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PubMed1998

Differential protein localization in sarcomeric and nonsarcomeric contractile structures of cultured cardiomyocytes.

The use of cardiomyocyte cell culture models allows the identification of various cell mediators that bring about changes in subcellular structures and gene expression associated with hypertrophy. The effects of insulin-like growth factor-I (IGF-I), basic fibroblast growth factor (bFGF), and triiodothyronine (T3) on gene expression and on the structural organization of myofibrillar and cytoskeletal proteins were compared in adult atrial (aARC) and ventricular (vARC) as well as in neonatal ventricular rat cardiomyocytes (vNRC) in long-term culture. Structural changes were evaluated by confocal microscopy and correlated to biochemical alterations. In vARC, IGF-I enhanced myofibrillar growth, whereas bFGF or T3 restricted sarcomere assembly to the central cell area, forming a sharp boundary in more than 50% of the cells. However, myosin occurred both in the cross-striated myofibrillar structures and in patches running along the nonsarcomeric fibrillar structures (also called stress fiber-like structures) in the cell periphery. In cells treated with either bFGF or T3, the expression of alpha-smooth muscle actin (alpha-sm actin) was greatly increased. This actin isoform was incorporated mainly into the nonsarcomeric contractile structures outside the area where myofibrils ended abruptly. alpha-sm actin protein increased up to 14- to 17-fold while the mRNA showed a moderate increase of 2- to 4-fold. This suggests that alpha-sm actin is mainly regulated at the translational or posttranslational level. In contrast, the cytoskeletal proteins alpha-actinin and vinculin increased only moderately (less than 2-fold) but also showed a relocalization in cells with restricted myofibrils. In aARC and in vNRC, alpha-sm actin was only moderately upregulated by bFGF or T3 and no drastic morphological changes were observed. In conclusion, IGF-I, bFGF, and T3 induced characteristic structural phenotypes depending on the type of cardiomyocyte. Large amounts of alpha-sm actin as expressed in bFGF and T3 treated vARC seem to be incompatible with sarcomere assembly.

Actinin↗
PubMed1998

Implications of quantal motor action in biological systems.

We demonstrate in this paper that quantal behavior is a central feature of biological motile and contractile systems. Step-like behavior has been demonstrated in the interaction between single molecules and filaments both in the kinesin-microtubule system and in the myosin-actin filament system. We show here that the step-like molecular features appear also in the single intact sarcomere. We studied single sarcomeres of single bumble-bee myofibrils, both in the unactivated and activated states. Myofibril-length changes induced by a motor-imposed ramp were accompanied by corresponding sarcomere-length changes. However, the sarcomere-length changes were stepwise. Computer analysis of the stepwise shortening patterns revealed a step-size distribution containing multiple peaks. In the activated state, the peaks were separated by 2.7 nm per half-sarcomere which is the linear actin-subunit spacing. Thus, translation steps are an integer multiple of the actin-subunit spacing. This result parallels the one observed in the kinesin-tubulin spacing, where step size is a multiple of the tubulin-subunit spacing. In the muscle system, however, the steps are preserved on a macroscopic scale, implying high synchrony. The quantal steps are easily explained by a model in which the actin filament propels itself over stationary cross-bridges: if actin binds to the cross-bridges between steps, then the observed quantal result is inevitable. As probes of contractile phenomena approach the molecular level, the discrete unitary events underlying contraction begin to emerge. Thus, step-like behavior is observed as the single kinesin molecule translates along the microtubule, as the single myosin molecule translates over the actin filament, and as the single isolated titin molecule is stretched.

Actins↗
PubMed1995

Differentiation and growth of muscle in the fish Sparus aurata (L): I. Myosin expression and organization of fibre types in lateral muscle from hatching to adult.

