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[Electron microscopy of elastic system fibers in the rat mandibular joint].

We study the Elastic System Fibers (ESFs) in the rat mandibular joint using light microscope and image analyzer system and Electron Microscope. The results showed that the ESFs in the articular disc and capsule were more than in the articular cartilage. In addition, microfibrils and elaunin were the principal ESFs in all the articular components. The microfibrils in the articular surfaces ran at nearly right angle to the collagen fibers. The ESFs beneath the articular surfaces and the other articular components showed no specific directivity. ESFs construct an extensive fibers network in the disc and the capsule.

Animals↗

Marfan syndrome and fibrillin disorders.

Marfan syndrome is the second most common inherited connective tissue disorder after osteogenesis imperfecta. Musculoskeletal abnormalities are at the forefront of the clinical picture and count among the major diagnostic criteria for Marfan syndrome, together with cardiovascular and ocular system involvement. Early diagnosis is of the utmost importance since preventive measures significantly increase life expectancy and prevent the occurrence of impairments and disabilities. Marfan syndrome is due to mutations within the fibrillin-1 gene, which is the main protein of the microfibril network. Microfibrils play a crucial role in the trophicity and function of elastic tissue. Multidisciplinary management of the patients and their families is vital.

Extracellular Matrix Proteins↗

A light and electron microscopic study of proliferation and maturation of fibrous astrocytes in the optic nerve of the human embryo.

Optic nerves from perfusion-fixed human embryos of 28,50,75,105,120 and 165 mm crown-rump length were examined in the electron microscope. The number of glial cells per section was found to increase steadily from 10 weeks post-conception to 18 weeks and a close correlation (r = 0.92) was found between the percentage vascularity and the glial population. Mitotic figures were present in all optic nerves examined. From 14 weeks onwards all glial cells, except pericytes, were found to be fibrous astrocytes. The human fibrous astrocyte appears to pass through the following stages of development: (1) Astrocytic precursors (dark glioblasts) have a dense cytoplasmic matrix with few organelles, although a single cilium is frequently present.(2) Concomitant with the increase in vascularization of the optic nerve found between 12 and 14 weeks glycogen granules increase in the cytoplasm of astrocytic precursors, followed by microfibrils, which appear first in the processes and later extend into the perikaryon. (3) With the appearance of glycogen granules the cytoplasmic organelles, particularly mitochondria, increase in amount and the cytoplasmic matrix gradually becomes less dense. (4) With increasing age fewer organelles are found in astrocytic processes, which become thinner and densely packed with microfibrils.

Astrocytes↗

Intracellular and extracellular localization of fibronectin in primary cultures of aortic smooth muscle cells using immunoperoxidase cytochemistry in electron microscopy.

This report describes the intracellular and extracellular localization of fibronectin at the ultrastructural level in primary cultures of aortic smooth muscle cells. Fibronectin was present in all the cisternae of the rough endoplasmic reticulum except the perinuclear cisterna, in large vesicles associated with the trans side of the Golgi complex, and in single large vesicles in the cytoplasm often associated with microtubules. The extracellular microfibrils were heavily stained. In sections parallel to the plane of growth bundles of extracellular microfibrils in continuity with arrays of intracellular microfilaments were observed (fibronexus). The basement membrane around the aortic smooth muscle cells was discontinuous and diffusely stained. The results indicate that fibronectin is localized in the cytoplasmic membranous apparatus of protein synthesis, processing, and secretion. The lack of reaction product in the flat cisternae of the Golgi complex let suggest either that fibronection may not be present in significant amounts within the flattened cisternae or that the method is insufficient in detecting the glycoprotein in this subcompartment off the Golgi complex.

Animals↗

A freeze-fracture study on the differentiation of Golgi and plasma membranes in plant cells.

