression was greater than that for fibrillin-1 and the ratio of fibrillin-2 to fibrillin-1 was higher than in the ligament. In contrast to the fibrillins, MAGP expression in nuchal ligament and aorta remained at a constant high level throughout the fetal period. Indirect immunofluorescent staining and immunoelectron microscopy localized both fibrillins as well as MAGP to elastic fiber microfibrils in these developing tissues. The coordinate upregulation of fibrillin-1 and fibrillin-2 expression with the onset of tropoelastin production is consistent with a role in elastic fiber assembly. Our findings also suggest temporal and tissue-specific regulation for the fibrillins during development.

Age Factors↗

Cortical microtubules form a dynamic mechanism that helps regulate the direction of plant growth.

Plants form an axis by controlling the direction of cell expansion; this depends on the way in which cellulose microfibrils in the wall resist stretching in particular directions. In turn, the alignment of cellulose microfibrils correlates strongly with the alignment of plasma membrane-associated microtubules, which therefore seem to act as templates for laying down the wall fibrils. Microtubules are now known to be quite dynamic, and to reorient themselves between transverse and longitudinal alignments. Plants "steer" the direction of growth by reorienting the cellulose/microtubule machinery. For example, the model predicts that a transverse reorientation on one flank of an organ and a longitudinal orientation on the other should lead to bending. This response has recently been observed in living, gravistimulated maize coleoptiles microinjected with fluorescent microtubule protein. This paper reviews the idea of the dynamic microtubule template and discusses possible mechanisms of reorientation. Recent biochemical work has shown that microtubules are decorated with different classes of associated proteins, whose potential roles are outlined.

Cell Wall↗

AA protein in experimental murine AA amyloid fibrils: a high resolution ultrastructural and immunohistochemical study comparing aldehyde-fixed and cryofixed tissues.

In a previous study, the fibrils of experimental murine AA amyloid were found to be microfibril-like structures with the AA protein (in the form of 1 nm wide flexible filaments) on their exterior surface. In this study, we have re-examined the AA amyloid fibrils with advanced methods of cryofixation and freeze substitution which are known to retain ultrastructural detail as close as possible to the living state. The observations were compared to those obtained with conventional methods of aldehyde fixation. Cryofixation and freeze substitution confirmed the microfibril-like nature of the inner part of the AA amyloid fibril. The AA protein was present on the exterior surface in the form of 3 nm wide 'helical rods' formed by the tight coiling of the 1 nm wide AA protein flaments. The 'helical rods' were arranged parallel to the axis of the fibril and to one another with a uniform center-to-center distance of 5 nm. This arrangement was fully preserved in amyloid fibrils after cryofixation and freeze substitution, but was present in only some areas of formaldehyde fixed mouse spleen AA amyloid This conformation and orientation of AA protein is likely to be that in its native state, given the ability of these advanced methods of biological preservation to retain structures close to that of the living state. This information shoulld be of considerable value in comparing the structure of amyloid fibrils observed in situ with those isolated from tissue or generated in vitro.

Amyloid↗

Electron-microscopic identification of pseudoexfoliation material in extrabulbar tissue.

The structure and distribution of pseudoexfoliation material in extrabulbar tissues from five eyes with typical unilateral intraocular pseudoexfoliation syndrome and two intraocularly unaffected fellow eyes were examined by transmission electron microscopy. In all seven eyes, unevenly distributed pseudoexfoliation aggregates were found in limbal conjunctivae, extraocular rectus and oblique muscles, orbital connective-tissue septa, and the walls of the posterior ciliary arteries, vortex veins, and central retinal vessels passing through the optic nerve sheaths. Typical pseudoexfoliation fibers occurred in close association with connective-tissue components, especially elastic fibers; a moderate predisposition of pseudoexfoliation clumps to accumulate around blood vessels was observed. The findings of pseudoexfoliation material in similar extrabulbar locations in intraocularly uninvolved fellow eyes indicates that pseudoexfoliation fiber formation outside the globe precedes its intraocular manifestation. The intermingling of pseudoexfoliation fibers, microfibrils, and elastic and collagen fibers suggests that pseudoexfoliation fiber formation might result from a disordered synthesis and/or assembly of connective-tissue microfibrils.

