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S Swasdison

Publications and source records attributed to S Swasdison.

10 recordsLinked to original sources
PubMed2006

Central neurilemmoma of the jaw in concurrence with radicular cyst: a case report.

We report the features of a central neurilemmoma in the mandible of a patient having an inflammatory apical dental (radicular) cyst in the same region. A 29-year-old woman complained of numbness on the right side of the lower lip of 3 months duration and noted following endodontic therapy to the right mandibular first molar tooth. Panoramic radiography revealed a bilocular radiolucency in the right body of the mandible. Excisional biopsy was performed. The histopathology revealed neurilemmoma of the mandible in concurrence with inflammatory apical dental (radicular) cyst. No recurrence was detected during a 1-year follow-up.

Adult↗
PubMed1998

Primary structure and expression of a chicken laminin beta chain: evidence for four beta chains in birds.

Characterization of a full length cDNA sequence for a chicken laminin beta chain is described which is most closely related to the mammalian beta 2 chain. Comparison with published sequences shows that the chicken beta 2-like chain corresponds to a fragment of a previously described laminin beta chain called B1-2 (O'Rear, 1992). The sequence of the chicken beta 2-like chain differed from fragments of two other chicken laminin beta chains that were previously described and designated B1-1 (now called beta 1; O'Rear, 1992) and beta x (Ybot-Gonzalez et a1.,1995). In addition, the beta 2- like chain does not appear to be the chicken equivalent of the mammalian laminin beta 3 chain, since it differs markedly in cDNA sequence, possesses domain IV and has a transcript size of 6 kb. We therefore propose that there are at least four laminin beta chains in the chicken. Sequence comparison of the beta 2-like laminin chain with previously cloned beta 1 and beta 2 chains shows a somewhat closer relationship to rat and human beta 2 than to mouse and human beta 1, especially in domains I, II and alpha. In addition, two expressed fragments of the chicken beta 2-like chain were recognized by a monoclonal antibody (C4) regarded as specific for the rat beta 2 chain (Hunter et al., 1989a). The results therefore suggest that the laminin chain previously described as a potentially novel chain called B1-2 (O'Rear, 1992) is likely to be the chicken equivalent of the mammalian beta 2 chain.

Amino Acid Sequence↗
PubMed1994

Immunization with undenatured bovine zonular fibrils results in monoclonal antibodies to fibrillin.

Microfibrils were dissected from the zonular apparatus of the bovine eye, homogenized and used as an immunogen to prepare monoclonal antibodies. Initial screening of hybridomas was performed by immunoblotting to a sonicate of zonular fibrils and by immunolocalization to frozen sections of the zonular apparatus. Subsequently, monoclonal antibodies with strong immunoreactivity to zonular fibrils were shown to recognize microfibrils in a wide range of connective tissues both by immunofluorescent staining and by electron microscopic immunolocalization. All antibodies were found to recognize a single protein of 350 kDa on Western blotting of the proteins secreted by bovine aortic smooth muscle cells. A protein of the same molecular weight and properties was recognized by an antibody previously prepared by another group against fibrillin. A member of the fibrillin family therefore represents the major immunogen of intact zonular fibrils, and the results support previous evidence for a close relationship between zonular fibrils and other connective tissue microfibrils. The zonular apparatus is a suitable system to obtain purified preparations of microfibrils in order to investigate their composition and structural organization.

Actin Cytoskeleton↗
PubMed1992

Monoclonal antibodies that distinguish avian type I and type III collagens: isolation, characterization and immunolocalization in various tissues.

Monoclonal antibodies were prepared that were specific for chicken type I and type III collagens. The specificity of these antibodies was determined by ELISA, inhibition ELISA, and immunoblot assays. The results showed that the monoclonal antibodies were specific for their respective antigens without significant cross reactivity to other types of collagen. An analysis of the location of the epitopes by rotary shadowing that a monoclonal antibody for type I collagen (called DD4) recognized type I procollagen close to the large globular domain at the carboxyl terminus of the molecule. A monoclonal antibody for type III collagen (called 3B2) recognized both the intact type III molecule and also the TCA fragment of type III collagen after mammalian collagenase digestion. The epitope was located approximately one-fifth of the distance from the amino-terminus of the intact molecule. The monoclonal antibodies were used for immunolocalization of type I and type III collagens in cryosections of heart, aorta, kidney, liver, thymus, skin, gizzard and myotendinous junction. In heart, aorta, kidney, liver, thymus and skin, type I and III collagens were colocalized in the connective tissue of each organ. In contrast, gizzard and myotendinous junction showed distinctly different staining patterns for the distribution of type I and type III collagen. The two monoclonal antibodies reported here are potentially useful reagents to study fibril formation involving type I and type III collagens.