Post-hatching development of lateral muscle in a teleost fish, Sparus aurata (L) was examined. At hatching only two fibre types were present, several layers of mitochondria-poor, myofibril-rich deep muscle fibres surrounded the notochord and were covered by a superficial monolayer of mitochondria-rich, myofibril-poor A third ultrastructurally distinct fibre type first appeared as one or two fibres located just under the lateral line at 6 days post-hatching. This type, which gradually increased in number during larval life, contained a slow isoform of myosin, identified by mATPase staining and immunostaining with myosin isoform-specific antibodies. Deep muscle fibres--the presumptive fast-white type--contained a fast myosin, and superficial monolayer fibres an isoform similar but not identical to that in adult pink muscle fibres. The only fibres present during larval life which showed a clear change in myosin expression were the superficial monolayer fibres, which gradually transformed into the slow type post-larvally. Pink muscle fibres first appeared near the end of larval life. Both slow and pink muscle fibres remained concentrated around the horizontal septum under the lateral line during larval life, expanding outwards towards the apices of the myotomes only after metamorphosis. Between 60 and 90 days very small diameter fibres with a distinct mATPase profile appeared scattered throughout the deep, fast-white muscle layer, giving it a 'mosaic' appearance, which persisted into adult life. A marked expansion in the slow muscle layer began at the same time, partly by transformation of superficial monolayer fibres, but mainly by addition of new fibres both on the deep surface of the superficial monolayer and close to the lateral line. The order of appearance of these fibre types, their myosin composition, and the significance of the superficial monolayer layer are discussed and compared to muscle fibre type development in higher vertebrates.

Aging↗
PubMed1995

Characterization of ultrastructural and contractile activation properties of crustacean (Cherax destructor) muscle fibres during claw regeneration and moulting.

Long-(SL > 6 microns) and short-sarcomere (SL < 4 microns) fibres were isolated from the claw muscle of the yabby (Cherax destructor) during limb regeneration and at different stages of the moult cycle. Long-sarcomere fibres were more susceptible to the changes resulting from the moult-induced atrophy compared with the short-sarcomere fibres. Signs of atrophy included fibre erosion, loss of myosin filaments, a reduction in the diameter of myosin filaments and changes associated with the Z line. The intracellular structure of the fibres, however, remained intact in both fibre types. Fibres taken immediately prior to ecdysis could not be fully activated with Ca2+ or Sr2+ without breaking. In contrast fibres taken within 4 h after ecdysis could develop and maintain full force when activated by Ca2+ or Sr2+. The results suggest that loss of myofibrillar proteins via the moult-induced atrophy and/or events associated with fibre elongation may occur in the period just prior to ecdysis and that these changes may be responsible for the fibres inability to function during the premoult stage. Results from this study showed that short-sarcomere fibres add sarcomeres by at least two different mechanisms (1) transverse sarcomere splitting and (2) Z line splitting. Long-sarcomere fibres appear to be elongated by mechanism(s) other than those used by short-sarcomere fibres which possibly involve large electron dense structures which are positioned between the myofibrils and within the A and I bands. Results from the regenerating chelae limb bud showed that sarcomeres form from separate units comprising myosin filaments and actin filaments anchored into Z lines respectively. These sub-sarcomeric units then join together to form sarcomeres. Myofibril formation is aided by electron dense regions which are closely associated with the membrane system. These fibres although short in length and still within the non-functional limb bud could be activated by Ca2+ and Sr2+ suggesting that full fibre function exists before the chelae become functional. Regenerating muscle fibres consisted predominantly of fibres with short-sarcomeres.

Animals↗
PubMed1994

Structural and functional reconstitution of thin filaments in skeletal muscle.