Dictyosomes, Golgi vesicles, and plasma membranes were investigated after freeze-fracture in cells from growing root tips of cress (Lepidium sativum L.), that are distinguishable by different cellulose content of the cell wall, into (i) meristematic cells during early formation of the cell plate, (ii) statocytes of the root cap, and (iii) cortex cells of the differentiation zone. The results of this study show that the number of intramembrane particles (imps) is high in dictyosome cisternae, but low in membranes of budding or dictyosome-derived vesicles. Imps are disperse in the vesicle membranes of meristematic cells (i), but are often grouped into clusters in vesicle membranes of statocytes (ii), and of cortex cells (iii). For the number of particle aggregates in vesicle membranes, the following relation holds: (i) < (ii) < (iii). The number of particles on both fracture faces (PF and EF) of the plasma membrane differs widely between the cell types investigated. There are approximately 250, 1400, and 3100 imps microns-2 on the PF and 50, 500, and 300 on the EF of (i), (ii), and (iii), respectively. The structural complexity of the plasma membrane as judged by the degree of particle aggregations on the PF and the number of cellulose microfibrils in the cell wall show the same relationship: (i) < (ii) < (iii). Thus, the strong correlation between the distribution of imps in vesicle membranes, the structural complexity of the plasma membrane, and the content of cellulose microfibrils indicate that selection of imps during vesicle formation at dictyosome cisternae is an integral component of biogenesis and structural differentiation of plant plasma membranes.

Brassica↗

Scanning Tunneling Microscopy of the Ultrastructure of Cotton Fiber.

The ultrastructure of the cotton fiber in Lumian No.11 was investigated with scanning tunneling microscope (STM), and the results were compared with that by scanning electron mincrocope(SEM). With SEM, fibrils could be seen, it was difficult, however, to further observe the fine structures in fibrils. Otherwise, with STM, fibrils could be seen clearly, and by making scan areas smaller, it could be observed that the fibrils were composed of microfibrils, and the microfibrils were composed of elementary fibrils, which were the smallest structural units of the fibril, which were arranged in parallel.

Journal Article↗

Effect of monoclonal antibodies to defined regions of tropoelastin on elastogenesis in vitro.

Primary cultures of chick embryo aorta cells were grown for one week in the presence of mouse monoclonal antibodies directed against defined regions of chick tropoelastin. This treatment did not significantly alter cell proliferation, cell viability and incorporation of labeled amino acids into total protein or tropoelastin compared with control cultures in which antibodies were either omitted or substituted with an unrelated monoclonal antibody. Tropoelastin-reactive material in the cell layer was revealed by immunologic staining with rabbit antibodies against the chick protein both at the optical and ultrastructural level. Immunofluorescence of control cultures showed that tropoelastin was incorporated into thin and straight fibrils which were sometimes associated with spot-like elements. In the electron microscope tropoelastin-reactive sites were found mainly on the amorphous core of typical, small elastic fibers. The morphological picture of tropoelastin deposits in cultures exposed to anti-tropoelastin monoclonal antibodies depended on the molecular form (whole antibody or Fab fragments) and the binding specificity of the antibody used. Although alterations common to different antibodies were observed, the main structural features were peculiar for each antibody. Two antibodies which bound epitopes present in two regions of tropoelastin grossly altered the formation of amorphous elastin. Moreover, two antibodies directed against the region of tropoelastin containing the polypentapeptide-repeat (VPGVG)n stimulated the deposition of the protein into the amorphous core of normal-looking elastic fibers and disorganized the compact bundles of parallel microfibrils seen in controls. Finally, one antibody which recognized a unique epitope close to the carboxy-terminal end of tropoelastin and Fab fragments from all antibodies apparently inhibited the formation of the amorphous nuclei of elastic fibers, but not the association of tropoelastin with microfibrils. The data suggest that the association of tropoelastin molecules during fiber assembly is not random, but follows an ordered alignment process which the antibodies alter by imposing a different molecular packing.

Animals↗

[The three-dimensional ultrastructure of the collagen fibers, reticular fibers and elastic fibers: a review].

