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PubMed2003

Vascular matrix remodeling in patients with bicuspid aortic valve malformations: implications for aortic dilatation.

BACKGROUND: Patients with bicuspid aortic valve malformations are at an increased risk of aortic dilatation, aneurysm formation, and dissection. Vascular tissues with deficient fibrillin-1 microfibrils release matrix metalloproteinases, enzymes that weaken the vessel wall by degrading elastic matrix components. In bicuspid aortic valve disease a deficiency of fibrillin-1 and increased matrix metalloproteinase matrix degradation might result in aortic degeneration and dilatation. METHODS: Samples of the pulmonary artery and aorta were obtained from surgical patients with bicuspid aortic valves (n = 21) and tricuspid aortic valves (n = 16). RESULTS: Fibrillin-1 content was reduced in bicuspid aortic valve aortas compared with that seen in tricuspid aortic valve aortas (P =.001), whereas the associated matrix components, elastin and collagen, were unchanged (P =.51 and P =.21). Reductions of aortic fibrillin-1 content were independent of valve function and patient age. Compared with tricuspid aortic valve aorta, matrix metalloproteinase 2 activity was increased more than 2-fold in bicuspid aortic valve aortas (P =.04) and correlated positively with aortic diameter (r = 0.74, P =.05). Matrix metalloproteinase 9 activity was not significantly different. Fibrillin-1 content was also reduced in the pulmonary arteries of patients with bicuspid aortic valves (P =.06), suggesting a systemic deficiency of fibrillin-1. Promatrix metalloproteinase 2 was increased (P =.04), reflecting an increased production of matrix metalloproteinase 2 in these fibrillin-1-deficient tissues, whereas active matrix metalloproteinase 2 and matrix metalloproteinase 9 species were unchanged, and correspondingly, the pulmonary arteries were not dilated. CONCLUSIONS: Deficient fibrillin-1 content in the vasculature of patients with bicuspid aortic valves might trigger matrix metalloproteinase production, leading to matrix disruption and dilatation. This process of vascular matrix remodeling in patients with bicuspid aortic valves offers novel therapeutic targets to prevent the aortic degeneration and dilatation characteristic of this disease.

Adult↗
PubMed1983

Light microscopy, electron microscopy, and X-ray diffraction analysis of glycerinated collagen fibers.

Light microscopy, transmission electron microscopy (freeze-fracture replicas and thin sections), and X-ray diffraction techniques were used to investigate the structure of rat tail tendon collagen fibers subjected to one of the following treatments: water, phosphate buffer, glutaraldehyde, glutaraldehyde followed by glycerol, glycerol, and glycerol followed by phosphate buffer. As seen by light microscopy, only treatment with glycerol induces a remarkable swelling of the native (untreated) collagen specimens. Replicas and thin sections show that this swelling is due to an expansion of the interfibrillar space, and to a dissociation of the collagen fibrils into microfibrils. X-Ray diffraction analysis reveals great disorder in the glycerol-swollen collagen fibers. However, this does not appreciably involve the microfibrillar and molecular structure. Light and electron microscopy as well as X-ray diffraction techniques show that the collagen fiber swelling induced by glycerol is an almost completely reversible process.

Animals↗
PubMed2001

Reassessment of qualitative changes in lignification of transgenic tobacco plants and their impact on cell wall assembly.

In tobacco plants the effect of antisense down-regulation of various genes encoding enzymes of the monolignol biosynthetic pathway resulted in quantitative and qualitative changes in lignin distribution and in diverse alterations of the secondary wall assembly of modified tobacco plants. Total lignin content, composition in syringyl and guaiacyl units, and absolute proportions of condensed and non-condensed substructures occurring in the cell walls, were differentially modified according to the repressed gene. Immunocytochemical characterisation and visualisation of the distribution of condensed and non-condensed lignin substructure epitopes in transmission electron microscopy (TEM) revealed that some transformations entailed profound and specific alterations in the secondary wall biogenesis. Correlation between micro-morphological cell wall alterations and semi-quantitative immuno-analysis of the topochemical distribution of lignin sub-units suggests that the mode of polymerisation of monolignols into non-condensed units, favoured by the microfibril matrix of the secondary wall, plays an important part in the lignified cell wall assembly.