Thin filaments were reconstituted by incorporating exogenous actin, tropomyosin and troponin into glycerinated skeletal muscle fibres or myofibrils. Firstly, thin filaments except short fragments at the Z line were selectively removed by treatment with plasma gelsolin, an actin severing protein. As a result, the fibres (or fibrils) lost the ability to generate active tension. Next, actin filaments were reconstituted by adding purified G-actin which polymerizes onto the actin fragments which remained at the Z line. Rhodamine phalloidin staining of myofibrils showed that exogenous actin was incorporated into the position where the intrinsic thin filaments located. Thin section electron micrographs of fibres showed that reconstituted actin filaments ran from the Z line to the inside of the A band, with some reaching the H zone. The number density of reconstituted actin filaments in the A band was about 20% of that found in intact fibres. The actin filament-reconstituted fibres (or fibrils) generated active tension in a Ca(2+)-insensitive manner and the tension was reversibly suppressed by 2,3-butanedione 2-monoxime. The recovered active tension was about 20% of tension developed by intact fibres. These results indicate that reconstituted actin filaments bear active tension similar to that borne by intact thin filaments. Thin filament-reconstituted fibres, which were prepared by adding purified tropomyosin-troponin complexes into actin filament-reconstituted fibres, showed Ca(2+)-sensitive tension generation. The maximum tension generated was not affected by the presence of tropomyosin and troponin. SDS-PAGE analysis showed that more than 25% of actin and 20% of tropomyosin and troponin was incorporated into the reconstituted fibres. These results indicate that the structure and function of thin filaments are substantially reconstituted by self-assembly of actin, tropomyosin and troponin. The reconstituted fibres and fibrils will be useful for studying the molecular mechanism of muscle contraction and its regulation.

Actin Cytoskeleton↗
PubMed1993

Mini-titins in striated and smooth molluscan muscles: structure, location and immunological crossreactivity.

Invertebrate mini-titins are members of a class of myosin-binding proteins belonging to the immunoglobulin superfamily that may have structural and/or regulatory properties. We have isolated mini-titins from three molluscan sources: the striated and smooth adductor muscles of the scallop, and the smooth catch muscles of the mussel. Electron microscopy reveals flexible rod-like molecules about 0.2 micron long and 30 A wide with a distinctive polarity. Antibodies to scallop mini-titin label the A-band and especially the A/I junction of scallop striated muscle myofibrils by indirect immunofluorescence and immuno-electron microscopy. This antibody crossreacts with mini-titins in scallop smooth and Mytilus catch muscles, as well as with proteins in striated muscles from Limulus, Lethocerus (asynchronous flight muscle), and crayfish. It labels the A/I junction (I-region in Lethocerus) in these striated muscles as well as in chicken skeletal muscle. Antibodies to the repetitive immunoglobulin-like regions and also to the kinase domain of nematode twitchin crossreact with scallop mini-titin and label the A-band of scallop myofibrils. Electron microscopy of single molecules shows that antibodies to twitchin kinase bind to scallop mini-titin near one end of the molecule, suggesting how the scallop structure might be aligned with the sequence of nematode twitchin.

Animals↗
PubMed1996

Development of myocardial fiber organization in the rat heart.

Confocal laser-scanning microscopy of phalloidine-stained actin fibers is a relatively new tool for studying the development of myocardial fiber organization. It seems to show orientation of myocytes in rather early embryonic stages. To further evaluate the differentiation of the myocardium, this technique was compared with transmission electron microscopy in rat embryos aged between 11 and 18 days. Although the confocal images of actin filament patterns pointed to early myocyte orientation, the electron micrographs revealed that even at 17 days the ventricular myocardium was far from mature. Myofibrils never completely filled the myocytes, and lack of organization was the rule rather than the exception. The organized structure as revealed by confocal microscopy was based on cell-to-cell continuity, whereas electron microscopy showed crossing and disarray within individual myocytes. Exceptions were in the ventricular trabeculations, which showed precocious myofiber differentiation. The trabeculations probably support ventricular systole in those stages in which the free walls do not yet provide efficient contractions. The other exception was the wall of the outflow tract, which showed well-oriented myofibrils from early stages onwards. Apparently, the outflow tract has a different function in these stages. The differences found between confocal microscopy and electron microscopy suggest that some caution is indicated in the interpretation of fluorescent images of relatively low magnification.

