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 145 records · Page 8Linked to original sources
PubMed2002

Fibrillin: from microfibril assembly to biomechanical function.

Fibrillins form the structural framework of a unique and essential class of extracellular microfibrils that endow dynamic connective tissues with long-range elasticity. Their biological importance is emphasized by the linkage of fibrillin mutations to Marfan syndrome and related connective tissue disorders, which are associated with severe cardiovascular, ocular and skeletal defects. These microfibrils have a complex ultrastructure and it has proved a major challenge both to define their structural organization and to relate it to their biological function. However, new approaches have at last begun to reveal important insights into their molecular assembly, structural organization and biomechanical properties. This paper describes the current understanding of the molecular assembly of fibrillin molecules, the alignment of fibrillin molecules within microfibrils and the unique elastomeric properties of microfibrils.

Animals↗
PubMed2005

COBRA, an Arabidopsis extracellular glycosyl-phosphatidyl inositol-anchored protein, specifically controls highly anisotropic expansion through its involvement in cellulose microfibril orientation.

The orientation of cell expansion is a process at the heart of plant morphogenesis. Cellulose microfibrils are the primary anisotropic material in the cell wall and thus are likely to be the main determinant of the orientation of cell expansion. COBRA (COB) has been identified previously as a potential regulator of cellulose biogenesis. In this study, characterization of a null allele, cob-4, establishes the key role of COB in controlling anisotropic expansion in most developing organs. Quantitative polarized-light and field-emission scanning electron microscopy reveal that loss of anisotropic expansion in cob mutants is accompanied by disorganization of the orientation of cellulose microfibrils and subsequent reduction of crystalline cellulose. Analyses of the conditional cob-1 allele suggested that COB is primarily implicated in microfibril deposition during rapid elongation. Immunodetection analysis in elongating root cells revealed that, in agreement with its substitution by a glycosylphosphatidylinositol anchor, COB was polarly targeted to both the plasma membrane and the longitudinal cell walls and was distributed in a banding pattern perpendicular to the longitudinal axis via a microtubule-dependent mechanism. Our observations suggest that COB, through its involvement in cellulose microfibril orientation, is an essential factor in highly anisotropic expansion during plant morphogenesis.

Arabidopsis↗
PubMed2002

Mutant alleles of Arabidopsis RADIALLY SWOLLEN 4 and 7 reduce growth anisotropy without altering the transverse orientation of cortical microtubules or cellulose microfibrils.

The anisotropic growth of plant cells depends on cell walls having anisotropic mechanical properties, which are hypothesized to arise from aligned cellulose microfibrils. To test this hypothesis and to identify genes involved in controlling plant shape, we isolated mutants in Arabidopsis thaliana in which the degree of anisotropic expansion of the root is reduced. We report here the characterization of mutants at two new loci, RADIALLY SWOLLEN 4 (RSW4) and RSW7. The radial swelling phenotype is temperature sensitive, being moderate (rsw7) or negligible (rsw4) at the permissive temperature, 19 degrees C, and pronounced at the restrictive temperature, 30 degrees C. After transfer to 30 degrees C, the primary root's elongation rate decreases and diameter increases, with all tissues swelling radially. Swelling is accompanied by ectopic cell production but swelling is not reduced when the extra cell production is eliminated chemically. A double mutant was generated, whose roots swell constitutively and more than either parent. Based on analytical determination of acid-insoluble glucose, the amount of cellulose was normal in rsw4 and slightly elevated in rsw7. The orientation of cortical microtubules was examined with immunofluorescence in whole mounts and in semi-thin plastic sections, and the orientation of microfibrils was examined with field-emission scanning electron microscopy and quantitative polarized-light microscopy. In the swollen regions of both mutants, cortical microtubules and cellulose microfibrils are neither depleted nor disoriented. Thus, oriented microtubules and microfibrils themselves are insufficient to limit radial expansion; to build a wall with high mechanical anisotropy, additional factors are required, supplied in part by RSW4 and RSW7.

Anisotropy↗
PubMed1996

Computational study of packing a collagen-like molecule: quasi-hexagonal vs "Smith" collagen microfibril model.