Fibrous components of the connective tissue are light-microscopically classified into three types: collagen fibers, reticular fibers and elastic fibers. The present paper reviews the three-dimensional ultrastructure of these fibrous components, mainly based on our studies by scanning electron microscopy. The collagen fibers are shaped like tapes or cords about 1 to 20 microns in diameter. Each fiber is a bundle of fibrils running roughly parallel to each other. These collagen fibrils vary in diameter from 30 to 300 nm depending on their locating area of the body, and show a repeating pattern of depressed and protruding segments on the surface. The reticular fibers consist of collagen fibrils about 20-40 nm in diameter, which run singly or in small bundles. They are usually interwoven elaborately to form thin lace-like sheets or sheaths attaching to basal laminae of such cells as epithelial, endothelial and muscular cells. These fibers are considered to play an important role not only in adhering the cells to the collagen fibers, but also in constituting the skeletal framework suitable for individual cells and tissues. The elastic fibers consist of two different components: elastin and fibrillin. Elastin forms unit fibrils of 0.1-0.2 micron thickness which are arranged in bundles or laminae specific to individual organs and tissues. Fibrillin, on the other hand, forms microfibrils about 10 nm in diameter running in or along elastin bundles. These microfibrils also form delicate networks separate from elastin components. For a comprehensive understanding of the fibrous components in the connective tissue, the author proposed categorizing them into two systems: the collagen fibrillar system as a supporting framework of tissues and cells, and the fibrillin-elastin fibrillar system for distributing stressing forces uniformly in tissues.

Connective Tissue↗

Ultrastructural immunocytochemical analysis of elastin in the human lamina cribrosa. Changes in elastic fibers in primary open-angle glaucoma.

The elastic fiber consists of several components: a central core of alpha-elastin and a microfibrillar sheath containing three components: fibrillin, microfibril-associated glycoprotein, and a 35-kD protein with amine oxidase activity. Elastin is a major component of the elastic fibers of the extracellular matrix (ECM) of the lamina cribrosa, and elastic fibers undergo marked changes in primary open-angle glaucoma (POAG). These changes, as demonstrated previously, include loss and fragmentation of elastic fibers at the bottom of the glaucomatous cup and disorganization in the peripheral walls of the cup. The author characterized the changes in elastic fibers with age and in POAG at the ultrastructural level, using colloidal gold immunostaining and anti-human alpha-elastin antibody. In fetal eyes, there was no detectable elastin in the ECM of the lamina cribrosa. In infant eyes, elastin was present in microfibrillar aggregates in the core of the plates. In young adults, thin elastic fibers were present that ran longitudinally in the core of the plates. With age, elastic fibers become thicker, tubular, and surrounded by densely packed collagen fibers. In mild POAG, tubular elastic fibers no longer were identifiable. Fragments of elastic fibers and microfibrillar aggregates stained positively for elastin suggested new synthesis of elastin that was not organized into tubular elastic fibers. In advanced POAG, masses of nonfibrillar elastin-positive material had a spotted appearance. Throughout the cribriform plates, there was a loss of collagen fibers, proliferation of basement membranes, and bundles of elastin-negative microfibrils not associated with collagen or elastic fibers. The progression of marked changes in elastic fibers and the disorganization of the ECM of the lamina cribrosa was associated with the loss of function and continuous remodeling of the optic nerve head in POAG.

Adolescent↗

An immunohistochemical study of the collagens of rabbit synovial interstitium.

The interstitial pathway from joint cavity to synovial transport vessels contains a complex extracellular matrix. Rabbit knee synovial intima contains 3 fibrous elements--banded collagen fibrils, microfibrils and broad banded aggregates. The distribution of 4 types of collagen in rabbit knee synovium was investigated immunohistochemically. Types I and III collagens are both present, although the binding of anti-type I antibody was weak. Type V collagen, which forms thin fibrils, or is copolymerized with type I collagen, and type VI collagen, which forms broad banded aggregates and microfibrils, are widely distributed throughout the intimal and subintimal matrices.

Animals↗

Simulations of the static and dynamic molecular conformations of xyloglucan. The role of the fucosylated sidechain in surface-specific sidechain folding.