Cell Wall↗
PubMed2002

Structure of cellulose-deficient secondary cell walls from the irx3 mutant of Arabidopsis thaliana.

In the Arabidopsis mutant irx3, truncation of the AtCesA7 gene encoding a xylem-specific cellulose synthase results in reduced cellulose synthesis in the affected xylem cells and collapse of mature xylem vessels. Here we describe spectroscopic experiments to determine whether any cellulose, normal or abnormal, remained in the walls of these cells and whether there were consequent effects on other cell-wall polysaccharides. Xylem cell walls from irx3 and its wild-type were prepared by anatomically specific isolation and were examined by solid-state NMR spectroscopy and FTIR microscopy. The affected cell walls of irx3 contained low levels of crystalline cellulose, probably associated with primary cell walls. There was no evidence that crystalline cellulose was replaced by less ordered glucans. From the molecular mobility of xylans and lignin it was deduced that these non-cellulosic polymers were cross-linked together in both irx3 and the wild-type. The disorder previously observed in the spatial pattern of non-cellulosic polymer deposition in the secondary walls of irx3 xylem could not be explained by any alteration in the structure or cross-linking of these polymers and may be attributed directly to the absence of cellulose microfibrils which, in the wild-type, scaffold the organisation of the other polymers into a coherent secondary cell wall.

Arabidopsis↗
PubMed1990

Role of elastic fiber degradation in emphysema-like lesions of pulmonary lymphangiomyomatosis.

To study the pulmonary structural remodeling in pulmonary lymphangiomyomatosis, electron microscopy and light and electron microscopic immunohistochemical observations for elastin and alpha 1-antitrypsin were performed on five open lung biopsy samples. Lung specimens showed emphysema-like changes in areas of abnormally accumulated smooth muscle cells. In the alveolar walls having accumulated smooth muscle cells, elastic fibers were decreased in number, disrupted, granular, and occasionally accumulated. Ultrastructurally, elastic fibers in areas of smooth muscle cell accumulation showed poorly outlined amorphous components and a few microfibrils, and occasionally showed electron-dense granular deposits in and around the amorphous components. Spiraling collagen fibrils were frequently found associated with these abnormal elastic fibers. Immunohistochemistry for elastin showed even staining of amorphous components of elastic fibers in the areas of smooth muscle cell accumulation. alpha 1-Antitrypsin was also detected evenly in amorphous components of elastic fibers in the areas of smooth muscle cell accumulation. It is proposed that the emphysema-like lesions of lymphangiomyomatosis are mediated by the degradation of elastic fibers, and these degraded elastic fibers are related to an imbalance of the elastase/alpha 1-antitrypsin system similar to the probable pathogenesis of emphysema.

Adult↗
PubMed1976

The carcinoid endocardial plaque; an ultrastructural study.

Ultrastructural studies disclosed that the plaque-like endocardial thickenings in three patients with the carcinoid syndrome were composed of smooth muscle cells embedded in a stroma that was rich in acid mucopolysaccharides, collagen, and microfibrils, but devoid of elastic fibers. The smooth muscle cells contained variable numbers of myofilaments and cisterns of rough surfaced endoplasmic reticulum, and their basement membranes were greatly thickened, reduplicated, and arranged in layers. The endocardial plaques appeared histologically and ultrastructurally similar regardless of their location in the heart. The smooth muscle cells in these plaques appear to have been derived from primitive mesenchymal cells, which normally are present in the subendocardial endothelial space. These observations are interpreted as indicating that the plaques develop as a result of healing of a superficial endocardial injury, which may be initiated by release of bradykinin from hepatic metastases of a carcinoid tumor.

Endocardium↗
PubMed1981

Bilateral malignant Brenner tumor: report of a case with ultrastructural study.

An unusual case of bilateral malignant Brenner tumor with liver and omental metastases is reported. The tumor was histologically a transitional cell carcinoma comparable to a grade III bladder carcinoma. A benign component was not identified, but there were a few nests of malignant epithelial cells distributed in a dense stroma, a pattern identical to that seen in a benign Brenner tumor. Whether this represents malignant change in a previously benign focus or a well differentiated part of a de novo carcinoma is unclear. Nevertheless it is suggested that the current histologic criteria for malignant Brenner tumor be modified to exclude the requirement of an intimately associated benign Brenner tumor. Ultrastructurally the malignant Brenner tumor has many features of the benign Brenner tumor. Some features, notably the basal lamina, micropinocytotic vesicles, nd intracytoplasmic microfibrils, are herein described for the first time in a malignant Brenner tumor.

