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PubMed1995

Elastic fibre assembly: macromolecular interactions.

To investigate the mechanisms behind elastic fibre assembly, we studied the molecular interactions between elastin and microfibrillar components using solid-phase binding assays. Fibrillin 1, purified from tissue using reductive-saline extraction, showed no binding to microfibril-associated glycoprotein (MAGP) or tropoelastin. MAGP, however, was found to bind specifically to tropoelastin in a divalent-cation independent manner. Antibody inhibition studies indicated that the C-terminus of tropoelastin defined the interactive site with MAGP. MAGP and fibrillin were also substrates for transglutaminase, which may provide an important mechanism for stabilizing microfibrillar structure. In other studies we found that a major cross-linking region in elastin is formed through the association of domains encoded by exons 10, 19 and 25 of tropoelastin and that the three chains are joined together by one desmosine and two lysinonorleucine cross-links.

Amino Acid Sequence↗
PubMed1976

Elastic fiber formation in monolayer and organ cultures of chondrocytes isolated from auricular cartilage.

Chondrocytes were isolated from auricular cartilage of immature rabbits and maintained in monolayer or organ culture for 14 days. In both types of culture the chondrocytes formed conspicuous elastic fibers. In monolayer culture the fibers could be identified by orcein staining in the culture dish. Electron microscopy of organ cultures revealed the presence of two basic components of elastic fibers, i.e. microfibrils and elastin.

Animals↗
PubMed1983

Ultrastructural changes associated with the mineralization of deer antler cartilage.

The maturation and mineralization of deer antler cartilage were investigated ultrastructurally by using enzymatic digestions and subsequent staining with ruthenium red (RR) or phosphotungstic acid (PTA). RR staining of matrix granules was observed in the immature prechondroblastic matrix and became more intense as the cartilage matured into a mineralized tissue. The granules got larger and more numerically dense in the mature matrix. There were matrix granules that coalesced around matrix vesicles or remnants of such in the mineralized zone. These granules were observed after demineralization, and they were RR and acidic PTA-positive (they were not susceptible to hyaluronidase nor trypsin digestion, however). It appears that the granules were modified such that the matrix vesicle formed a centralized nidus for mineralization. The growth of hydroxyapatite crystals along matrix granules (which in this zone may or may not represent proteoglycan monomers) may have caused the coalescence. Microfibrils associated with matrix granules probably represented the hyaluronic acid core of the large proteoglycan complexes because of their susceptibility to hyaluronidase digestion.

Animals↗
PubMed1983

Ultrastructure of cartilage from young adult sea lamprey, Petromyzon marinus L: a new type of vertebrate cartilage.

Ultrastructural observations of cartilage from adult sea lamprey, Petromyzon marinus, reveal a highly cellular cartilage with an unusual extracellular matrix. The avascular cartilage is surrounded by a vascular perichondrium, which consists of dense connective tissue containing fibroblasts, collagen fibrils, and microfibrils. The cells (chondrocytes) vary in morphology in different parts of the cartilage in a way that may reflect their state of activity. Chondrocytes within the peripheral cartilage contain tubulo-vesicular structures along the cell surface, an extensive lamellar rough endoplasmic reticulum, and a well-developed Golgi complex with associated vesicles and vacuoles. The presence of material within the Golgi elements that resembles components of the extracellular matrix suggests the involvement of the peripheral chondrocytes in the synthesis and secretion of the matrix components. Chondrocytes within the central cartilage are hypertrophied and contain a pale cytoplasm with a reduced number of organelles that are widely spaced throughout the cell. The appearance of the organelles within these cells suggests that they are not as actively involved in the production of the matrix as those of the peripheral cartilage. The extracellular matrix consists of a dense network of randomly arranged, branched, noncollagenous matrix fibrils 15-40 nm in diameter and varying amounts of electron-dense matrix granules. Due to the unique nature of its extracellular matrix, the cartilage of the lamprey cannot be likened to any of the known vertebrate cartilages and, therefore, must be considered a new type of vertebrate cartilage.

Animals↗
PubMed1984

Cartilage in the Atlantic hagfish, Myxine glutinosa.