Actins↗
PubMed1995

Mitochondrial abnormalities of muscle tissue in mice with juvenile visceral steatosis associated with systemic carnitine deficiency.

A mouse with juvenile visceral steatosis (the JVS mouse) has been recognized as a novel animal model for systemic carnitine deficiency. We examined cardiac, skeletal and smooth muscle cells in JVS and control mice by light and electron microscopy. Cardiac and skeletal muscle cells of these mice at 4 weeks of age exhibited a ragged-red appearance after trichrome staining. Electron microscopy, demonstrated increased numbers of mitochondria and lipid droplets in the cells. Compression or distortion of the myofibril bundles, primarily due to the increased number of mitochondria, suggests the possible existence of a functional disturbance of the cardiac and skeletal muscle. In the urinary bladder, only one or two large lipid droplets and slightly increased number of mitochondria were recognized in the perinuclear region of the smooth muscle cells. At 8 weeks of age, the mouse enzyme histochemistry specific for mitochondria, such as cytochrome c oxidase and succinic dehydrogenase, and oil red O staining, confirmed further increases in the number of mitochondria and lipid droplets in the heart. However, the accumulation of these organelles in the skeletal and smooth muscle cells was no greater than that noted in JVS mice at 4 weeks of age. In the cardiac muscle cells, autolysosomes or autophagic vacuoles containing electron-dense membranous, lamellar or whorled structures closely associated with mitochondria and pseudoinclusion bodies in the nucleus were recognized, and bundles of myofibrils were buried under numerous mitochondria, suggesting the existence of disturbed contractile function in the heart of JVS mice. These results indicate that this murine strain associated with systemic carnitine deficiency exhibits a generalized mitochondrial abnormality in the muscle system especially in the heart.

Animals↗
PubMed1989

Structural changes at the myogenic cell surface during the formation of myotendinous junctions.

Myotendinous junctions are sites which are morphologically and molecularly specialized for force transmission between intracellular and extracellular structural proteins. In the present investigation, the formation of these specialized junctions is studied in chicken embryos from 9 days following fertilization to 1 day posthatching, using light and electron microscopy. Observations indicate that the first discernible event in myotendinous junction formation is the appearance of basement membrane at the incipient junction at 9-10 days postfertilization, concomitant with the aggregation of fibroblasts at the junctional regions of myogenic cells. Subsequently, subsarcolemmal densities appear at sites opposite basement membrane locations by 13 days postfertilization. Myofibrils insert into subsarcolemmal densities by day 15 and invaginations of the cell membrane are initiated at those insertions. Type I collagen fibers appear at the cell surface at day 17. Junctional structure at day 17 qualitatively resembles that of adult myotendinous junctions. Changes in junctional structure following day 17 are primarily increases in the amount of subsarcolemmal densities, myofibril-membrane associations, and amount of junctional membrane folding.

Animals↗
PubMed1983

Sheep cardiac Purkinje fibers: configurational changes during the cardiac cycle.

Previous attempts to study the cytoarchitecture of cardiac Purkinje fibers with the scanning electron microscope (SEM) have been limited by the surrounding dense connective tissue. In this study the connective tissue was removed by treatment with 8N HCl, after adult sheep hearts were fixed in diastole or systole and tissue taken for SEM and transmission electron microscopy (TEM). In SEM, Purkinje fibers freely anastomosed in false tendons and formed a subendocardial plexus. In systole, medium and small-sized Purkinje fibers formed deep clefts not observed in diastole. The clefts are thought to be due to sarcolemmal folding and fiber buckling and may therefore affect conduction. The myofibrils beneath the laterally apposed sarcolemmas of adjacent Purkinje cells when fixed in systole were often observed as tightly curved arches in series. Similar configurations with expanded arches were observed in diastole. The formation of arches by myofibrils is unique to Purkinje fibers and is interpreted as the mechanism responsible for their compliance to stretch. The significance of contraction in producing the observed geometric changes in Purkinje fibers and the implications of their cytoarchitecture with respect to conduction are discussed.

