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PubMed1987

Mechanical integration of muscle, tegument, and subtegumental tissues by anchoring fibrils and microfibrils in the cestode Hymenolepis diminuta.

Electron microscopic examination of the epidermal basement membrane region of the rat tapeworm, Hymenolepis diminuta, has revealed specialized connective tissue structures that appear to anchor the epidermis, or tegument, to the parenchymal tissues of the helminth, as well as interconnect subtegumental muscle fibers, tegument, and parenchyma. Anchoring fibrils-cross-banded bundles of ca. 3 nm diameter filaments--were observed to directly interlink tegument and muscle, muscle and muscle, and tegument, muscle, and parenchymal connective tissue. Anchoring fibrils therefore appear to mechanically integrate epidermal tissue movements in response to subtegumental muscle contraction. A well-developed stratum of microfibrils, forming the lamina reticularis of the tegumental basement membrane, may also help anchor the tegument as well as to serve as a flexible, reinforcing sheath that protects parenchymal tissues from excessive radial displacement due to muscle contraction.

Animals↗
PubMedDate not supplied

Immunolocalization of a 35K structural glycoprotein to elastin-associated microfibrils.

In this study, a rabbit antiserum directed against a 35K glycoprotein (35K-GP), extracted from connective tissue, was used to examine the localisation of this antigen within foetal bovine ligamentum nuchae at stages of development preceding (4th month) and coinciding with (7th month) active elastin biosynthesis. In these tissues the antibody, detected by a colloidal gold conjugate technique, localised specifically to 11-nm fibrils, identified as the microfibrillar component, present both in the form of independent bundles and in association with elastin in the developing elastic fibres. No other connective tissue component was recognised by the antibodies which had been purified by affinity chromatography. The ability of the antibodies to bind to the microfibrils appeared to be dependent on embedding in LR White resin, as colloidal gold binding was greatly reduced in tissue embedded in epoxy resin. These results are discussed with respect to the role that 35K-GP may play in the morphogenesis of the elastic fibre.

Animals↗
PubMed2005

Regulatory elements of microfibril-associated glycoprotein-1 gene expression in muscle cells.

The Mfap2 gene encodes the microfibril-associated glycoprotein-1 (MAGP1), an extracellular matrix protein of microfibrillar structures. The gene is transcribed from a major transcription start site embedded in a CpG island. Mapping of transcriptionally active regions in the 5' flanking sequence identified a region, located between nucleotides -339 and -109 as the Mfap2 basal promoter. Site-directed and random mutagenesis demonstrated that a KLF sequence motif at -256/-270, an E-box at -222/-229, and a GC-box at -117/-125, are critical for the promoter function. Using electrophoresis mobility shift assays, we find that the KLF motif mediates the binding of GKLF/KLF4, whereas the E-box is a target for both Upstream Stimulatory Factors 1 and 2, and the GC box at -117/-125 forms complexes with Sp1 and Sp3, but not with Sp4 or AP2alpha. A sequence element spanning position -150 may represent the binding motif of an uncharacterized transcription factor. The basal transcriptional regulation of Mfap2 in muscle cells is discussed.

Animals↗
PubMed1992

Helicoidal self-ordering of cellulose microfibrils in aqueous suspension.

In many skeletal support systems of plants and animals, cellulose, chitin, and collagen occur in the form of microfibrils ordered in a chiral nematic fashion (helicoids). However, these structures remain poorly understood due to the many constituents present in biological tissues. Here we report an in vitro system that attracts by its simplicity. Only one chemical component, cellulose, is present in the form of fibrillar fragments dispersed in water. Above a critical concentration the colloidal dispersion separates spontaneously into a chiral nematic liquid crystalline phase. On drying this phase solidifies into regularly twisted fibrillar layers that mimic the structural organization of helicoids in nature.

Cellulose↗
PubMed1999

Inhibitory effect of microfibril wheat bran on azoxymethane-induced colon carcinogenesis in CF1 mice.

