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PubMed2006

Mesopore structure of microcrystalline cellulose tablets characterized by nitrogen adsorption and SEM: the influence on water-induced ionic conduction.

Tablets of microcrystalline cellulose were formed at different compaction pressures and physical properties, such as pore size distribution, surface area, and pore surface fractality, were extracted from N2 adsorption isotherms. These properties were compared to previously published data on the water-induced ionic conductivity of the tablets. The conduction process was shown to follow a percolation model with a percolation exponent of 2 and a porosity percolation threshold of approximately 0.1. The critical pore diameter for facilitated charge transport was shown to be in the 5-20 nm range. When the network of pores with a diameter in this interval is reduced to the point where it no longer forms a continuous passageway throughout the compact, the conduction process is dominated by charge transport on the surfaces of individual microfibrils mainly situated in the bulk of fibril aggregates. A fractal analysis of nitrogen adsorption isotherms showed that the dominant interface forces during adsorption is attributed to surface tensions between the gas and the adsorbed liquid phase. The extracted fractal dimension of the analyzed pore surfaces remained unaffected by the densification process at low compaction pressures (< approximately 200 MPa). At increased densification, however, pore-surface structures smaller than approximately 100 nm become smoother as the fractal dimension decreases from approximately 2.5 at high porosities to approximately 2.3 for the densest tablets under study.

Adsorption↗
PubMed2004

Is the wall of a cellulose fiber saturated with liquid whether or not permeable with CO2 dissolved molecules? Application to bubble nucleation in champagne wines.

In this paper, the transversal diffusion coefficient D perpendicular of CO2 dissolved molecules through the wall of a hydrated cellulose fiber was approached, from the liquid bulk diffusion coefficient of CO2 dissolved molecules modified by an obstruction factor. The porous network between the cellulose microfibrils of the fiber wall was assumed being saturated with liquid. We retrieved information from previous NMR experiments on the self-diffusion of water in cellulose fibers to reach an order of magnitude for the transversal diffusion coefficient of CO2 molecules through the fiber wall. A value of about D perpendicular approximately 0.2D0 was proposed, D0 being the diffusion coefficient of CO2 molecules in the liquid bulk. Because most of bubble nucleation sites in a glass poured with carbonated beverage are cellulose fibers cast off from paper or cloth which floated from the surrounding air, or remaining from the wiping process, this result directly applies to the kinetics of carbon dioxide bubble formation from champagne and sparkling wines. If the cellulose fiber wall was impermeable with regard to CO2 dissolved molecules, it was suggested that the kinetics of bubbling would be about three times less than it is.

Journal Article↗
PubMedDate not supplied

The structure of alpha-keratin.

Known structural principles (close packing, maximum hydrogen bonding, the tendency of like groups to be surrounded in like manner, and the approximate constancy of interatomic distances and bond angles) are used, with meridional and equatorial x-ray data, to deduce and check the structure pattern for alpha-keratin. Internally hydrogen-bonded polypeptide helices are grouped into "3-stacks", in which each chain is rotated and shifted vertically a distance equal to the helix pitch (5.15 A, average), relative to the other two. This shift accounts simply for the meridional x-ray reflection at this spacing. The 3-stack structure repeats after three turns, except for differences in the R groups and a slight twist, required to give satisfaction of both intrachain and interchain forces. The 3-stacks are grouped into 9-stacks and these into 27-stacks (all twisting), giving a crystallographic unit containing 81 chains, with the chain axes spaced approximately like those of close-packed cylinders. When the twisting reaches the limit of stability for good interchain contacting and cross-linking, the residue/turn ratio in each chain helix shifts to another, with twisting in the opposite direction. The twisting reversal mechanism keeps all the helix axes approximately straight, parallel, and in a close-packed arrangement. Interchain distances and orientations are suitable for cystine cross-linking. The dimensions of the 27-stacks agree well with estimates of the "effective radius" of microfibrils. X-ray measurements of spacing changes during fiber extension are explained as due to alternation of zones with much cross-linking and zones with few cross-links.

Chemical Phenomena↗
PubMed1999

A novel E-type endo-beta-1,4-glucanase with a putative cellulose-binding domain is highly expressed in ripening strawberry fruits.