Animals↗
PubMed1992

The fate of desmin and titin during the degeneration and regeneration of the soleus muscle of the rat.

We studied the fate of desmin and titin in rat skeletal muscle during a cycle of degeneration and regeneration induced in vivo by the inoculation of a snake venom. Cryosections of muscle were labelled using antibodies to the two proteins, and examined at fixed time points after venom injection. Early pathological changes in the muscle, such as hypercontraction, preceded the loss of desmin. Immunolabelling using anti-desmin antibodies showed that desmin bridges were still intact when adjacent myofibrils were no longer aligned. The results suggested that although the hydrolysis of desmin is not necessary for the hypercontraction of muscle fibres, it probably contributes to complete fibre breakdown. Titin, or at least the part which lies close to the M-line, remained intact longer than desmin, but was also hydrolysed prior to complete disintegration of the fibres. Both desmin and titin were re-expressed in the regenerating myotubes by 2 days after venom inoculation, and became well organised even before the myofibrils became aligned. We conclude that desmin and titin are involved in both establishing and maintaining the structural integrity of the muscle fibres.

Animals↗
PubMedDate not supplied

HSP25 in isolated perfused rat hearts: localization and response to hyperthermia.

Recent investigations concentrate on the correlation between the myocardial expression of the inducible 70-kDa heat shock protein (HSP70i) by different stress conditions and its possible protective effects. Only few studies have focused on the involvement of small heat shock proteins in this process. We analyzed the location of the small heat shock protein HSP25 in isolated cardiomyocytes as well as its location and induction in isolated perfused hearts of rats. By immunofluorescence microscopy HSP25 was found to colocalize with actin in the I-band of myofibrils in cardiomyocytes of isolated perfused hearts as well as in isolated neonatal and adult cardiomyocytes. Hyperthermic perfusion of isolated hearts for 45 min resulted in modulation of different parameters of heart function and in induction of HSP25 is constitutively expressed even in normothermic perfused (44-46 degrees C) were lethal with respect to the contractile function of the hearts. Compared to control hearts perfused at 37 degrees C, significant increases during hyperthermic perfusion at 42 degrees C and 43 degrees C were obtained for heart rate, contraction velocity and relaxation velocity. In response to hyperthermia at 43 degrees C and after subsequent normothermic perfusion for 135 min at 37 degrees C, left to control values immediately after the period of heat treatment. HSP25 is constitutively expressed even in normothermic perfused hearts as shown by Western blotting. Hyperthermia increased the content of HSP25 only in the left ventricular tissue. In contrast, HSP70i was strongly induced in all analyzed parts of the myocardium (left ventricle, right ventricle, septum). Our findings suggest a differential regulation of HSP25 and HSP70i expression in response to hyperthermia in isolated perfused hearts. The constitutively expressed HSP25 seems to be located adjacent to the myofibrils which implies a specific role of this protein even under unstressed conditions for the contractile function of the myocardium.

Animals↗
PubMed1991

Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster.

We have created missense mutations in the indirect flight muscle (IFM)-specific Act88F actin gene of Drosophila melanogaster by random in vitro mutagenesis. Following P element-mediated transformation into wild-type flies and subsequent transfer of the inserts into Act88F null strains, the effects of the actin mutants on the structure and function of the IFMs were examined. All of the mutants were antimorphic for flight ability. E316K and G368E formed muscle with only relatively small defects in structure whilst the others produced IFMs with large amounts of disruption. E334K formed filaments but lacked Z discs. V339I formed no muscle structure in null flies and did not accumulate actin. E364K and G366D both had relatively stable actin but did not form myofibrils. Using an in vitro polymerisation assay we found no significant effects on the ability of the mutant actins to polymerise. E364K and G366D also caused a strong induction of heat shock protein (hsp) synthesis at normal temperatures and accumulated large amounts of hsp22 which, together with the mutant actin, was resistant to detergent extraction. Both E316K and E334K caused a weak induction of hsp synthesis. We discuss how the stability, structure and function of the different mutant actins affects myofibril assembly and function, and the induction of hsps.