The hemicellulosic polysaccharide xyloglucan binds with a strong affinity to cellulosic cell wall microfibrils, the resulting heterogeneous network constituting up to 50% of the dry weight of the cell wall in dicotyledonous plants. To elucidate the molecular details of this interaction, we have performed theoretical potential energy calculations of the static and dynamic equilibrium conformations of xyloglucan using the GEGOP software. In particular, we have evaluated the preferred sidechain conformations of hexa-, octa-, deca- and heptadecasaccharide model fragments of xyloglucan for molecules with a cellulose-like, flat, glucan backbone, and a cellobiose-like, twisted, glucan backbone conformation. For the flat backbone conformation the determination of static equilibrium molecular conformations revealed a tendency for sidechains to fold onto one surface of the backbone, defined here as the H1S face, in the fucosylated region of the polymer. This folding produces a molecule that is sterically accessible on the opposite face of the backbone, the H4S face. Typically, this folding onto the H1S surface is significantly stabilized by favorable interactions between the fucosylated, trisaccharide sidechain and the backbone, with some stabilization from adjacent terminal xylosyl sidechains. In contrast, the trisaccharide sidechain folds onto the H4S face of xyloglucan fragments with a twisted backbone conformation. Preliminary NMR data on nonasaccharide fragments isolated from sycamore suspension-cultured cell walls are consistent with the hypothesis that the twisted conformation of xyloglucan represents the solution form of this molecule. Metropolis Monte Carlo (MMC) simulations were employed to assess sidechain flexibility of the heptadecasaccharide fragments. Simulations performed on the flat, rigid, backbone xyloglucan indicate that the trisaccharide sidechain is less mobile than the terminal xylosyl sidechains. MMC calculations on a fully relaxed molecule revealed a positive correlation between a specific trisaccharide sidechain orientation and the 'flatness' of the backbone glucosyl residues adjacent to this sidechain. These results suggest that the trisaccharide sidechain may play a role in the formation of nucleation sites that initiate the binding of these regions to cellulose. Based on these conformational preferences we suggest the following model for the binding of xyloglucan to cellulose. Nucleation of a binding site is initiated by the fucosylated, trisaccharide sidechain that flattens out an adjacent region of the xyloglucan backbone. Upon contacting a cellulose microfibril this region spreads by step-wise flattening of successive segments of the backbone. Self-association of xyloglucan molecules in solution may be prevented by the low frequency of formation of these nucleation sites and the geometry of the molecules in solution.

Carbohydrate Sequence↗

The glomerular filtration barrier of the kidney in seven vertebrates classes. Comparative morphological and histochemical observations.

In the mammalian kidney, the glomerular filtration barrier (GFB) is mostly composed of endothelial and epithelial cells with the glomerular basement membrane interposed. In lower vertebrates, extensive regions of the GFB consist of the endothelial and epithelial cells, each lying on its own basement membrane. These two basement membranes border the mesangium, which contains mesangial cells (surrounded by its own discontinuous basement membrane), microfibrils and collagens (cross-striated fibrils, anchoring fibrils, and 5 nm interfibrillar filaments). Occurrence and extension of these mesangial components decrease from fish to mammals. Anionic binding sites associated with the different structures of the GFB of all animal species have been demonstrated by using dyes such as Alcian blue (with or without addition of electrolytes), Ruthenium red or Safranine O. The surface coat of endothelial and epithelial cells, the laminae rarae (interna and externa) of the glomerular basement membrane, the laminae rara and diffusa (wherever distinct endothelial and epithelial basement membranes occurred) as well as the collagen fibrils show particles (with polycationic dyes) or filaments (with monocationic dyes). The mesangial microfibrils are usually well preserved and intensively stained.

Animals↗

[Ultrastructural findings of arachnoid cysts and epithelial cysts].