Light and electron microscopic observations and biochemical analysis of the lingual cartilages from the Atlantic hagfish, Myxine glutinosa, reveal two different types of cartilage, designated types 1 and 2, respectively. The anterior and medial lingual are type 1, while the posterior lingual cartilage is type 2. Chondrocytes in type 1 cartilage are similar to those found in other vertebrate cartilages. The presence within the Golgi elements of material that resembles a component of the extracellular matrix suggests the involvement of active chondrocytes in the synthesis of the matrix. The matrix of the type 1 cartilage contains fibrils arranged to form concentric lamellae in the territorial matrix and irregularly arranged, branched fibrils in the interterritorial matrix. Biochemical analysis of the type 1 cartilage reveals that it is composed primarily of a cyanogen bromide (CNBr)-insoluble protein of unique composition that we have termed " myxinin ." Myxinin appears to be similar, but not identical, to lamprin . Type 2 cartilage bears no resemblance to any other known vertebrate cartilage. The principal cells are hypertrophied and are characterized by masses of cytoplasmic filaments. The appearance of the organelles in smaller nest cells suggests that nest cells are active in the production of some of the matrix, which consists primarily of collagen. Microfibrils and a basal lamina-like material are also present. Biochemical analysis of the type 2 cartilage reveals that the CNBr-insoluble material is different from myxinin . Comparisons of lamprey and hagfish cartilages prompt the concept that these two agnathans probably followed long-independent evolutionary histories.

Animals↗
PubMed1988

Three-dimensional network of cords: the main component of basement membranes.

Basement membranes were divided into two types: 1) thin basement membranes, such as those of the epidermis, trachea, jejunum, seminiferous tubule, and vas deferens of the rat, the ciliary process of the mouse, and the seminiferous tubule of the monkey, and 2) thick basement membranes, such as the lens capsule of the mouse and Reichert's membrane of the rat. High-magnification electron microscopy was used to examine both types after fixation either in glutaraldehyde followed by postosmication or in potassium permanganate. The basic structure of thin and thick basement membranes was found to be a three-dimensional network of irregular, fuzzy strands referred to as "cords"; the diameter of these cords was variable, but averaged 4 nm in all cases examined. The spaces separating the cords differed, however. In the lamina densa of thin basement membranes, the diameter of these spaces averaged about 14 nm in every case, whereas in the lamina lucida it ranged up to more than 40 nm. Intermediate values were recorded in thick basement membranes. Finally, the third, inconstant layer of thin basement membranes, pars fibroreticularis, was composed of discontinuous elements bound to the lamina densa: i.e., anchoring fibrils, microfibrils, or collagen fibrils. In particular, collagen fibrils were often surrounded by processes continuous with the lamina densa and likewise composed of a typical cord network. Finally, two features were encountered in every basement membrane: 1) a few cords were in continuity with a 1.4- to 3.2-nm thick filament or showed such a filament within them; the filaments became numerous after treatment of the seminiferous tubule basement membrane with the proteolytic enzyme, plasmin, since cords decreased in thickness and could be reduced to a filament, and 2) at the cord surface, it was occasionally possible to see 4.5-nm-wide sets of two parallel lines, referred to as "double tracks." On the basis of evidence that the filaments are type IV collagen molecules and the double tracks are polymerized heparan sulfate proteoglycan, it is proposed that cords are composed of an axial filament of type IV collagen to which are associated glycoprotein components (laminin, entactin, fibronectin) and the double tracks of the proteoglycan.

Alouatta↗
PubMed2001

Novel approach to the molecular diagnosis of Marfan syndrome: application to sporadic cases and in prenatal diagnosis.

Marfan syndrome is an autosomal dominant disorder affecting the skeletal, ocular, and cardiovascular systems. Defects in the gene that encodes fibrillin-1 (FBN1), the main structural component of the elastin-associated microfibrils, are responsible for the disorder. Molecular diagnosis in families with Marfan syndrome can be undertaken by using intragenic FBN1 gene markers to identify and track the disease allele. However, in sporadic cases, which constitute up to 30% of the total, DNA-based diagnosis cannot be performed using linked markers but rather requires the identification of the specific FBN1 gene mutation. Due to the size and complexity of the FBN1 gene, identification of a causative Marfan syndrome mutation is not a trivial undertaking. Herein, we describe a comprehensive approach to the molecular diagnosis of Marfan syndrome that relies on the direct analysis of the FBN1 gene at the cDNA level and detects both coding sequence mutations and those leading to exon-skipping, which are often missed by analysis at the genomic DNA level. The ability to consistently determine the specific FBN1 gene mutation responsible for a particular case of Marfan syndrome allows both prenatal and pre-implantation diagnosis, even in sporadic instances of the disease.