The lateral packing of a collagen-like molecule, CH3CO-(Gly-L-Pro-L-Pro)4-NHCH3, has been examined by energy minimization with the ECEPP/3 force field. Two current packing models, the Smith collagen microfibril twisted equilateral pentagonal model and the quasi-hexagonal packing model, have been extensively investigated. In treating the Smith microfibril model, energy minimization was carried out on various conformations including those with the symmetry of equivalent packing, i.e., in which the triple helices were arranged equivalently with respect to each other. Both models are based on the experimental observation of the characteristic axial periodicity, D = 67 nm, of light and dark bands, indicating that, if any superstructure exists, it should consist of five triple helices. The quasi-hexagonal packing structure is found to be energetically more favorable than the Smith microfibril model by as much as 31.2 kcal/mol of five triple helices. This is because the quasi-hexagonal packing geometry provides more nonbonded interaction possibilities between triple helices than does the Smith microfibril geometry. Our results are consistent with recent x-ray studies with synthetic collagen-like molecules and rat tail tendon, in which the data were interpreted as being consistent with either a quasi-hexagonal or a square-triangular structure.

Animals↗
PubMed1985

Ultrastructural cytochemistry of carbohydrates in microfibrils associated with the amorphous elastin in the monkey aorta.

Two distinct ultrastructural components of elastic fibers can be identified--namely, the amorphous elastin and the microfibrils. We have examined the tunica adventitia of monkey aortas to demonstrate differential localization of carbohydrates in elastic fibers and collagen fibrils using Thiéry's periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) staining of thin sections for vicinal-glycol-containing complex carbohydrates, en bloc concanavalin A (Con A) staining specific for alpha-D-mannosyl and alpha-D-glucosyl groups, and en bloc wheat germ agglutinin (WGA) staining specific for N-acetyl-D-glucosamine, N-acetylneuraminic acid, and N-acetyl-D-galactosamine. The PA-TCH-SP method moderately stained microfibrils and weakly stained collagen fibrils, but did not stain the amorphous elastin. Both Con A and WGA staining methods strongly stained microfibrils and moderately stained collagen fibrils, whereas the amorphous elastin lacked staining. Thus PA-TCH-SP, Con A, and WGA staining methods allow differential ultrastructural localization of carbohydrates in elastic fibers and collagen fibrils in monkey aortic adventitia and demonstrate the presence of more carbohydrate components in microfibrils than in collagen fibrils, whereas amorphous elastin lacks carbohydrate staining.

Animals↗
PubMed1986

Assembly of microfibrils in vivo and in vitro from (1----3)-beta-D-glucan synthesized by protoplasts of Saccharomyces cerevisiae.

Polymer chains of (1----3)-beta-D-glucan were dissolved with 1 M NaOH at 4 degrees C from native microfibrillar protoplast nets. The chains associated into microfibrils during NaOH neutralization or dialysis. In contrast to the native microfibrils which are of uniform width individually (10 to 20 nm) and arranged in flat bundles, the microfibrils formed in vitro showed no band formation and consisted of fibrous spindle-shaped subunits of variable width or loose elementary fibrils about 1.7 nm wide. X-ray diagrams of native nets indicated a fairly high crystallinity and were different for wet and dry specimens. They corresponded to those of paramylon. Precipitated glucans produced diagrams different from the former and revealing a lower crystallinity especially with the dry samples. The X-ray pattern, combined with other data, allowed the precipitated microfibrils to be identified as aggregates of molecular strands composed each of three intertwined helical glucan chains. Since these triple helical chains are about 1.7 nm wide the elementary fibrils of this width can represent only single triple-helical strands. These helices have 7 glucose residues per turn and therefore a low symmetry which explains the poor crystallizing properties. The 7 membered helix represents a basic difference with the well crystallized native glucan which is built of highly symmetrical triple helices with 6 glucose residues per turn. Since 6(1) helical conformation is not formed in vitro at normal temperatures its generation in vivo must be due to the action of synthesizing enzymes at the protoplast membrane. The intertwining of these helices and crystallization of the strands are determined by their symmetry and physical properties of the chains.(ABSTRACT TRUNCATED AT 250 WORDS)

Actin Cytoskeleton↗
PubMed1994

Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin.