There may be several kinds of pathological conditions in the cystic lesion which are clinically diagnosed as benign intracranial cysts on CT scan. Light and electron microscopic studies on cyst walls were important in the differential diagnosis of benign intracranial cysts. We have studied 5 cases of intracranial arachnoid cysts and two epithelial cysts using the light and electron microscopy. Five cases of intracranial arachnoid cysts included two children and three adults (three females and two males). Three cases of them were localized in the middle cranial fossa, one case in the anterior and middle cranial fossa and one case in the lateral ventricle, giving headache and convulsion as the initial complaints. As for the epithelial cysts, one was localized at the para-collicular area complaining enlarged head and swollen anterior fontanelle and the other of four years was located in the fourth ventricle with headache and ataxic gait. On CT all of them demonstrated diffuse low density areas in both the arachnoid and the epithelial cysts without communicating findings between the cystic cavities and subarachnoid space on metrizamide CT cisternography. The arachnoid cyst walls were basically similar in structure to the normal arachnoid membrane and composed of elongated epithelial cells like the arachnoid cell and the connective tissues with lamellar collagen fiber bundles. However, 3 of the 5 cases had only fibrous tissues without epithelial cells. The inner sheath of the arachnoid cyst walls was composed of one or several layers of the arachnoid cells with flattened and relatively electron-dense cytoplasm on electron micrograph. They had a lot of elongated process and were tangled with each other, making large extracellular spaces between them. Below the electron dense arachnoid cells, compact packed cells with interdigitation partly demonstrated intercellular contacts such as numerous desmosomes and tight junctions. In those intercellular spaces collagen fibers and microfibrils were observed. The cells contained abundant cytoplasmic microfibrils and numerous organelles. They were separated from numerous collagen fibers and fibroblasts by non continuous basal lamina under the epithelial cells. Epithelial cyst wall had a layer of cuboidal or columnal epithelium in the inner layer of cyst wall. Those epithelial cells demonstrated granules having positive in PAS and mucicarmine stain in their cytoplasm. On electron microscopical study epithelial cells revealed a lot of microvilli and coating materials on the surface of them without cilia. The basement membranes were well developed under the epithelial cells separated from the connective tissues. In the intercellular clefts of the epithelial cells tight junctions and interdigitations were recognized.(ABSTRACT TRUNCATED AT 400 WORDS)

Adult↗

Elastic fiber components and protease inhibitors in pinguecula.

The nature of the abnormal elastotic materials seen in pingueculae and their insensitivity to elastase are poorly understood. The authors investigated their composition by immunoelectron microscopy using antibodies to elastic fiber components, serum and tissue components known to be associated with elastosis in other sites. The abnormal elastic fibers showed labeling for elastin, microfibrillar protein, and amyloid P where these components never co-localize normally, indicating the fibers are not simply immature but aberrant in organization. There was mild positivity for the serum protease inhibitor alpha-1 antitrypsin at the edges of the abnormal elastic tissue and marked positivity for lysozyme. The more superficial region of pingueculae had similar elastic constituents but no fiber formation and a paucity of elastic microfibrils. The subepithelial dense concretions showed strong staining for lysozyme, the first component to be identified in these aggregates. Amyloid P and lysozyme are characteristic components of dermal elastosis, postulated to have an inhibitory effect on elastolytic processes, indirectly affecting the control of elastogenesis. The greater prominence of nonfiber-forming aggregates in pingueculae may be related to their marked deficiency of elastic microfibrils compared with dermal elastoses. This difference speaks for more severe actinic cellular damage in the poorly protected conjunctival tissue.

Aged↗

Ultrastructural changes of the patellar tendon as a cruciate ligament substitute (one year and two year results).

In four black-faced sheep, the posterior cruciate ligament was replaced with a free autogenous patellar tendon transplant. Tissue samples from the transplants were investigated by light and electron microscopy 1 year and 2 years after surgery. The normal contralateral posterior cruciate ligament and the normal contralateral patellar tendon were used as controls. The structural differences concerned cells, collagen fibrils, elastic tissue and proteoglycans. Most of the cells of the contralateral patellar tendon were spindle-shaped, whereas those of the transplant were frequently chondroid. In the central region of the transplant as well as in the area far from the bone, cell degenerations, and occasionally hypo- or even acellular zones were found. Measurements of the diameter of collagen fibrils in both contralateral patellar tendon and posterior cruciate ligament showed a more or less pronounced bimodal distribution. A unimodal distribution with mainly thin fibrils (20-60 nm) was demonstrated in the transplant tissue which also revealed some morphological alterations of the collagen fibrils. Thin elastic fibers (microfibrils and amorphous material) were randomly scattered among the collagen fibrils of the control samples, bundles of microfibrils (without amorphous material) characterized the transplant. Staining with Alcian blue in the presence of 0.3 M MgCl2 demonstrated a close relationship between proteoglycans and collagen fibrils as well as elastic components in patellar tendon. This arrangement was lost in the transplant where abundant proteoglycans were revealed which, however, composed a tight irregular network between the collagen fibrils. The results serve as a baseline for understanding the impaired biochemical properties of a free autogenous patellar tendon transplant.