Adult↗
PubMed2003

A boy with developmental delay, malformations, and evidence of a connective tissue disorder: possibly a new type of cutis laxa.

We report a 7.5-year-old boy with loose translucent skin, aortic dilatation, hyperextensible veins, recurrent respiratory problems, pectus excavatum, arthralgias, lax joints, mild epiphyseal dysplasia, and umbilical and inguinal hernias. He also has developmental delay, progressive bilateral sensorineural hearing loss, an unusual facial appearance, terminal digit hypoplasia with unusual radiographic changes in some of the phalanges, glandular hypospadias, shawl scrotum, and undescended testes. Biochemical investigations, including electrophoresis of Types 1 and 3 procollagens and collagens, and quantification of serum copper and ceruloplasmin, are normal. Relative to age-matched control patients the electron micrographs of the boy's dermis show elastin fibers to be decreased in number, and abnormal in appearance, with a low matrix to microfibril ratio. The organ distribution of abnormalities and the nature of the findings suggest a connective tissue disorder. We contrast and compare this boy's phenotype to those of the classic connective tissue disorders. We conclude that he has cutis laxa with features that distinguish him from previously described types of cutis laxa.

Abnormalities, Multiple↗
PubMed2004

Marfanoid habitus with abnormal situs.

Marfanoid habitus suggests abnormal microfibril formation, whereas a situs ambiguus or situs inversus phenotype points to defective left-right axis determination. The concurrence of these two abnormalities has been reported only once in the literature. We report a similar phenotype in two unrelated patients. Documentation of this specific combination of Marfanoid habitus and abnormal situs gives further credence to the notion that the combination may represent a distinct syndrome.

Female↗
PubMed2004

Craniofacial structure in Marfan syndrome: a cephalometric study.

Marfan syndrome (MFS) is a connective tissue disorder with autosomal dominant inheritance. Mutations in the FBN1 gene cause deficient processing of fibrillin-1, the main constituent of extracellular microfibrils, affecting tissues displaying elastic properties. Clinical manifestations are widespread and involve the skeletal, ocular, cardiovascular and pulmonary systems, skin and integumentum, and dura. A highly arched palate and retrognathia have been assigned to the symptoms with minor diagnostic specificity, although epidemiological data on prevalence are lacking yet. Twenty-six patients with MFS (n = 26) were studied for craniofacial characteristics using cephalometric measurements on lateral cranial radiographs. The purposes of this study were (1) to compare cephalometric variables of MFS group with age- and sex-matched population norms, and (2) to assess differences in palatal vault dimensions among adult MFS (n = 17) and matched controls (n = 32) by means of cephalometric measurements. Significant differences with population norms were found in the structures of the cranial base, the maxillary complex, the mandible body, and the relations of the jaws with respect to the cranial base and to each other. Palatal height and palatal length were significantly larger in MFS, and were significantly correlated to each other and to the height of the maxillo-alveolar processus. The present data disprove in part previously reported findings, possibly due to biased patient selection in these studies or demographic differences. However, a strong correlation was found between maxillary/mandibular retrognathia, long face, highly arched palate, and MFS. A combination of both intrinsic genetic factors and environmental factors is suggested as a possible explanation for specific morphogenetic aspects of the craniofacial complex in MFS.

Adolescent↗
PubMed2005

Histopathology and fibrillin-1 distribution in severe early onset Marfan syndrome.