Aged↗
PubMed1983

Clear cell sarcoma of tendons and aponeuroses: electron microscopic findings suggesting Schwann cell differentiation.

A case of clear cell sarcoma of tendons and aponeuroses arising in the elbow of a young woman is reported. Local recurrence and lymph node metastases occurred despite radiation therapy, chemotherapy, and amputation of the right arm, and the patient died of the tumor approximately ten months after the initial diagnosis. Although melanin was not observed histologically, electron microscopic studies revealed immature melanosomes. In addition, well-developed and duplicated basement membranes, and abundant intracytoplasmic microfibrils suggested melanotic Schwann cell differentiation. On sections stained immunohistochemically, S-l00 protein was present focally. The six previously reported cases of clear cell sarcoma studied electron microscopically are reviewed.

Adult↗
PubMed1985

Glomerular matrix proteins in nodular glomerulosclerosis in association with light chain deposition disease and diabetes mellitus.

The diagnosis of light chain deposition nephropathy is based on the immunohistochemical demonstration of monoclonal light chain deposits within connective tissue matrix and on the presence at the ultrastructural level of electron-dense granular deposits along glomerular and tubular basement membranes. A nodular glomerulopathy characterized by amorphous periodic acid-Schiff-positive and argyrophilic widened mesangium and nodules is described in three patients with light chain deposition nephropathy. Light microscopic examination did not allow discrimination between the glomerular changes found in these specimens and the nodular glomerulosclerosis described in four patients with well-documented diabetes mellitus. Electron microscopic examination revealed microtubular fibrils 10 to 12 nm thick in mesangial areas in both groups. Such microfibrils could be glycoproteins. Immunofluorescence localization of matrix proteins, by staining with affinity-purified antibodies to types I, III, IV, and V (A, B) collagens, fibronectin, laminin, and heparan sulfate-containing proteoglycans, showed similar distributions in the two conditions. The mechanism of this abnormal accumulation of mesangial and glomerular basement membrane matrix proteins in two different conditions remains unknown.

Basement Membrane↗
PubMed1990

Recovery of non-specific cholinesterase activity in sensory corpuscles of mouse toe skin after irreversible inhibition of this enzyme and cold injury.

Mouse digital corpuscles, located in the dermal papillae of toe pad skin, consist of the sensory axon terminals enveloped by the cytoplasmic processes of Schwann-derived cells forming the so-called inner core. The inner core cells are capable to synthetize nCHE molecules which are released into the interlamellar spaces filled by the basal lamina, collagenous microfibrils, and amorphous matrix. In the present study, the histochemical detection of the nCHE activity was investigated in the sensory corpuscles after sciatic and saphenous nerve transections and subsequent application of irreversible nCHE inhibitor (iso-OMPA) or cryo-treatment of toe pad skin. The recovery of the nCHE reaction product in both intact and denervated corpuscles revealed the resynthesis of the nCHE molecules by the inner core cells without assistance of sensory terminals, as well. The cellular constituents of corpuscles were degraded while extracellular matrix appeared to be undamaged after freezing injury. The molecules of nCHE attached to the extracellular matrix components disappeared in coincidence with the disintegration of Schwann-derived cells. After about 5 d of survival, the Schwann cells exhibiting the nCHE reactivity migrated through the basal lamina tubes as guidance of regrowing axons or alone. After 7 d from the treatment, immature Schwann cells marked by the nCHE reaction product occupied the scaffolds of old damaged sensory corpuscles. During further days of surviving, the Schwann cells entering the extracellular matrix of degraded corpuscles were differentiated to the inner core cells. The re-differentiation of the Schwann cells into the inner core cells was observed not only in the presence but also in the absence of sensory terminals. These findings suggest certain trophic independence of inner core cells upon sensory terminals in the sensory corpuscles of adult animals.

Animals↗
PubMed1978

The distribution of disulfide-groups in Descemet's membrane, lens capsule, and zonular fibers.