We present ultrastructural and biochemical evidence for the turnover of intact fibrillin microfibrils by the serine proteinases, neutrophil elastase, chymotrypsin and trypsin. Rotary shadowing electron microscopy revealed that serine proteinase treatment of intact microfibrils isolated from foetal bovine skin resulted in extensive degradation. Microfibrils were destroyed by neutrophil elastase and effectively disrupted by chymotrypsin and trypsin, with no morphologically identifiable arrays remaining. Evidence of defined fibrillin degradation products was obtained by Western blotting of these enzyme-treated fibrillin assemblies. Fibrillin immunoprecipitated from dermal fibroblast culture medium was also comprehensively degraded by these enzymes. These observations demonstrate that serine proteinases are potent effectors for the physiological and pathological catabolism of microfibrils, and suggest a key role in elastic fibre degradation.

Animals↗
PubMed1983

The role of the cytoskeleton during oriented microfibril deposition. I. Elucidation of the possible interaction between microtubules and cellulose synthetic complexes.

A detailed analysis of changes in the cytoskeletal organization during cell elongation and oriented microfibril deposition has been done in the four plant species, clover (Trifolium repens), radish (Raphanus sativus), corn (Zea mays), and sorghum (Sorghum vulgare). Microtubules of variable lengths were found in all the cells examined. Some grouping of microtubules was observed with inter microtubule distances ranging from 14 to 40 nm. Single microfilaments were often observed between parallel microtubules. During cell elongation, microtubule frequency (No./microns) was maintained, thus indicating that microtubules must be formed continuously. The parallel orientation of wall microfibrils is disrupted as they deviate around plasmodesmata and pit-fields; however the cortical microtubules, thought to be influencing microfibril orientation, exhibit no consistent deviation around pit-fields. These observations are used to argue that cortical microtubules cannot influence microfibril orientation through a direct association with cellulose synthetic complexes via microtubule cross bridges.

Cell Wall↗
PubMed1997

Collagen type VI is a component of the extracellular matrix microfibril network of the prostatic stroma.

Stroma-epithelium relationships are of great relevance in prostatic morphogenesis and physiology. However, little knowledge exists about either stromal cells or extracellular matrix composition and arrangement in this system. Ultrastructural analysis revealed the existence of a microfibrillar system which occupies large areas of the rat prostatic stroma. In this work, we have applied immunocytochemistry and an ATP treatment for the ultrastructural identification of collagen type VI microfibrils, aiming at examining its participation in the prostatic microfibrillar network. Immunocytochemistry was also extended to a human case of prostatic nodular hyperplasia. Both methods succeeded in identifying collagen type VI in the rat ventral prostate. Collagen type VI is evenly distributed throughout the stroma but mainly associated with the basal lamina, collagen fibrils, and around the stromal cells. The use of ATP treatment allowed for the discrimination between collagen type VI and elastin-associated microfibrils, and demonstrated that these two classes of microfibrils establish an extended, mixed, and open network. The same aspects of association with the basal lamina, with stromal cells (particularly with smooth muscle cells), and with fibrillar components of the stroma were observed in the human tissue. We suggest that the collagen type VI and elastin-associated microfibril system may be involved in the control of some aspects of cellular behavior and may also play a structural role, maintaining the organ integrity after the deformations occurring under smooth muscle contraction.

Animals↗
PubMed1999

Microfibrils from the arterial subendothelium.

Microfibrillar structures of the subendothelium are represented by either type VI collagen or elastin-associated microfibrils which are also referred to as fibrillin-containing microfibrils. These structures are present throughout the subendothelium irrespective of the presence of elastin. The localization, structure, and protein composition of microfibrils are reviewed. The arterial subendothelium is thrombogenic despite its very low content in fibrillar collagens. This thrombogenicity is linked to the microfibrillar structures, essentially to type VI collagen and to thrombospondin-containing microfibrils. Their respective ability to bind the von Willebrand factor and to activate blood platelets is discussed.

Animals↗
PubMed1986

In vitro collagen fibril assembly in glycerol solution: evidence for a helical cooperative mechanism involving microfibrils.