Microfibril wheat bran (MFW), a processed dietary fiber prepared by milling of coarse wheat bran (WB), is softer and has a more pleasant taste than WB. In this study, we examined the inhibitory effect of MFW on azoxymethane (AOM)-induced colon carcinogenesis in female CF1 mice and compared its effect with that of WB and cellulose (CL). The mice were fed a modified AIN 76 A diet supplemented with either MFW, WB, or CL at a final concentration of 20% (w/w). Six weekly s.c. injections of AOM (10 mg/kg body weight) were administered per mouse commencing 1 week after the start of the feeding period. Control mice were injected with saline only. Thirty-three weeks after the initial injection, the mice were sacrificed, examined for tumors, and the cecal contents were analyzed to determine the moisture content and the concentrations of short-chain fatty acids (SCFA). The average number of total tumors per mouse in the MFW (2.9 +/- 0.6, P = 0.017) and WB (5.3 +/- 1.3, P = 0.373) diet groups was lower than that of the CL diet group (7.5 +/- 1.3), though there was no significant difference in tumor incidence (94.7%, 90.0% and 94.7%, respectively) between the groups. More than 90% of the tumors in each group were adenocarcinomas. The incidence of adenoma and that of carcinoma in situ in the MFW diet group (5.3% and 0%, respectively) were also lower than those in the CL diet group (26.3 and 26.3%, respectively; P = 0.180 and P = 0.046, respectively). Analysis of the cecal contents revealed a significantly higher moisture content and significantly higher concentrations of SCFA, butyrate in particular, in the MFW and WB diet groups. The results of this study indicate that the source and texture of dietary fiber can influence tumor development in CF1 mice, and more specifically that MFW is a promising and useful dietary supplement with properties serving to protect against the development of colon cancer.

Adenocarcinoma↗
PubMed1999

Microfibril-associated protein 4 is present in lung washings and binds to the collagen region of lung surfactant protein D.

We have purified a glycoprotein from bovine lung washings using affinity chromatography on a maltose-affinity column. On SDS-polyacrylamide gel electrophoresis the protein showed a molecular mass of 36 kDa in the reduced state and 66 kDa in the unreduced state. On gel permeation chromatography the apparent molecular mass was 250 kDa. N-terminal sequencing showed homology to the human matrix protein microfibril-associated protein (hMFAP4), and the glycoprotein was designated bovine MFAP4 (bMFAP4). Lung surfactant protein D (SP-D) was also purified from lung washings, and calcium-dependent binding was demonstrated between bMFAP4 and SP-D. hMFAP4 was cloned, and recombinant hMFAP4 showed the same binding pattern to SP-D as bMFAP4. No binding was seen to recombinant SP-D composed of the neck region and carbohydrate recognition domain of SP-D, indicating that the interaction between MFAP4 and SP-D is mediated via the collagen region of SP-D. MFAP4 also showed calcium-dependent binding to mannan, which was partially inhibited by maltose. Our findings indicate that MFAP4 has two binding specificities, one for collagen and one for carbohydrate, and we suggest that MFAP4 may fix the collectins in the extracellular compartment during inflammation.

Amino Acid Sequence↗
PubMed2001

Kinked collagen VI tetramers and reduced microfibril formation as a result of Bethlem myopathy and introduced triple helical glycine mutations.

Mutations in the genes that code for collagen VI subunits, COL6A1, COL6A2, and COL6A3, are the cause of the dominantly inherited disorder, Bethlem myopathy. Glycine mutations that interrupt the Gly-X-Y repetitive amino acid sequence that forms the characteristic collagen triple helix have been defined in four families; however, the effects of these mutations on collagen VI biosynthesis, assembly, and structure have not been determined. In this study, we examined the consequences of Bethlem myopathy triple helical glycine mutations in the alpha1(VI) and alpha2(VI) chains, as well as engineered alpha3(VI) triple helical glycine mutations. Although the Bethlem myopathy and introduced mutations that are toward the N terminus of the triple helix did not measurably affect collagen VI intracellular monomer, dimer, or tetramer assembly, or secretion, the introduced mutation toward the C terminus of the helix severely impaired association of the mutant alpha3(VI) chain with alpha1(VI) and alpha2(VI). Association of the three chains was not completely prevented, however; and some non-disulfide bonded tetramers were secreted. Examination of the secreted Bethlem myopathy and engineered mutant collagen VI by negative staining electron microscopy revealed the striking finding that in all the cell lines a significant proportion of the tetramers contained a kink in the supercoiled triple helical region. Collagen VI tetramers from all of the mutant cell lines also showed a reduced ability to form microfibrils. These results provide the first evidence of the biosynthetic consequences of collagen VI triple helical glycine mutations and indicate that Bethlem myopathy results not only from the synthesis of reduced amounts of structurally normal protein but also from the presence of mutant collagen VI in the extracellular matrix.