Marfan syndrome (MFS) is an autosomal dominant condition which may involve the cardiovascular, ocular, skeletal, and other systems. Mutations causing MFS are found in the FBN1 gene, encoding fibrillin-1, an extracellular matrix protein involved in microfibril formation. In the most severe cases, mutations are generally found in exons 24-32, and children with these mutations usually die in the first years of life, of cardiopulmonary failure. We present clinical, molecular and histopathological studies on a patient with severe early onset MFS. He has a mutation in exon 25 of FBN1, a G>A transition at nucleotide position 3131 that converts the codon TGC, coding for cysteine at position 1044, to TAC, coding for tyrosine (C1044Y). This has resulted in abnormalities of the extracellular matrix and a severe clinical phenotype, although he has survived to the age of 14 years.

Adolescent↗
PubMed2006

COL6A1 genomic deletions in Bethlem myopathy and Ullrich muscular dystrophy.

We have identified highly similar heterozygous COL6A1 genomic deletions, spanning from intron 8 to exon 13 or intron 13, in two patients with Ullrich congenital muscular dystrophy and the milder Bethlem myopathy. The 5' breakpoints of both deletions are located within a minisatellite in intron 8. The mutations cause in-frame deletions of 66 and 84 amino acids in the amino terminus of the triple-helical domain, leading to intracellular accumulation of mutant polypeptides and reduced extracellular collagen VI microfibrils. Our studies identify a deletion-prone region in COL6A1 and suggest that similar mutations can lead to congenital muscle disorders of different clinical severity.

Adult↗
PubMed2002

Distribution of the elastic fiber and associated proteins in flexor tendon reflects function.

The elastic fiber is known to be an important component of skin, lung, and vasculature. Much less is known about the distribution of elastin and elastic fiber-related proteins in connective tissues, yet genetic defects of elastic fiber constituents can lead to deficiencies in these tissues. For the first time, we determine the distribution of elastin, fibrillins 1 and 2, and microfibril-associated glycoproteins (MAGPs) 1 and 2 in the flexor digitorum profundus (FDP) tendon. Three functionally distinct regions of the FDP tendon, the fibrocartilagenous (FC) region, avascular/tensional (AV/T) region, and insertion region, were evaluated by immunohistochemical methods for these five proteins. Biochemical analysis of desmosine content, an elastin-specific cross-link, demonstrated the presence of elastin in each region, and this was verified histochemically. The fibrillins were found with elastin and also pericellularly with internal fibroblasts where elastin was not detected. Although there was overlapping distribution, fibrillin 2 was more prominent in the interior of the tendon while fibrillin 1 was prominent in outer cell layers that contained elastic fibers. Both MAGP-1 and -2 were found throughout the tendon, although the greatest abundance was near the tendon insertion to bone. Surprisingly, MAGP-1 demonstrated a filamentous appearance within the fibrocartilage that did not correspond to the fibrillin 1 or 2 or MAGP-2 staining pattern. Lastly, we have shown that a vincular membrane located along the dorsal surface of the tendon near the insertion has a very high elastin content and a unique interface with the tendon that consists of an elastic anchor within the tendon body.

Animals↗
PubMed1977

Ultrastructural distinction between reticular and collagenous fibers with an ammoniacal silver stain.

Reticular and collagenous fibers stain differently when subjected to ammoniacal silver reduction. A variety of tissues were subjected to such a "reticulin" technique and the association of reaction product with intercellular connective tissue elements was studied with the electron microscope. The reaction with reticular fibers was primarily associated with the interfibrillar matrix, and was globular in form having a wide variety of particle sizes. Conversely, in dermal collagen the unit fibrils were stained rather than the interfibrillar matrix. The precipitate was punctate in form and was associated with the cross striations of unit collagen fibrils. Large microfibrils also reacted positively with the stain, imparting a faint periodicity. Basement membranes were stained uniquely. The underlying plasmalemma and the lamina densa were heavily stained with silver while the lamina lucida was relatively unstained. The unit fibrils of the lamina reticularis stained in the same manner as dermal unit collagen while the ground substance remained unstained. This represents a clear distinction between the argentophilic characteristics of collagenous fibers, reticular fibers, and basement membranes.

Animals↗
PubMed1979

Response of periodontal ligament cells to orthodontic force: ultrastructural identification of proliferating fibroblasts.