Glycerol inhibits the in vitro self-association of monomeric collagen into fibrils and induces the dissociation of fibrils preassembled from NaBH4-reduced collagen. These effects were investigated in an effort to understand the mechanism of fibril assembly of the protein. In PS buffer (0.03 M NaPi and 0.1 M NaCl, pH 7.0) containing 0.1-1.0 M glycerol, the self-association of type I collagen from calf skin took place only if the protein concentration was above a critical value. This critical protein concentration increased with increasing glycerol concentration. Velocity sedimentation studies showed that below the critical protein concentration and under fibril assembly conditions, the collagen was predominantly in a monomeric state. Electron microscopic examinations revealed that the collagen aggregates formed above the critical concentration consisted mostly of microfibrils of 3-5-nm diameter along with some banded fibrils were found. Collagen treated with pepsin to remove its nonhelical telopeptides also self-associated into microfibrils and fibrils in the presence of glycerol, but the reaction did not exhibit any critical concentration. These results are consistent with a mechanism of in vitro collagen fibril assembly which involves the initial formation of microfibrils through a helical cooperative mechanism. They also suggest that contacts of the nonhelical telopeptides of each collagen with its neighboring molecules provide the necessary negative free energy change for the cooperativity and that subsequent lateral association of the microfibrils leads to banded fibrils.

Animals↗
PubMed1979

Glomerular microfibrils in renal disease: a comparative electron microscopic study.

Microfibrils are a common component of connective tissue that have been described only rarely in the renal glomerulus. Structurally, microfibrils are fibrotubules with an average diameter of 12 nm, a lucid core, and a dark periphery. High resolution electron microscopy, including stereo microscopy performed on renal biopsy tissues, demonstrated the presence of microfibrils under the endothelium of the capillary walls and in the mesangium in several glomerular diseases. These diseases were characterized by widening of lamina rara interna or separation of the endothelium from the basement membrane, among them transplant glomerulopathy, focal segmental glomerulosclerosis (including a case associated with Marfan syndrome), preeclamptic toxemia, and less frequently hemolytic-uremic syndrome and malignant hypertension. The number of microfibrils generally correlated with the degree of subendothelial widening.

Basement Membrane↗
PubMed1973

Induction of orientation of bacterial cellulose microfibrils by a novel terpenoid from Acetobacter xylinum.

1. The bacterium Acetobacter xylinum produces extracellular cellulose microfibrils that form a pellicle in the medium enmeshing the bacterial cells. These microfibrils may show some localized alignment, which can be seen as birefringence when the culture is viewed between crossed Polaroid sheets. 2. An increase in birefringence can be induced by the addition of small amounts of certain classes of lipids, particularly sterols, to the cultures. 3. A crude lipid extract from Acetobacter cells induced greatly increased birefringence when added to fresh cultures of this organism. 4. When the bacterial lipids were fractionated, most of the activity was recovered in a complex, polar lipid. The lipid is secreted into the medium during growth and is unstable. The non-saponifiable portion of this lipid is shown to be a 1:1 mixture of a saturated and a monounsaturated C(35) tetrahydroxy terpene with a hopane ring system in the accompanying paper by Förster et al. (1973). The saturated molecule is referred to as tetrahydroxybacteriohopane. 5. Tetrahydroxybacteriohopane is itself capable of inducing birefringence in cultures as is 22-hydroxyhopane, which was also isolated from the non-saponifiable fraction of the total lipids. 6. The mechanism of induction of birefringence (orientation of microfibrils) is not known. This is unlikely to be a specific effect, since all the above compounds are active (intact lipid, tetrahydroxybacteriohopane, 22-hydroxyhopane), as are other classes of lipid. It is suggested, however, that a common mechanism may be involved and that similar compounds may be concerned with control of microfibril alignment in the cells of higher plants.

Alcohols↗
PubMed1984

Tunicamycin Prevents Cellulose Microfibril Formation in Oocystis solitaria.

The effect of tunicamycin (TM) on the development of the cell wall in Oocystis solitaria has been investigated. It was found that 10 micromolar TM completely stops the assembly of new microfibrils as observed at the ultrastructural level. During cell wall formation, freeze fracture replicas of the E-face of the plasma membrane reveal two major substructures: the terminal complexes (TC), paired and unpaired, and the microfibril imprints extending from unpaired TCs. In cells treated for 3 hours or longer with TM, the TCs are no longer visible, whereas microfibril imprints are still present. Because of the reported highly selective mode of action of TM, our results implicate a role for lipid-intermediates in cellulose synthesis in O. solitaria. It is assumed that TM prevents the formation of a glycoprotein which probably is a fundamental part of the TCs and may act as a primer for the assembly of the microfibrils.