Aged↗

Ultrastructural age-related changes on the posterior iris surface. A possible relationship to the pathogenesis of exfoliation.

OBJECTIVES: To verify the presence of age-related changes in the human iris and to determine whether such changes could be related to the pathogenesis of the exfoliation syndrome. DESIGN: Ultrastructural examination of the posterior surface of the normal iris in 9 enucleated eyes. PATIENTS OR OTHER PARTICIPANTS: Eyes of persons aged 1 day, 3 months, and 3, 9, 27, 52, 59, 59, and 65 years. MAIN OUTCOME MEASURE: The presence of aging changes in the iris. RESULTS: Aging changes included duplication of the basal lamina of posterior iris pigment epithelial cells, formation of atrophic invaginations in the posterior cell membranes containing interlacing basal lamina, formation (or deposition) of microfibrils 11 to 13 nm in diameter, with a banding periodicity of 12 to 16 nm, deposition of electron-dense material in relation to the basal lamina and/or microfibrils, and the presence of some fine granular material overlying the basal lamina. CONCLUSION: These changes have been consistently described before in association with exfoliation material, which suggests the possibility that exfoliation is an eventual aging process.

Adult↗

A priori crystal structure prediction of native celluloses.

The packing of beta-1,4-glucopyranose chains has been modeled to further elaborate the molecular structures of native cellulose microfibrils. A chain pairing procedure was implemented that evaluates the optimal interchain distance and energy for all possible settings of the two chains. Starting with a rigid model of an isolated chain, its interaction with a second chain was studied at various helix-axis translations and mutual rotational orientations while keeping the chains at van der Waals separation. For each setting, the sum of the van der Waals and hydrogen-bonding energy was calculated. No energy minimization was performed during the initial screening, but the energy and interchain distances were mapped to a three-dimensional grid, with evaluation of parallel settings of the cellulose chains. The emergence of several energy minima suggests that parallel chains of cellulose can be paired in a variety of stable orientations. A further analysis considered all possible parallel arrangements occurring between a cellulose chain pair and a further cellulose chain. Among all the low-energy three-chain models, only a few of them yield closely packed three-dimensional arrangements. From these, unit-cell dimensions as well as lattice symmetry were derived; interestingly two of them correspond closely to the observed allomorphs of crystalline native cellulose. The most favorable structural models were then optimized using a minicrystal procedure in conjunction with the MM3 force field. The two best crystal lattice predictions were for a triclinic (P(1)) and a monoclinic (P2(1)) arrangement with unit cell dimensions a = 0.63, b = 0.69, c = 1.036 nm, alpha = 113.0, beta = 121.1, gamma = 76.0 degrees, and a = 0.87, b = 0.75, c = 1.036 nm, gamma = 94.1 degrees, respectively. They correspond closely to the respective lattice symmetry and unit-cell dimensions that have been reported for cellulose Ialpha and cellulose Ibeta allomorphs. The suitability of the modeling protocol is endorsed by the agreement between the predicted and experimental unit-cell dimensions. The results provide pertinent information toward the construction of macromolecular models of microfibrils.

Carbohydrate Conformation↗

Reticular meshwork of the spleen in rats studied by electron microscopy.