Biopolymers↗
PubMed2000

Characterization of cross-links between cellulose microfibrils, and their occurrence during elongation growth in pea epicotyl.

The occurrence and chemical nature of the cross-links between cellulose microfibrils in outer epidermal cell walls in Pisum sativum cv. Alaska was investigated by rapid-freezing and deep-etching techniques coupled with chemical and enzymatic treatments. The cell wall in the elongating region of epidermal cells was characterized by the absence of the cross-links, while in the elongated region, the cell wall was characterized by the presence of cross-links. The cross-links remained in the cell wall of the elongated region after treatment with SDS electrophoresis sample buffer and treatment with 4% potassium hydroxide. After treatment with endo-1,4-beta-glucanase, which fragments xyloglucan, the cross-links were remarkably reduced from the cell wall of the elongated region. The endoglucanase treatment also reduced immunogold labeling of xyloglucan in the cell wall. The endoglucanase hydrolysate from the cell wall fraction of the elongated region gave spots of oligosaccharides in thin layer chromatography, which were identical to the spots of xyloglucan oligosaccharides produced by xyloglucanase from both the cell wall fraction and tamarind xyloglucan. These results indicate that the cross-links are made of xyloglucan. We discussed the possibility of cross-links involved in the control of mechanical properties of the cell wall.

Cell Wall↗
PubMed1986

HB8: a monoclonal antibody recognizing elastic fibre microfibrils.

We report an ultrastructural study of the reactivity of an IgG monoclonal antibody, which reacts with human dermal elastic fibres. On electron microscopy, immunogold labelling demonstrated the reactivity of HB8 with the microfibrillar component of the fibres. In contrast, the electron-dense granular component which contains elastin was unlabelled with HB8. A fine network of microfibrils from the level of the oxytalan fibres to the large elastic fibres of the deep dermis was labelled with gold particles. No reactivity was detected on collagen fibres. These results demonstrate that HB8 reacts with the microfibrillar glycoproteins of the elastic fibres in normal skin. The precise biochemical nature of the antigens identified by HB8 is still unknown.

Animals↗
PubMed2006

Microfibril-associated protein 4 binds to surfactant protein A (SP-A) and colocalizes with SP-A in the extracellular matrix of the lung.

Pulmonary surfactant protein A (SP-A) is an oligomeric collectin that recognizes lipid and carbohydrate moieties present on broad range of micro-organisms, and mediates microbial lysis and clearance. SP-A also modulates multiple immune-related functions including cytokine production and chemotaxis for phagocytes. Here we describe the molecular interaction between the extracellular matrix protein microfibril-associated protein 4 (MFAP4) and SP-A. MFAP4 is a collagen-binding molecule containing a C-terminal fibrinogen-like domain and a N-terminal located integrin-binding motif. We produced recombinant MFAP4 with a molecular mass of 36 and 66 kDa in the reduced and unreduced states respectively. Gel filtration chromatography and chemical crosslinking showed that MFAP4 forms oligomers of four dimers. We demonstrated calcium-dependent binding between MFAP4 and human SP-A1 and SP-A2. No binding was seen to recombinant SP-A composed of the neck region and carbohydrate recognition domain of SP-A indicating that the interaction between MFAP4 and SP-A is mediated via the collagen domain of SP-A. Monoclonal antibodies directed against MFAP4 and SP-A were used for immunohistochemical analysis, which demonstrates that the two molecules colocalize both on the elastic fibres in the interalveolar septum and in elastic lamina of pulmonary arteries of chronically inflamed lung tissue. We conclude, that MFAP4 interacts with SP-A via the collagen region in vitro, and that MFAP4 and SP-A colocates in different lung compartments indicating that the interaction may be operative in vivo.

Animals↗
PubMed1976

A presumptive subunit of elastic fiber microfibrils secreted by arterial smooth-muscle cells in culture.