Two full-length cDNA clones (faEG1 and faEG3, respectively) have been isolated by screening a cDNA library representing transcripts from red strawberry fruits. Southern blot analysis of genomic DNA suggests that the strawberry endo-beta-1,4-glucanases (EGases) are encoded by a multigene family. The cognate genes are predominantly expressed during the ripening process proper, although, in the case of faEG3, some expression has also been observed in large green fruits and, at low amounts, in young vegetative green tissues. In agreement with other ripening-related genes in strawberry, also the expression of faEG1 and faEG3 is down-regulated by treatment with an auxin analogue (1-naphthaleneacetic acid, NAA). Differences in temporal expression of the two EGase genes in fruits are not accompanied by differences in spatial expression. The pattern of expression and the sequence characteristics of the two polypeptides suggest that the two strawberry EGases operate in a synergistic and coordinate manner. The protein encoded by faEG1 looks like one of the usual higher-plant EGases (average molecular mass of 54 kDa), while the protein encoded by faEG3 has a greater deduced molecular mass (about 68 kDa) due to the presence of an extra peptide of about 130 amino acids at the C-terminus. Such unusual peptide shows some features also found in microbial cellulases and contains a putative cellulose-binding domain. We propose that the faEG3-encoded EGase might especially hydrolyse the xyloglucans coating the cellulose microfibrils, thus rendering the cell wall more susceptible to the subsequent hydrolytic activity of the faEG1-encoded EGase.

Amino Acid Sequence↗
PubMed1998

Expression of a wool intermediate filament keratin transgene in sheep fibre alters structure.

Alteration of the protein composition of the wool fibre via transgenesis with sheep wool keratin and keratin associated protein (KAP) genes may lead to production of fibre types with improved processing and wearing qualities. Using this approach, we have demonstrated that high level cortical-specific expression of a wool type II intermediate filament (IF) keratin gene, K2.10, leads to marked alterations in both the microstructure and macrostructure of the wool fibres, which have higher lustre and reduced crimp. Analysis of mRNA found reduced levels of transcripts from endogenous cortical type I (p < 0.05) and type II (p < 0.01) keratin IF genes and from the KAP8 (p < 0.001) and KAP2 (p < 0.01) gene families. Examination of protein composition revealed an altered ratio in the keratin type II protein family of the wool fibre cortex. Whilst the over-expressed K2.10 transgene product constituted the majority of keratin type II IF protein, it appeared unable to form heterodimers with much of the expressed endogenous keratin type I IF. In comparison with non-transgenic sheep, fewer IF microfibrils were visible in the cortical cells of fibres from transgenics. The combined effect on fibre structure was disruption of the formation of orthocortical and paracortical cells in the fibre cortex, a factor which could account for the reduction in fibre crimp. No effects upon transcript or protein levels, or fibre microstructure or macrostructure were observed in transgenic sheep expressing the transgene at lower levels, indicating that subtle changes to the gene expression profile in sheep wool follicles can be tolerated. The data here also illustrate that control over endogenous transcript levels in the cortex results when factors acting on the endogenous keratin type I, keratin type II and KAP gene sequences are sequestered by the active K2.10 transgene locus. Moreover, interference to a transcriptional hierarchy shared by keratin and KAP genes may occur prior to establishment of the orthocortical and paracortical compartments of the follicle cortex, at the level of the chromatin.

Animals↗
PubMed2000

Structure of the tendon connective tissue.

Tendons consist of collagen (mostly type I collagen) and elastin embedded in a proteoglycan-water matrix with collagen accounting for 65-80% and elastin approximately 1-2% of the dry mass of the tendon. These elements are produced by tenoblasts and tenocytes, which are the elongated fibroblasts and fibrocytes that lie between the collagen fibers, and are organized in a complex hierarchical scheme to form the tendon proper. Soluble tropocollagen molecules form cross-links to create insoluble collagen molecules which then aggregate progressively into microfibrils and then into electronmicroscopically clearly visible units, the collagen fibrils. A bunch of collagen fibrils forms a collagen fiber, which is the basic unit of a tendon. A fine sheath of connective tissue called endotenon invests each collagen fiber and binds fibers together. A bunch of collagen fibers forms a primary fiber bundle, and a group of primary fiber bundles forms a secondary fiber bundle. A group of secondary fiber bundles, in turn, forms a tertiary bundle, and the tertiary bundles make up the tendon. The entire tendon is surrounded by a fine connective tissue sheath called epitenon. The three-dimensional ultrastructure of tendon fibers and fiber bundles is complex. Within one collagen fiber, the fibrils are oriented not only longitudinally but also transversely and horizontally. The longitudinal fibers do not run only parallel but also cross each other, forming spirals. Some of the individual fibrils and fibril groups form spiral-type plaits. The basic function of the tendon is to transmit the force created by the muscle to the bone, and, in this way, make joint movement possible. The complex macro- and microstructure of tendons and tendon fibers make this possible. During various phases of movements, the tendons are exposed not only to longitudinal but also to transversal and rotational forces. In addition, they must be prepared to withstand direct contusions and pressures. The above-described three-dimensional internal structure of the fibers forms a buffer medium against forces of various directions, thus preventing damage and disconnection of the fibers.