The reticular meshwork of the rat spleen, which consists of both fibrous and cellular reticula, was investigated by transmission electron microscopy. The fibrous reticulum of the splenic pulp is composed of reticular fibers and basement membranes of the sinuses. These reticular fibers and basement membranes are continuous with each other. The reticular fibers are enfolded by reticular cells and are composed of two basic elements: 1) peripheral basal laminae of the reticular cells, and 2) central connective tissue spaces in which microfibrils, collagenous fibrils, elastic fibers, and unmyelinated adrenergic nerve fibers are present. The basement membranes of the sinuses are sandwiched between reticular cells and sinus endothelial cells and are composed of lamina-densalike material, microfibrils, collagenous fibrils, and elastic fibers. The presence of these connective tissue fibrous components indicates that there are connective tissue spaces in these basement membranes. The basement membrane is divided into three parts: the basal lamina of the reticular cell, the connective tissue space, and the basal lamina of the sinus endothelial cell. When the connective tissue space is very small or absent, the two basal laminae may fuse to form a single, thick basement membrane of the splenic sinus wall. The fibrous reticulum having these structures is responsible for support (collagenous fibrils) and rebounding (elastic fibers). The cells of the cellular reticulum--reticular cells and their cytoplasmic processes, which possess abundant contractile microfilaments, dense bodies, hemidesmosomes, basal laminae, and a well-developed, rough-surfaced endoplasmic reticulum, and Golgi complexes, which are characteristic of both fibroblasts and smooth muscle cells--are considered to be myofibroblasts. They may play roles in splenic contraction and in fibrogenesis of the fibrous reticulum. The contractile ability may be influenced by the unmyelinated adrenergic nerve fibers that pass through the reticular fibers. The three-dimensional reticular meshwork of the spleen consists of sustentacular fibrous reticulum and contractile myofibroblastic cellular reticulum. This meshwork not only supports the organ but also contributes to a contractile mechanism in circulation regulation, in collaboration with major contractile elements in the capsulo-trabecular system.

Animals↗

Ultrastructure of the pronephric kidney in upstream migrant sea lamprey, Petromyzon marinus L.

The pronephric kidneys were examined in upstream migrant sea lampreys, Petromyzon marinus L., by transmission and scanning electron microscopy. Each pronephros consists of an enlarged renal corpuscle (glomus) and ciliated nephrostomes, but there are no renal tubules. The renal corpuscle contains an extensive mesangium, which consists of a highly fibrous extracellular matrix, numerous mesangial cells, granulocytes, and macrophages. The extracellular matrix contains microfibrils with a morphology similar to amyloid P microfibrils, fibrils with a periodicity similar to fibrin, and abundant collagen. Often these fibrillar components are aggregated in the region of the basement membrane, giving it a thickened appearance. Some podocytes of the visceral epithelium appear swollen, and their cytoplasm contains numerous vacuolar inclusions, and many have only primary major processes with only a few or no foot processes. The morphological features of the pronephric kidney of the lamprey at this time in the life cycle reflect the regression of this organ, but some features also resemble those seen in renal pathologies of higher vertebrates.

Animals↗

The development of proline-containing extracellular connective tissue fibrils by chick notochordal epithelium in vitro.

Notochords were isolated from Hamburger-Hamilton stages 13-15 chick embryos by trypsinization and microdissection. These were shown by electron microscopy to be completely devoid of extracellular materials or mesenchymal contaminants. Cultivation of notochordal isolates was carried out on a non-collagenous (Falcon Plastic) substratum for 0 to 48 hours. At 12 hours of in vitro incubation, a discontinuous basal lamina could be demonstrated on the surface of notochordal cells. This was followed by the appearance of microfibrils of various sizes and other components of the extracellular matrix. By 48 hours of in vitro incubation, the same extracellular materials which surround the notochord in vivo (notochord sheath) could be demonstrated in vitro. Autoradiographic studies show that tritiated proline is taken up by notochordal cells and secreted to the extracellular space where label is associated with basal lamina, microfibrils and ground substance. When cis-hydroxyproline, a known collagen-specific inhibitor is added to the system, tritiated proline label is located primarily intracellularly and fewer areas of active fibrillogenesis are noted. This suggests that ultrastructurally recognizable materials produced by notochordal cells in vitro may be at least partially collagenous. Significantly, these materials are produced in vivo at the same time (following stage 10) that notochordal tissues actively induce somite differentiation and cartilage formation. It seems reasonable that a biochemically or ultrastructurally identifiable component of the extracellular matrix may possibly mediate such induction.

Animals↗

Ultrastructural distribution of sulfated complex carbohydrates in elastic cartilage of the young rabbit.