Animals↗
PubMed1992

Formation of highly organized skeletal muscle fibers in vitro. Comparison with muscle development in vivo.

Two methods were developed in which long-term cultures of quail skeletal muscle were established so that all of the muscle fibers develop in a highly oriented manner. The muscle fibers became spontaneously and vigorously contractile and established strong connections with the extracellular matrix at their ends that closely duplicate the structure of the myotendinous junction. A continuous basal lamina was formed around each muscle fiber that contained type IV collagen, laminin and heparan sulfate proteoglycan. With one of the methods, an extensive extracellular matrix developed around each muscle fiber that was highly organized with the formation of a distinctive epimysium, perimysium and endomysium. Analysis of the cultures by both methods for different isoforms of myosin showed expression of an adult form of myosin by some of the muscle cells. The results therefore demonstrate that muscle development in the present culture systems proceeds extensively for several weeks. It will now be possible to investigate directly the structure of the connections between muscle fibers and the extracellular matrix.

Animals↗
PubMed1991

In vitro attachment of skeletal muscle fibers to a collagen gel duplicates the structure of the myotendinous junction.

The myotendinous junction (MTJ) and its associated cells and connective tissue are important structures involved in transmission of contractile force from skeletal muscle to tendon. A model culture system was developed to investigate the formation of the MTJ and its attachment to collagen fibers. Skeletal muscle cells were cultured in a well modeled from two layers of a native gel of type I collagen. Muscle cells cultured in this manner formed attachments to the collagen gel and developed into highly contractile multinucleated muscle fibers with the development of extensive terminal invaginations of the sarcolemma. In addition, the subsarcolemma at the ends of muscle fibers showed areas of increased electron density which corresponded well with the termini of myofibrils. The results indicate that the development of sarcolemmal invaginations at the end of a muscle fiber probably occurs intrinsically during muscle development in vivo. The direct association of collagen fibers with the basal lamina at the end of muscle fibers was only occasionally observed in culture, suggesting that other fibrils or proteins may also be involved in the attachment of collagen fibers to the basal lamina of muscle fibers at the MTJ.

Animals↗
PubMed1991

Computer-aided mechanogenesis of skeletal muscle organs from single cells in vitro.

Complex mechanical forces generated in the growing embryo play an important role in organogenesis. Computerized mechanical application of similar forces to differentiating skeletal muscle myoblasts in vitro generate three-dimensional artificial muscle organs. These organs contain parallel networks of long unbranched myofibers organized into fascicle-like structures. Tendon development is initiated and the muscles are capable of performing directed, functional work. Kinetically engineered organs provide a new method for studying the growth and development of normal and diseased tissue.

Animals↗
PubMed1989

Location of the integrin complex and extracellular matrix molecules at the chicken myotendinous junction.

The distribution of several extracellular matrix macromolecules was investigated at the myotendinous junction of adult chicken gastrocnemius muscle. Localization using monoclonal antibodies specific for 3 basal lamina components (type IV collagen, laminin, and a basement membrane form of heparan sulfate proteoglycan) showed strong fluorescent staining of the myotendinous junction for heparan sulfate proteoglycan and laminin, but not for type IV collagen. In addition, a strong fluorescent stain was observed at the myotendinous junction using a monoclonal antibody against the beta subunit of the chicken integrin complex (antibody JG 22). Neither fibronectin nor tenascin were concentrated at the myotendinous junction, but instead were present in a fibrillar staining pattern throughout the connective tissue which was closely associated with the myotendinous junction. Tenascin also gave bright fluorescent staining of tendon, but no detectable staining of the perimysium or endomysium. Type I collagen was observed throughout the tendon and in the perimysium, but only faintly in the endomysium. In contrast, type III collagen was present brightly in the endomysium and in the perimysium, but could not be detected in the tendon except when associated with blood vessels and in the epitendineum, which stained intensely. Type VI collagen was found throughout the tendon and in all connective tissue partitions of skeletal muscle. The results indicate that one or more molecules of the integrin family may play an important role in the attachment of muscle to the tendon. This interaction does not appear to involve extensive binding to fibronectin or tenascin, but may involve laminin and heparan sulfate proteoglycan.

Animals↗