The morphologic response of periodontal ligament (PDL) cells in an area of tension created by orthodontic force has been assessed by transmission electron microscopy. Young adult male rats were sacrificed at 24, 48, 72, 96 and 120 hours following orthodontic stimulation. The earliest detectable response was the appearance of increased numbers of mitotic cells in the PDL at 24 hours post-stimulation. The most significant ultrastructural feature of these cells was the presence of intracellular vesicles containing collagen microfibrils. These vesicles were identical to profiles present in interphase PDL fibroblasts involved in collagen phagocytosis associated with turnover of the ligament. Between 48 and 120 hours the alveolar bone surface in the region examined was characterized by the presence of newly generated osteoblasts and active bone formation. Intracellular collagen was never observed in osteoblasts. These observations suggest that at least a portio- of the population of PDL cells which proliferate in response to orthodontic force represent functional ligament fibroblasts.

Alveolar Process↗
PubMed1981

Organization of collagen in the human pulmonary alveolar wall.

The purpose of this study was to determine the organization of collagen in the wall of the human pulmonary alveolus. Samples of human lung obtained at surgery were processed for light and electron microscopy. Light microscopy confirmed the general findings of Orsos ('36): there were 3 common fibers called primary, secondary, tertiary in this study in order of their increasing size. Primary fibers (called "pericapillary" by Orsos) formed a continuous mesh in the alveolar wall and were often confluent within the intercapillary regions of the wall ("knötenpunkten," or nodes, Orsos). The tortuous secondary fibers ("circulatory fibers," Orsos) passed frequently across the thickness of the alveolar wall and were closely applied to capillary walls. Tertiary fibers ("respiratory fibers," Orsos) were continuous with the alveolar ostia and formed the supportive struts of the alveolar wall as they crossed the wall in a more direct course than the serpiginous secondary fibers. Electron microscopy (serial sections and stereo pairs) showed that the primary fibers inserted near the edge of an intercapillary region, where they were attached to the endothelial or epithelial basal lamina directly or by a smaller fiber or microfibril resembling the fibrous component of elastin or oxytalan. Primary fibers passed through a typical intercapillary region while describing a helix or a portion thereof. Secondary fibers were more coarse than primary, and both secondary and tertiary fibers resembled woven ropes.

Adult↗
PubMed1981

Ultrastructural changes in hamster lung four hours to twenty-four days after exposure to elastase.

A single endotracheal instillation of elastase initiates a series of changes in animal lungs that results in a condition resembling human panlobular emphysema. An ultrastructural examination of this series of changes was conducted on the lungs of male golden hamsters exposed to 3H-methylated pancreatic elastase and sacrificed at intervals between 4 hour and 24 days after exposure to enzyme. Lung tissue between 4 and 48 hours showed evidence of hemorrhage and progressive degradation of elastic fibers. Very little indication of epithelial cell damage accompanied these changes. Four days after exposure to elastase, synthesis of new elastic fibers began with the appearance of small clumps of microfibrils in close association with interstitial cells, fibroblasts, and smooth muscle cells. There was also evidence of alterations in alveolar type II cells at this time. Small fibrillar elastic fibers continued to be present in the lung through twenty-four days and may represent a slow repair process or may indicate a structural difference in elastic fibers synthesized after exposure to elastase. Evidence of the continued degradation of elastic fiber could be found up to 16 days after exposure to elastase, revealing that repair processes were occurring in some areas of the lung while destructive process still predominated in other areas.

Animals↗
PubMed1983

Distribution of polyanionic sites in the developing gonads and the dorsal mesentery of the chick embryo.

The distribution of glycoconjugates was investigated in the embryonic trunk mesoderm used as a substrate by migrating primordial germ cells (PGCs) by means of ultrastructural cytochemistry. In both mesentery and developing gonads polyanionic sites were abundant in epithelial and mesenchymal cell coats, basal laminae, and extracellular matrices (ECM). In the latter, polyanions distributed on microfibrils and granules were associated with collagen fibers, forming an entangled network. No preferential association of this fibrillo-granular material with PGCs was observed, suggesting that polyanions present in ECM likely act by promoting inflation of the extracellular spaces rather than by providing mechanical guides for the moving cells.

Animals↗