Sulfated glycosaminoglycans are an integral component of elastic cartilage. We have investigated the ultrastructural distribution of sulfated complex carbohydrates (CC) in the mature cartilage and the perichondrium of young rabbit auricles using the high iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP) and the tannic acid-ferric chloride (TA-Fe) methods. In the mature cartilage, HID-TCH-SP stained intracellular Golgi saccules of the mature face, secretory granules, and the extracellular matrix granules, but staining was not discernible in collagen fibrils and osmiophilic elastic fibers consisting of only amorphous elastin. The HID and TA-Fe staining were similarly observed in matrix granules, whereas the elastic fibers and collagen fibrils lacked the staining. The pericellular matrix granules had a diameter of 34 +/- 5 nm (mean +/- SD; n = 30). Thiéry's periodate-TCH-SP (PA-TCH-SP) method stained vicinal glycol-containing CC in collagen fibrils but failed to stain matrix granules and elastic fibers. In the perichondrium, HID-TCH-SP staining of the organelles was less intense in the flattened chondrocytes when compared with those in large mature chondrocytes. The extracellular HID and HID-TCH-SP staining were observed in the matrix granules. The diameter of pericellular matrix granules (19 +/- 4 nm, mean +/- SD; n = 30) was significantly smaller when compared to those in the mature cartilage (P less than 0.001). The HID-TCH-SP staining was closely associated with collagen fibrils. However, the staining was not seen in collagen fibrils and osmiophilic elastic fibers consisting of elastin and microfibrils. The PA-TCH-SP method stained collagen fibrils and microfibrils but did not stain the amorphous elastin. Thus these studies demonstrate that sulfated CC are packaged in chondrocyte secretory granules and are released into the extracellular matrix to form matrix granules, but are not incorporated into collagen fibrils and elastic fibers.

Animals↗

Differentiation of the chorionic plate of the placenta: cellular and extracellular matrix changes during development in the macaque.

BACKGROUND: The chorionic plate forms the fetal side of the placental disc, and its proper growth and development is important to the formation of a normal placenta. The development and structure of the chorionic plate has received little attention. Therefore, we have conducted a developmental and immunohistochemical study of the chorionic plate of the macaque placenta. METHODS: Conventional light and transmission electron microscopy techniques were used to study macaque placental tissues collected from 22 days of gestation to near term. Standard immunoperoxidase methods were used to identify type IV collagen, laminin, and fibronectin in paraffin sections. RESULTS: Early in gestation the chorionic plate trophoblast consisted of an outer layer of syncytiotrophoblast and a single underlying layer of cytotrophoblast. Beginning at about 100 days of gestation, the cytotrophoblast layer became stratified. The cytotrophoblast cells also became surrounded by variable amounts of extracellular matrix containing type IV collagen, laminin, and fibronectin. Ultrastructurally, the matrix contained abundant 10-12 nm diameter microfibrils. During later gestation the syncytiotrophoblast had a tendency to separate from the cytotrophoblast. CONCLUSIONS: The chorionic plate of the macaque placenta undergoes several distinctive morphological changes over the course of gestation. During the period of rapid diametrical growth of the disc, the chorionic plate trophoblast consists of a layer of syncytiotrophoblast and a single layer of cytotrophoblast. During later gestation the cytotrophoblast layer stratifies at a time coincident with that at which diametrical growth of the disc slows. The cytotrophoblast cells of later gestation appear synthetically active and at least some of their products are extracellular matrix components that encapsulate many of these cells. These components include type IV collagen, laminin, fibronectin, and microfibrils.

Animals↗

Changes in the structural properties and rate of hydrolysis of cotton fibers during extended enzymatic hydrolysis.