Monkey smooth cells, maintained for five weeks in confluent cultures, accumulated a substantial extracellular matrix. Elastic fibers possessing the characteristic amorphous elastin component and 11 nm diameter microfibrils could be isolated from this matrix by extraction with 5 M guanidine. Further extraction under reducing conditions selectively removed the microfibrillar component. Gel electrophoresis of this extract in the presence of sodium dodecylsulfate revealed a single protein band with an apparent molecular weight of 270000. The amino acid composition of this presumptive subunit of the microfibrillar protein was rich in acidic and hydrophilic amino acids and distinctly different from that of collagen or elastin. When smooth muscle cell cultures were incubated with labeled cystine, the predominant labeled protein in the culture medium also had a molecular weight of 270000. This labeled protein comigrated with a major protein band and could be partially purified by DEAE-cellulose ion-exchange chromatography and gel filtration on agarose. It shared manu of the properites of the presumptive microfibrillar protein.

Amino Acids↗
PubMed1978

Comparison of rhapidosomes and asbestos microfibrils.

Rhapidosomers (cylindrical nucleoprotein rods of bacterial origin) show great structural similarity to the microfibrils of chrysotile asbestos when negatively stained and observed with the electron microscope. If the negative stain is omitted, the asbestos retains its structural detail whereas the rhapidosomes appear to be unstructured bodies. When the microscope is adjusted into a selected area diffraction mode, the asbestos shows characteristic electron diffraction patterns whereas the rhapidosomes appear to be amorphous to electron diffraction.

Asbestos↗
PubMed1991

Microfibril-microvessel connections in the uvea and optic nerve of the mammalian eye.

Light- and electron-microscopic examination of arterioles, venules and capillaries of the eyes of several mammalian species has shown that the microfibrils of ocular elastic tissue attach to microvascular basement membranes throughout the uvea (iris, ciliary body, choroid) and optic nerve. Although described sporadically in prior investigations, this report shows that the connections are a common feature of the mammalian eye. The connections appear most numerous at venules and capillaries and are sparse at arterioles. The connections may provide a mechanism by which perivascular elastic tissue influences microvascular function, e.g. the control of blood pressure in them or their response to changes in intraocular pressure.

Animals↗
PubMed2006

Early emphysema in the tight skin and pallid mice: roles of microfibril-associated glycoproteins, collagen, and mechanical forces.

The nature of the development of emphysema in the tight skin (Tsk) and the pallid (Pa) mice are not well understood. We assessed the mechanical and nonlinear properties of the respiratory system, the alveolar structure, and the levels of microfibril-associated glycoproteins (MAGP) 1 and 2 in Tsk mice with developmental emphysema; in Pa mice, which are thought to develop adult onset emphysema; and their background, the C57BL/6 mice, at an age of 7 wk. Minor differences between collagen-related elastic properties of the lungs of the Pa and C57BL/6 mice were seen at this early age. The lungs of the Tsk mice were significantly softer yet more nonlinear than those of the Pa and C57BL/6 mice. The MAGP-1 levels were similar in all three groups. However, the level of MAGP-2, which is associated with both fibrillin-1 and collagen, was higher in the Tsk than in the Pa mice, which also had more MAGP-2 than the C57BL/6. Both the mean and the variance of alveolar diameters were larger in the Tsk than in the other two groups, while the variance in the Pa was larger than in the C57BL/6 mice, implying early development of heterogeneity. Using a network model of the parenchyma, we linked the pathophysiologic changes in the Tsk mice to mechanical forces and failure of the alveolar walls. Our findings suggest the possibility that MAGP-2-related abnormal collagen assembly, combined with mechanical forces, is involved in the progression of emphysema in the Tsk mice.

Animals↗
PubMed1996

Latent transforming growth factor-beta 1 and its binding protein are components of extracellular matrix microfibrils.