Zonular fibers contain large quantities of disulfide-groups which histochemically can be demonstrated after thiosulfation or reduction with sodium thioglycollate. Zonular fibers share these staining behaviours with oxytalan fibers and elastic fiber microfibrils. Smaller amounts of disulfide-groups can be demonstrated when visualized by means of the thioglycollate/ferric-ferricyanide method. Diffusion of acidic staining solutions seems to be limited in Descemet's membrane and in the lens capsule: only surfaces of these membranes become reactive after thiosulfation. It is assumed that the distribution of disulfide-groups in Descemet's membrane and in the lens capsule shows the distribution of type IV collagen.

Animals↗
PubMed1998

Extracellular matrix-associated transforming growth factor-beta: role in cancer cell growth and invasion.

Growth factors of the transforming growth factor-beta (TGF-beta) family inhibit the proliferation of epithelial, endothelial, and hematopoietic cells, and stimulate the synthesis of extracellular matrix components. TGF-beta s are secreted from cells in high-molecular-mass protein complexes that are composed of three proteins, the mature TGF-beta-dimer, the TGF-beta propeptide dimer, or latency-associated protein (LAP), and the latent TGF-beta binding protein (LTBP). Mature TGF-beta is cleaved from its propeptide during secretion, but the proteins remain associated by noncovalent interactions. LTBP is required for efficient secretion and processing of latent TGF-beta and it binds to LAP via disulfide bond(s). LTBP is a component of extracellular matrix microfibrils, and it targets the latent TGF-beta complex to the extracellular matrix. TGF-beta signaling is initiated by proteolytic cleavage of LTBP that results in the release of the latent TGF-beta complex from the extracellular matrix. TGF-beta is activated by dissociation of LAP from the mature TGF-beta. Subsequent signaling involves binding of active TGF-beta to its type II cell surface receptors, which phosphorylate and activate type I TGF-beta receptors. Type I receptors, in turn, phosphorylate cytoplasmic transcriptional activator proteins Smad2 and Smad3, inducing their translocation to the nucleus. Recent evidence suggests that acquisition of resistance to TGF-beta growth inhibition plays a major role in the progression of epithelial and hematopoietic cell malignancies. The role of secretion of TGF-beta in tumorigenesis is more complex. The secretion of TGF-beta s by tumor cells may contribute to autocrine growth inhibition, but on the other hand, it may also promote invasion, metastasis, angiogenesis, and even immunosuppression. Tumor cells may also fail to deposit LTBP:TGF-beta complexes to the extracellular matrix. The elucidation of the mechanisms of the release of TGF-beta from the matrix and its subsequent activation aids the understanding of the pathophysiologic roles of TGF-beta in malignant growth, and allows the development of therapeutic agents that regulate the activity of TGF-beta.

Cell Division↗
PubMed2005

Fibrous proteins: new structural and functional aspects revealed.

Coiled-coil proteins, collagen, and elastomers together comprise an important subset of the fibrous proteins. The former group-the alpha-fibrous coiled-coil proteins-are widely distributed in nature and, indeed, the characteristic heptad motif has been recognized as an oligomerisation motif in fibril-forming collagens. This volume has selected a number of the alpha-fibrous proteins for detailed discussion, including intermediate filament proteins, the spectrin superfamily, and fibrin?fibrinogen. Of particular interest is the growing realization that the design principles governing the structures of these coiled-coil proteins are now largely discernible and can be specified with a high degree of confidence, due in large part to the wealth of crystal structure data now available. Within the connective tissues covered in this volume, two constituents of defining importance mechanically are the collagen fibrils?networks and the elastic fibers. Crystal structures of collagen peptides have been published and are described. The effects of the precise sequence of the distinct constituent triplets on molecular conformation have also become clearer. The ultrastructures of connective tissues are largely defined by the spatial arrangement of the collagen fibrils and networks, and this is elucidated here in some detail. The elastic fibers with their elastin cores and fibrillin-containing microfibril palisades are also described. A theme underlying all of the proteins discussed in this volume is the significantly increased effort to characterize the structures and functions of mutants. Some of these occur naturally and lead to various disease states, while others have been genetically engineered in order to study design principles.