An extended enzymatic hydrolysis of cotton fibers by crude cellulase from Trichoderma pseudokoningii S-38 is described with characterization of both the enzyme changes of activities and cellulose structure. The hydrolysis rates declined drastically during the early stage and then slowly and steadily throughout the whole hydrolysis process the same trend could be seen during the following re-hydrolysis process. Morphological and structural changes to the fibers, such as swelling, frequent surface erosion, and variation in the packing and orientation of microfibrils, were investigated by scanning electron microscopy (SEM) and atomic force microscopy (AFM). Observation of X-ray diffraction and IR spectra suggests that the hydrolysis process results in a gradual increase in the relative intensity of the hydrogen bond network, and a gradual decrease in the apparent crystal size of cellulose. The I(alpha) crystal phase was hydrolyzed more easily than was the I(beta) crystal phase. Apart from the inactivation of CBHs activity, changes in the packing and arrangement of microfibrils and the structural heterogeneity of cellulose during hydrolysis could be responsible for the reduction in the rate of reaction, especially in its later stages. The results indicate that the enzymatic hydrolysis of cellulose occurs on the outer layer of the fiber surface and that, following this, the process continues in a sub-layer manner.

Adsorption↗

Hydrolytic degradation and morphologic study of poly-p-dioxanone.

The in vitro hydrolytic degradation of 2-0 size PDS monofilament suture was studied for the purpose of revealing its morphologic structure and degradation mechanism. The sutures were immersed in phosphate buffer of pH 7.44 for up to 120 days at 37 degrees C. These hydrolyzed sutures were examined by the changes in tensile properties, weight, thermal properties, x-ray diffraction structure, surface morphology, and dye diffusion phenomena. It was found that hydrolysis had significant effects on the change of PDS fiber morphology and properties. Hydrolysis, however, had no significant effect on overall molecular orientation of the fiber until the very late stage. PDS suture fibers retained their skeleton throughout the earlier periods of hydrolysis concurrent with mass and tensile strength losses. PDS sutures exhibited an absorption delay of 120 days. Both heat of fusion and melting point exhibited a maximum function of hydrolysis time. Hydrolysis of PDS suture fibers proceeded through two stages: random scission of chain segments located in the amorphous regions of microfibrils and intermicrofibrillar space, followed by stepwise scission of chain segments located in the crystalline regions of microfibrils. Dye diffusion data showed that the passage along the longitudinal direction of the fiber was relatively easier than the lateral direction as evident in the diffusion coefficient, activation energy, and flexibility of chain segments. Swiss-cheese model of fiber structure appears to describe the observed dye diffusion phenomena and their dependence on hydrolysis time and dying temperature.

Adsorption↗

Microfibrillar structures in the nucleus and cytoplasm of amoeba proteus.

The presence of microfibrillar structures in the nucleus and cytoplasm of Amoeba proteus has been described after glutaraldehyde and osmium fixation. The possible roles of cytoplasmic microfibrils in the contraction process of amoeba and nuclear microfibrils in the formation of the honeycomb nuclear lamina are discussed.

Amoeba↗

Fine structure and development of the sperm of the tick Ornithodoros (Pavlovskyella) erraticus (Ixodoidea, Argasidae).

Sperm development in Ornithodoros (Pavlovskyella) erraticus includes the formation of subsurface cisternae in the primary spermatocytes, which divide meiotically to secondary spermatocytes and ultimately to spermatids. During spermiogenesis the spermatid undergo morphological transformation including polarization of the nucleus and subsurface cisternae, formation of a cisternal tube, and modification of the subsurface cisternae to cellular processes surrounded by cisternal vesicles. Further transformation occurs after spermatids are introduced into the female. The spermatid cisternal tube now invaginates to form an inner cord surrounded by an outer sheath. The invaginated inner cord elongates anteriorly as the outer sheath continues to invaginate posteriorly during spermiogenesis. With further elongation, the spermatid membrane ruptures anteriorly, leaving the inner cord exposed as the outer surface of the maturing sperm. Posteriorly, the original plasma membrane invaginates to form an acrosomal canal which becomes surrounded by an acrosome. The hemispherical anterior end of the mature sperm is covered with rows of projections separated from the remainder of the sperm by a row of fringed processes. Except for the posterior end, the rest of the sperm is covered by longitudinally distributed electron-dense cellular processes and an outer mat of more electron-lucent tubular elements. Mitochondria and bundles of microfibrils are found beneath the cellular processes. Microfibrils are suggested to be the principal contractile organelles responsible for sperm motility. Cellular processes appear to be the main external motile structures, while movements of tubular elements and fringed processes may also contribute to sperm motility.

Animals↗