Collagen↗
PubMed1979

Electron microscope evidence for an 80 A unit in collagen fibrils.

Connective tissues are composite structures containing collagen, elastin, glycosaminoglycans, minerals, water and other minor components. In all cases the collagen exists predominantly in fibrillar form. The size distribution of the fibrils does, however, vary markedly with both age and the mechanical requirements of the tissue. Little is known about the mechanism of fibril formation in vivo, although some information is now available form in vitro polymerisation studies. We have now collected new and extensive electron microscope data on the size of collagen fibrils from tendon, skin, cornea and other tissues from both fetal and immature animals. The results reported here show that the diameters of the collagen fibrils thus measured lie close to a multiple of 80 A, a result which may be simply and readily interpreted in terms of the collagen microfibril and its mode of packing.

Animals↗
PubMed1980

Direct observation of a transverse periodicity in collagen fibrils.

Collagen fibrils have been extensively studied by electron microscopy, but only scant evidence has yet been obtained about their transverse structure. A transverse pediodicity of about 40 or 80 A might be expected if the microfibril model (until recently the common preference) is correct, but little direct evidence for such a periodicity has been obtained so far. We have studied electron micrographs of longitudinal cryosections of rat tail tendon. These appear very fibrous when studied by eye, but they produce at best only diffuse equatorial peaks in optical diffraction patterns. Nevertheless, we show here that like other fibrous protein structures, they do possess a strong transverse periodicity as revealed by their self-convolution functions (or auto-correlation functions). The observed periodicity is consistent with the presence of an 80 A structural unit in collagen fibrils in vivo.

Animals↗
PubMedDate not supplied

Helical microtubular arrays in onion root hairs.

The higher order patterns to which individual plant microtubules contribute are not yet fully described, perhaps because of the problems of reconstructing whole-cell conformations from electron microscope (EM) thin sections. Because microtubules may govern the way in which cellulose microfibrils are deposited in the plant cell wall, it is important to determine the range of permissible conformations for this has implications for the understanding of wall texture. Often, but not always, the EM shows that microtubules occur roughly transversely to the plant cell's long axis and they are usually conceived of as contributing to a series of 'hoops'. However, based on evidence that microtubules can be long relative to the cell's circumference and on the interconnected nature of the cytoskeleton, it was recently proposed that microtubules might be wound helically around the cell; the helical pitch being influenced by the expansion characteristics of the cell. By using whole-cell immunofluorescence and monoclonal antibodies to tubulin, evidence is now presented which confirms that unambiguous helices occur in formaldehyde-fixed onion root hairs.

Cell Wall↗
PubMed1991

Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes.

Marfan syndrome (MFS), one of the most common genetic disorders of connective tissue, is characterized by skeletal, cardiovascular and ocular abnormalities. The incidence of the disease is about 1 in 20,000, with life expectancy severely reduced because of cardiovascular complications. As the underlying defect is unknown, MFS diagnosis is based solely on clinical criteria. Certain phenotypic features of MFS are also shared by other conditions, which may be genetically distinct entities although part of a clinical continuum. Immunohistochemical studies have implicated fibrillin, a major component of elastin-associated microfibrils, in MFS aetiology. Genetic linkage analysis with random probes has independently localized the MFS locus to chromosome 15. Here we report that these two experimental approaches converge with the cloning and mapping of the fibrillin gene to chromosome 15q15-21, and with the establishment of linkage to MFS. We also isolated a second fibrillin gene and mapped it to chromosome 5q23-31. We linked this novel gene to a condition, congenital contractural arachnodactyly, that shares some of the features of MFS. Thus, the cosegregation of two related genes with two related syndromes implies that fibrillin mutations are likely to be responsible for different MFS phenotypes.

Amino Acid Sequence↗
PubMed1991

Marfan syndrome caused by a recurrent de novo missense mutation in the fibrillin gene.