Journal Article↗
PubMed1990

Cytochemical detection of disulfide and sulfhydryl groups in lamprey aortic microfibrils.

A cytochemical study was performed on the lamprey ventral aorta with special reference to disulfide and sulfhydryl groups of microfibrils, using the high-iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP) method combined with several other types of treatment. The HID-TCH-SP staining observed was classified into three categories: 1) weak staining in the periphery of collagen fibrils, 2) moderate staining in the boundaries of collagen fibrils, microfibrils and smooth muscle cells, and 3) intense staining of microfibrils. The first and second categories of staining were considered to represent chondroitin and/or heparan sulfate because of sensitivity of the staining to chondroitinase ABC (ChABC) and its specific localization. By contrast, the third category of staining was considered to represent disulfide and sulfhydryl groups of microfibrillar glycoprotein, because it was disclosed only after Oxone oxidation or thiosulfation and was not removed by ChABC digestion. Although this staining reactivity was not apparently altered by SH blockade prior to oxidation or thiosulfation, it was markedly diminished or completely inhibited by S-S reduction followed by SH blockade. These results indicate that lamprey aortic microfibrils contain more S-S groups than SH groups.

Actin Cytoskeleton↗
PubMed1983

Microfibrils in the aorta.

Ruthenium red was used to stain microfibrils in rat aorta after incubation of the tissues with or without one of the enzymes trypsin, collagenase, phospholipase C, chondroitinase ABC, hyaluronidase or neuraminidase, or the reducing agent dithiothreitol. Microfibrils exhibiting periodicity of ruthenium red binding were associated with elastic laminae and collagen fibrils and appeared to attach these structures to each other as well as to basal lamina. Microfibrils in rat and human aorta demonstrated fibronectinlike immunoreactivity, therefore fibronectin may be a component of aorta microfibrils and important in the architecture of blood vessels.

Animals↗
PubMed1991

Extracellular microfibrils are increased in localized and systemic scleroderma skin.

Extracellular microfibrils, about 10 nm thick with a hollow core have been found in most organs as free bundles or in association with elastic fibrils. Histochemistry of the dermis of 4 patients with localized and 6 with systemic scleroderma revealed numerous fine elastic fibrils in areas of fibrosis. Immunofluorescence and immunoelectron microscopy were performed with antibodies against fibrillin and amorphous elastin. The lower dermis revealed an increase in 10-nm microfibrils interspersed between collagen fibrils. These microfibrils stained for fibrillin but not for amorphous elastin. Fibrosis in localized and systemic scleroderma involves the deposition of collagen fibrils and microfibrils.

Extracellular Space↗
PubMed1986

The major antigen of elastin-associated microfibrils is a 31-kDa glycoprotein.

The major antigen derived from elastic fiber microfibrils was identified as a Mr = 31,000 glycoprotein, using immunoblotting and immunohistochemical techniques with antisera raised to "reductive guanidine extracts" of fetal bovine nuchal ligament, and to subfractions of these. A second, elastic fiber-derived, but unidentified, antigen of large molecular size (Mr greater than 200,000) was present in these extracts. Antisera raised to the purified 31-kDa glycoprotein were shown, by immunoelectron microscopy, to localize specifically to the elastin-associated microfibrils. Thus, the macro-molecule was called "microfibril-associated glycoprotein" or MAGP. MAGP is an acidic glycoprotein with a distinctive amino acid composition, being exceptionally rich in glutamic acid, rich in cystine, and low in glycine. MAGP was extractable from tissue homogenates using NaCl, urea, or guanidine hydrochloride solutions, only if a strong reducing agent was present. Thus, disulfide bonding is important for the strong association of MAGP with elastic fibers. Immunoblotting with anti-MAGP antiserum identified two additional reactive species, of Mr = 60,000 and Mr approximately 300,000, in tissue extracts. As only the 31-kDa species was detected in fibroblast culture medium, these additional species were probably aggregates, rather than precursors. MAGP did not react with antilysyl oxidase antiserum on immunoblots or by enzyme-linked immunosorbent assay. MAGP is the first macromolecule to have been established to be a constituent of elastin-associated microfibrils in both developing and mature elastic tissues.

Amino Acids↗