We studied the localization of latent transforming growth factor-beta 1 (TGF-beta 1) and its binding protein (LTBP-1) in the extracellular matrix of cultured human fibroblasts by immunofluorescence and immunoelectron microscopy. Immunofluorescence of confluent fibroblast cultures indicated that LTBP-1 localizes to extracellular fibrillar structures resembling fibronectin-collagen matrix. Similar fibrillar structures were detected in cells stained with antibodies specific for TGF-beta 1 propeptide (beta 1-LAP). Both LTBP-1 and beta 1-LAP colocalized with fibronectin in double immunofluorescence analysis. These fibrillar structures were resistant to extraction with sodium deoxycholate, which is further evidence that LTBP-1 and large latent TGF-beta 1 complexes are integral components of the extracellular matrix. SV-40-transformed human fibroblasts lacked extracellular LTBP-1 fibers. EM analysis revealed approximately 10-nm-thick microfibrils that were labeled by anti-LTBP at 90-140-nm intervals. In addition, LTBP-1 was found in structures that were heavily labeled for fibronectin. The accumulation of LTBP-1 in the fibronectin matrix could be reconstituted in vitro. When isolated matrix components were immobilized on nitrocellulose and incubated with fibroblast conditioned medium, LTBP-1 from the medium associated with cellular fibronectin but not with heparan or chondroitin sulfate, vitronectin, tenascin, laminin, or collagen I or IV. The association of LTBP-1 with cellular fibronectin was abolished by treatment of the medium with plasmin, which cleaves LTBP-1 and inhibits its assembly to matrix. The present results indicate that latent TGF-beta 1 complexes are components of the extracellular matrix and suggest that alterations of the pericellular matrix could result in aberrant TGF-beta signaling.

Carrier Proteins↗
PubMed1995

Cysteine-to-arginine point mutation in a 'hybrid' eight-cysteine domain of FBN1: consequences for fibrillin aggregation and microfibril assembly.

Mutations in the FBN1 gene encoding the microfibrillar glycoprotein fibrillin cause Marfan syndrome, a relatively common autosomal dominant connective tissue disease. Causative FBN1 mutations appear to be dispersed throughout the coding frame, and to date no predictable genotype: phenotype correlations have emerged. We have identified a point mutation within an eight-cysteine 'hybrid' motif of the fibrillin polypeptide which results in the substitution of an arginine for a cysteine, in a patient severely affected in the cardiovascular, skeletal and ocular systems. We have utilised cell cultures from various tissues of this patient to investigate the effects of this mutation on fibrillin expression and deposition, and the consequences in terms of microfibril assembly and organisation. We have established that there is no difference in the expression of normal and mutant alleles, and fibrillin synthesis, secretion and deposition are also normal. However, the rate of fibrillin aggregation is reduced and microfibrillar assemblies are both remarkably scarce and morphologically abnormal. These data clearly demonstrate that the mutated allele interferes with normal assembly, and strongly implicate this particular region of the fibrillin-1 molecule in stabilising microfibrillar assemblies.

Actin Cytoskeleton↗
PubMed1996

Cellulose microfibrils, cell motility, and plasma membrane protein organization change in parallel during culmination in Dictyostelium discoideum.

Prestalk cells of Dictyostelium discoideum contribute cellulose to two distinct structures, the stalk tube and the stalk cell wall, during culmination. This paper demonstrates by freeze fracture electron microscopy that two distinct types of intramembrane particle aggregates, which can be characterized as cellulose microfibril terminal complexes, occur in the plasma membranes of cells synthesizing these different forms of cellulose. The same terminal complexes were observed in situ in developing culminants and in vitro in monolayer cells induced to synthesize the two types of cellulose. We propose that cessation of cell motility is associated with a change in packing and intramembrane mobility of the particle aggregates, which cause a change in the nature of the cellulose synthesized. The terminal complexes are compared to those described in other organisms and related to the previous hypothesis of two modes of cellulose synthesis in Dictyostelium.

Animals↗
PubMed1983

Elastic fiber microfibrils: filaments that anchor the epithelium of the epiglottis.

Electron microscope study of the epiglottis in the rat and mouse reveals bundles of tubular-shaped filaments (11 nm diameter) that anchor the basal lamina of the epithelial lining. These anchoring filaments are present both on the laryngeal and oral surfaces of the organ. The filaments are shown to be continuous to elastic fiber microfibrils (EFM) of elastic fibers in the underlying connective tissue. It is suggested that EFM in adults function as anchoring filaments for cells and connective tissue fibers.

Animals↗