Connective Tissue↗
PubMed2005

Collagen fibril form and function.

The majority of collagen in the extracellular matrix is found in a fibrillar form, with long slender filaments each displaying a characteristic approximately 67?nm D-repeat. Here they provide the stiff resilient part of many tissues, where the inherent strength of the collagen triple helix is translated through a number of hierarchical levels to endow that tissue with its specific mechanical properties. A number of collagen types have important structural roles, either comprising the core of the fibril or decorating the fibril surface to give enhanced functionality. The architecture of subfibrillar and suprafibrillar structures (such as microfibrils), lateral crystalline and liquid crystal ordering, interfibrillar interactions, and fibril bundles is described. The fibril surface is recognized as an area that contains a number of intimate interactions between different collagen types and other molecular species, especially the proteoglycans. The interplay between molecular forms at the fibril surface is discussed in terms of their contribution to the regulation of fibril diameter and their role in interfibrillar interactions.

Animals↗
PubMed2002

Dynamic changes and the role of the cytoskeleton during the cell cycle in higher plant cells.

In higher plant cells microtubules (MTs) show dynamic structural changes during cell cycle progression and play significant roles in cell morphogenesis. The cortical MT (CMT), preprophase band (PPB), and phragmoplast, all of which are plant-specific MT structures, can be observed during interphase, from the late G2 phase to prophase, and from anaphase to telophase, respectively. The CMT controls cell shape, either irreversibly or reversibly, by orientating cellulose microfibril (CMF) deposition in the cell wall; the PPB is involved in determining the site of division; and the phragmoplast forms the cell plate at cytokinesis. The appearance and disappearance of these MT structures during the cell cycle have been extensively studied by immunofluorescence microscopy using highly synchronized tobacco BY-2 cells. Indeed, these studies, together with visualization of MT dynamics in living plant cells using the green fluorescent protein, have revealed much about the modes of MT structural organization, for example, of CMTs at the M/G1 interphase. The microfilaments which also show dynamic changes during the cell cycle, being similar to MTs at particular stages and different at other stages, appear to play roles in supporting MTs. In this article, we summarize our ongoing research and that of related studies of the structure and function of the plant cytoskeleton during cell cycle progression.

Actin Cytoskeleton↗
PubMed1997

The role of endoxyloglucan transferase in the organization of plant cell walls.

The plant cell wall plays a central role in morphogenesis as well as responsiveness to environmental signals. Xyloglucans are the principal component of the plant cell wall matrix and serve as cross-links between cellulose microfibrils to form the cellulose-xyloglucan framework. Endoxyloglucan transferase (EXGT), which was isolated and characterized in 1992, is an enzyme that mediates molecular grafting reaction between xyloglucan molecules. Structural studies on cDNAs encoding EXGT and its related proteins have disclosed the ubiquitous presence in the plant kingdom of a large multigene family of xyloglucan-related proteins (XRPs). Each XRP functions as either hydrolase or transferase acting on xyloglucans and is considered to be responsible for rearrangement of the cellulose-xyloglucan framework, the processes essential for the construction, modification, and degradation of plant cell walls. Different XRP genes exhibit potentially different expression profiles with respect to tissue specificity and responsiveness to hormonal and mechanical signals. The molecular approach to individual XRP genes will open a new path for exploring the controlling mechanisms by which the plant cell wall is constructed and reformed during plant growth and development.

Amino Acid Sequence↗
PubMed1996

Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders.

The nuclear magnetic resonance structure of a covalently linked pair of calcium-binding (cb) epidermal growth factor-like (EGF) domains from human fibrillin-1, the protein defective in the Marfan syndrome, is described. The two domains are in a rigid, rod-like arrangement, stabilized by interdomain calcium binding and hydrophobic interactions. We propose a model for the arrangement of fibrillin monomers in microfibrils that reconciles structural and antibody binding data, and we describe a set of disease-causing mutations that provide the first clues to the specificity of cbEFG interactions. The residues involved in stabilizing the domain linkage are highly conserved in fibrillin, fibulin, thrombomodulin, and the low density lipoprotein receptor. We propose that the relative orientation of tandem cbEGF domains in these proteins is similar, but that in others, including Notch, pairs adopt a completely different conformation.

Calcium-Binding Proteins↗