Actins↗
PubMed1989

Ultrastructural changes in skeletal muscle in ovine muscular dystrophy.

The initial ultrastructural changes in skeletal myofibers in ovine muscular dystrophy (MD) consisted of focal degeneration of myofibrils and the formation of Z-disc abnormalities, including nemaline rods, in adjacent sarcomeres. Peripheral and central sarcoplasmic masses, which occurred initially in large diameter fibers, contained a mixture of normal organelles and abnormal tubular and fibrillar formations. Vesiculate sarcolemmal nuclei with prominent nucleoli accumulated in central and subsarcolemmal locations in small clusters and short rows. Deformed individual nuclei were sometimes present within nuclear rows. Loss of the myofibrillar mass, increased density of small spherical nuclei, collections of fibrillar and tubular arrays, excessive folding of the sarcolemma and greatly reduced fiber diameter were seen in the end stage of the dystrophic process. Resting satellite cells were present at all stages of lesion development. The morphological progression of the lesions suggested an inherited inability to effectively replace lost myofibrils with ultimate exhaustion of the capacity for repair followed by pathological fiber atrophy.

Animals↗
PubMed1993

Postnatal development of the rat portal vein: correlation with occurrence of peptidergic innervation.

The portal vein of the rat is immature at birth, and is composed of an endothelium surrounded by undifferentiated cells of mesenchymal origin. Three days after birth, these cells have begun to differentiate and aggregate around the lumen to form two separate layers of perpendicularly oriented myoblasts, while a rich calcitonin gene-related peptide (CGRP) innervation is present around the vessel. In the internal circular muscle layer of the media myofibrils first develop on the endothelial side of the myoblasts, and then progressively reach the other side. In the longitudinal muscular layer of the media, which is separated from the circular layer by a connective lamina as early as 3 days after birth, myofibrils develop randomly in the cells. At the time of the enlargement of the longitudinal layer, long close contacts and intermediate junctions between external myoblasts and adventitial fibroblast-like cells were noted, suggesting that recruitment of this cell type is necessary for the maturation of the vessel wall. At about 28 days, the vein has reached its final structure and the smooth muscle cells are fully differentiated. The dense CGRP perivascular innervation already present at birth persists for the first 14 days of postnatal life when most of the cells have not yet acquired their complete contractile differentiation and are still capable of division. This innervation decreases transiently between 15-17 days, when the vessel acquires its spontaneous contractile activity, then rises to a peak between 20 and 25 days, and falls again. CGRP innervation, which is very scarce at 28 days, slowly increases during the peripubescent stage, by which time the adult structure of the vessel is established. Similar fluctuations in the density of peptidergic innervation were observed for substance P and neuropeptide Y, although these peptides were not yet present at birth and occurred only after 5 days. Vasoactive intestinal polypeptide- and bombesin-immunoreactive fibres were not found at any stage investigated. In addition to a description of the different cell-to-cell contacts which could play a role in the maturation of the vessel wall, we discuss the possible implication of the different peptides in the differentiation, maturation or maintenance of the vessel wall.

Animals↗
PubMed1989

Ultrastructural aspects of atrium development: demonstration of endocardial discontinuities and immunolabeling of atrial natriuretic factor in the Syrian hamster.

The endocardium ultrastructure of 13 embryonic day old hamsters was examined, especially in relationship with the atrial myocytes. The endothelial morphology was described, including the junctional attachments and their relationships with subjacent atrial myocytes. Characteristic atrial myocytes organelles were identified: myofibrils, atrial granules, lipidic inclusions, and polysomes. Immunogold labeling demonstrated that atrial natriuretic factor (ANF)-containing granules were already present in the differentiating cardiomyocytes, even before the myofibrils were completely organized. At this stage of development, while the endothelium was a narrow barrier between the blood and the cardiomyocytes, it displayed fenestrations, but also epithelial discontinuities. In addition it also contains immunoreactive-ANF products. In light of the current knowledge about ANF processing it was proposed that the endocardium lining could be an obligated passageway for transport or activating proANF into ANF before its release into the blood stream. In addition the endocardial gaps could suggest that, until about 13 to 14 days of fetal development, heart atrial tissue could be more susceptible to the effects of pathogenetic compounds than in a later state of development.