Marfan syndrome is an inherited disorder of connective tissue manifested in the ocular, skeletal and cardiovascular systems. It is inherited as an autosomal dominant with high penetrance, but has great clinical variability. Linkage studies have mapped the Marfan locus to chromosome 15q15-21.3. There have been no reports of genetic heterogeneity in the syndrome. Following the identification of fibrillin (a glycoprotein component of the extracellular microfibril), immunohistopathological quantification of the protein in skin and fibroblast culture, and examination of fibrillin synthesis, extracellular transport, and incorporation into the extracellular matrix (D. M. Milewicz, R.E.P., E. S. Crawford and P. H. Byers, manuscript in preparation) have demonstrated abnormalities of fibrillin metabolism in most patients. A portion of the complementary DNA encoding fibrillin has been cloned and mapped by in situ hybridization to chromosome 15. Here we report that the fibrillin gene is linked to the Marfan phenotype (theta = 0.00; logarithm of the odds (lod) = 3.9) and describe a de novo missense mutation in the fibrillin gene in two patients with sporadic disease. We thus implicate fibrillin as the protein defective in patients with the Marfan syndrome.

Adult↗
PubMed2002

Fibulin-5/DANCE is essential for elastogenesis in vivo.

The elastic fibre system has a principal role in the structure and function of various types of organs that require elasticity, such as large arteries, lung and skin. Although elastic fibres are known to be composed of microfibril proteins (for example, fibrillins and latent transforming growth factor (TGF)-beta-binding proteins) and polymerized elastin, the mechanism of their assembly and development is not well understood. Here we report that fibulin-5 (also known as DANCE), a recently discovered integrin ligand, is an essential determinant of elastic fibre organization. fibulin-5-/- mice generated by gene targeting exhibit a severely disorganized elastic fibre system throughout the body. fibulin-5-/- mice survive to adulthood, but have a tortuous aorta with loss of compliance, severe emphysema, and loose skin (cutis laxa). These tissues contain fragmented elastin without an increase of elastase activity, indicating defective development of elastic fibres. Fibulin-5 interacts directly with elastic fibres in vitro, and serves as a ligand for cell surface integrins alphavbeta3, alphavbeta5 and alpha9beta1 through its amino-terminal domain. Thus, fibulin-5 may provide anchorage of elastic fibres to cells, thereby acting to stabilize and organize elastic fibres in the skin, lung and vasculature.

Animals↗
PubMed1979

Urinary matrix calculi consisting of microfibrillar protein in patients on maintenance hemodialysis.

In seven patients on maintenance hemodialysis, de novo recurrent renal stone formation was observed. In all patients, the underlying disease was glomerulonephritis, with or without the nephrotic syndrome. All patients had considerable persistent proteinuria. The stones consisted predominantly of protein, as revealed by amino acid analysis, and had a negligible carbohydrate and lipid content. Only in some specimens, X-ray diffraction and scanning electron microscopy revealed the presence of small amounts of whewellit (calcium oxalate monohydrate) and/or uric acid. In semithin sections, the stones had a laminated texture and exhibited structural anisotropy under polarized light. With transmission electron microscopy, they were found to consist of peculair microfibrils. The proteinaceous material differed from fibrin or Tamm-Horsfall-protein, as indicated by ultrastructure, carbohydrate analysis, and amino acid analysis. Symptomatic de novo matrix stone formation constitutes another complication of dialyzed patients which has not been reported so far.

Adult↗
PubMed2006

Fibrillin expression and localization in various types of carcinomas of the thyroid gland.

Fibrillin is an extracellular matrix (ECM) glycoprotein, a main component of microfibrills, suggested to support cell attachment and to impact cell differentiation and migration. The aim of this study was to investigate fibrillin-1 expression in thyroid carcinomas at mRNA and protein level, since ECM proteins are suggested to be of great importance for the metastatic potential of carcinomas. RNA was extracted from 13 thyroid carcinoma cell lines and RT-PCR analysis with gene-specific primers revealed fibrillin-1 mRNA expression in all cell lines, with highest expression in the follicular carcinoma cell line WRO and lowest expression in the two anaplastic cell lines (APO, FRO). Furthermore, we investigated fibrillin-1 expression by immumohistochemistry in a commercially available tissue microarray including 50 thyroid carcinomas as well as in archival tissue from 33 thyroid carcinomas. Fibrillin-1 demonstrated a cytoplasmic location in the neoplastic cells of almost all carcinomas apart from the follicular ones. The most intense staining was observed in papillary carcinomas with some evidence of a slight increased intensity in advanced stages. Our data indicate that fibrillin-1 is strongly expressed by the neoplastic cells of thyroid carcinomas in different degree in the various histologic types and might be implicated in cell-stroma interaction in terms of signaling, attachment and migration.

Adenocarcinoma, Follicular↗
PubMed1996

Mutation in fibrillin-1 and the Marfanoid-craniosynostosis (Shprintzen-Goldberg) syndrome.