Animals↗

Transforming growth factor-beta 1 specifically localizes in elastin during synovial inflammation: an immunoelectron microscopic study.

We report here that extracellular TGF-beta 1 is associated exclusively with microfibrils of elastin which are present in the extracellular matrix of the inflamed articular joint of the rat. Inflammation was initiated by bacterial cell walls localized in the synovium following intraperitoneal injection of the bacterial components. This synovitis is associated with both destruction of connective tissue components and matrix deposition. The growth factor was localized by using a polyclonal antibody raised to a synthetic peptide corresponding to amino terminal 30 amino acids of TGF-beta 1 in conjunction with a gold-labeled secondary antibody. The results suggest a close association of TGF-beta 1 with proteoglycans which are known to be a major component of the microfibrils in elastin. Proteoglycan-mediated binding and concentration of TGF-beta 1 in specific areas of the extracellular matrix may constitute a mechanism whereby the growth factor could be targeted to specific sites of action.

Animals↗

Requirements of drug-induced endocytosis by intact human erythrocytes.

Study of drug-induced endocytosis in intact human erythrocytes continues to provide an opportunity for correlating membrane functions such as invagination and fusion with erythrocytic energetics and other determinants of plasma membrane function like Ca++. The studies reported indicate that high concentrations of vinblastine and chlorpromazine can produce endocytic vacuoles, albeit in reduced amounts, even in severely ATP depleted erythrocytes. In contrast, primaquine-induced endocytosis seems definitely dependent upon persistence of erythrocytic ATP stores. The ionophore mediated entry of Ca++ into erythrocytes potentiates primaquine endocytosis, inhibits vinblastine endocytosis, and has no regular effect on chlorpromazine endocytosis. Sodium lactate enhances primaquine endocytosis, probably by causing an increase in the entry of primaquine into erythrocytes. Cytochalasin B neither enhances nor inhibits erythrocytic endocytosis, thereby suggesting that microfibrils or analogues of microfibrils in erythrocytes are not involved in endocytosis. Cyclic nucleotide inhibition of endocytosis is confined to a very high concentration range of nucleotides in the medium. Primaquine and chlorpromazine endocytosis are inhibited by cyclic nucleotides as is vinblastine endocytosis.

Calcium↗

A fine structural localization of the non-specific cholinesterase activity in glomerular nerve formations (endings).

Snout glabrous skin (rhinarium) of the cat is innervated not only by typical simple lamellar corpuscles but also glomerular formations. In contrast to simple lamellar corpuscles, glomerular nerve formations are located away the dermal papillae. In cross sections, glomerular nerve formation consists of several axonal profiles enveloped by 1-2 cytoplasmic lamellae of Schwann cells. The space among them is filled by collagenous microfibrils and the basal lamina-like material. Capsule was composed from fibroblast-like cells without definite basal lamina. An electron-dense reaction product due to non-specific cholinesterase activity was associated with Schwann cells and their processes surrounding unmyelinated terminal portion of the sensory axons. Abundant reaction product was bound to the collagenous microfibrils and was deposited in extracellular matrix between Schwann cell processes. These results are further evidence for the presence of the non-specific cholinesterase molecules as integral component of the extracellular matrix in sensory corpuscles. On the basis of histochemical study two possible explanation are considered for functional involving of this enzyme in sensory nerve formations.

Animals↗