Animals↗
PubMed1977

[Systemic lupus erythematosus and congestive heart failure. Heart histological and ultrastructural study (author's transl)].

Histological and ultrastructural studies were performed on myocardial biopsies and aortic and mitral valve leaflets obtained during an operation on a patient with Systemic Lupus Erythematosus (S.L.E.). Congestive heart failure and valvular dysfunction appeared five years after the diagnosis of S.L.E. was made. On histological study, aortic and mitral valve leaflets are uniformly thickened by fibrous tissue with a nodular appearance. No active endocarditis was associated with the fibrous scarring. Atrial myocardium and papillary muscle countain a fibrous net-work discret in the former, extensive in the latter. The scattered foci of fibrosis in the papillary muscle surround vessels without obliteration or parietal necrosis. Ultrastructurally their lumina appears narrowed by prominent endothelial cells with cytoplasmic aggregates of tubuloreticular structures (T.R.S.). These tubules are also present in some endocardial endothelial cells but are rare in the normal intrapapillary or atrial vessels that are not associated with a scar. Myocardial fibrous foci enclose atrophic and severely degenerated cardiac muscle cells; other cells situated at the periphery of the foci are normal in size or hypertrophic and moderately degenerated. The most altered muscle cells show an important loss of myofibrils, a proliferation of sarcoplasmic reticulum in myofibril free spaces, or necrosis with macrophagic resorption. Focal changes with loss of myofilaments, Z material streaming and concentric lamellar bodies are found in moderately degenerate cardiac muscle cells. The remaining papillary muscle cells and the atrial cells are all hypertrophied without degeneration. These changes suggest that focal myocardial fibrosis and associated cardiac muscle cell degeneration may be responsible for impaired cardiac performance in some patients with S.L.E. According to the constant topographic relation between the narrowed vessels whose endothelial cells contain T.R.S. and the surrounding fibrous foci, we believe that the myocardial fibrous patches may correspond to scarring of microinfarcts related to active S.L.E. vascularitis.

Aortic Valve↗
PubMed1980

Infrared fluorescence microscopy of stained tissues: principles and technic.

Infrared photomicrography was used extensively from 1927 to the 1940's, but received little attention during the last decades. However, studies of infrared fluorescence of stained sections could not be found in the accessible literature. Ramsley (1968) published quantitative data on infrared fluorescence of approximately 250 dyes bound to textile fibers. The intensity of infrared fluorescence of many dyes varied widely with the substrate. It was therefore deemed of interest to determine whether or not similar differences in infrared fluorescence may occur when dyes are bound to histochemically distinct tissue structures. Myofibrils and collagens stained with triarylmethane dyes were chosen as test objects. Kodak infrared cut-off filter No. 301 and Wratten filter #16 were used as exciter filters to remove infrared and UV-blue and the light of a xenon lamp. Wratten filter #70 and #89B were employed as barrier filters. Infrared radiation was recorded with Kodak Ektachrome infrared film. To facilitate correlation of infrared fluorescence patterns with visible images, tissues were photographed also with conventional color film. Stained myofibrils, e.g. in myoepithelium, smooth and striated muscle emitted strong infrared fluorescence; collagen showed little or no fluorescence. Barrier filter Wratten #70 permitted simultaneous demonstration of infrared fluorescence and of non-fluorescent structures and thus facilitated histopathological studies. Preliminary findings indicate decrease or loss of infrared fluorescence of stained muscle fibers in various lesions, e.g. myocardial infarction, Duchenne-type muscular dystrophy.

Connective Tissue↗