Recent reports have described a distinct and recurrent pattern of systemic malformation that associates craniosynostosis and neurodevelopmental abnormalities with many clinical features of the Marfan syndrome (MFS), an autosomal dominant disorder of the extracellular microfibril caused by defects in the gene encoding fibrillin-1, FBN1 (ref. 8). Additional common findings include other craniofacial anomalies, hypotonia, obstructive apnea, foot deformity, and congenital weakness of the abdominal wall. So far, only 11 cases have been reported precluding the assignment of definitive diagnostic criteria. While it remains unclear whether these cases represent a discrete clinical entity with a single aetiology, they have been pragmatically grouped under the rubric Marfanoid-craniosynostosis or Shprintzen-Goldberg syndrome (SGS). Because of the significant clinical overlap between MFS and SGS, we proposed that they may be caused by allelic mutations. We now report two SGS patients who harbour mutations in FBN1. While it remains unclear whether these mutations are sufficient for the clinical expression of the entire SGS phenotype, these data suggest a role for fibrillin-1 in early craniofacial and central nervous system development. Our recent observation that FBN1 transcript is expressed as early as the 8-cell stage of human embryogenesis is consistent with this hypothesis.

Abnormalities, Multiple↗
PubMed2003

Dysregulation of TGF-beta activation contributes to pathogenesis in Marfan syndrome.

Marfan syndrome is an autosomal dominant disorder of connective tissue caused by mutations in fibrillin-1 (encoded by FBN1 in humans and Fbn1 in mice), a matrix component of extracellular microfibrils. A distinct subgroup of individuals with Marfan syndrome have distal airspace enlargement, historically described as emphysema, which frequently results in spontaneous lung rupture (pneumothorax; refs. 1-3). To investigate the pathogenesis of genetically imposed emphysema, we analyzed the lung phenotype of mice deficient in fibrillin-1, an accepted model of Marfan syndrome. Lung abnormalities are evident in the immediate postnatal period and manifest as a developmental impairment of distal alveolar septation. Aged mice deficient in fibrillin-1 develop destructive emphysema consistent with the view that early developmental perturbations can predispose to late-onset, seemingly acquired phenotypes. We show that mice deficient in fibrillin-1 have marked dysregulation of transforming growth factor-beta (TGF-beta) activation and signaling, resulting in apoptosis in the developing lung. Perinatal antagonism of TGF-beta attenuates apoptosis and rescues alveolar septation in vivo. These data indicate that matrix sequestration of cytokines is crucial to their regulated activation and signaling and that perturbation of this function can contribute to the pathogenesis of disease.

Animals↗
PubMed1995

Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly.

Congenital contractural arachnodactyly (CCA) is an autosomal dominant disorder that is phenotypically similar to Marfan syndrome (MFS) and characterized by arachnodactyly, dolichostenomelia, scoliosis, multiple congenital contractures and abnormalities of the external ears. In contrast to MFS, CCA does not affect the aorta or the eyes. Two closely related genes, FBN1 located on chromosome 15q15-21.3 and FBN2 located at 5q23-31, encode large fibrillin proteins found in extracellular matrix structures called microfibrils. The MFS is caused by mutations in FBN1, while CCA has been genetically linked to FBN2 (refs 2, 5, 6). We now describe a pair of FBN2 missense mutations in two CCA patients that cause substitution of distinct cysteine residues in separate epidermal growth-factor-like (EGF) repeats. Our study provides final proof of the association between FBN2 mutations and CCA pathology, thus establishing the role of the fibrillin-2 in extracellular matrix physiology and pathology.

Base Sequence↗
PubMed2006

Angiopoietin-like proteins stimulate ex vivo expansion of hematopoietic stem cells.

Successful ex vivo expansion of hematopoietic stem cells (HSCs) would greatly benefit the treatment of disease and the understanding of crucial questions of stem cell biology. Here we show, using microarray studies, that the HSC-supportive mouse fetal liver CD3(+) cells specifically express the proteins angiopoietin-like 2 (Angptl2) and angiopoietin-like 3 (Angptl3). We observed a 24- or 30-fold net expansion of long-term HSCs by reconstitution analysis when we cultured highly enriched HSCs for 10 days in the presence of Angptl2 or Angptl3 together with saturating levels of other growth factors. The coiled-coil domain of Angptl2 was capable of stimulating expansion of HSCs. Furthermore, angiopoietin-like 5, angiopoietin-like 7 and microfibril-associated glycoprotein 4 also supported expansion of HSCs in culture.

Angiopoietin-Like Protein 2↗