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Biomedical subjects

T F Robinson

Publications and source records attributed to T F Robinson.

At least 19 recordsLinked to original sources

Turnover of stable carbon isotopes in the muscle, liver, and breath CO2 of alpacas (Lama pacos).

Stable carbon isotope analysis of animal liver and muscle has become a widespread tool for investigating dietary ecology. Nonetheless, stable carbon isotope turnover of these tissues has not been studied in large mammals except with isotopically labelled tracer methodologies, which do not produce carbon half-lives analogous to those derived from naturalistic diet-switch experiments. To address this gap, we studied turnover of carbon isotopes in the liver, muscle, and breath CO2 of alpacas (Lama pacos) by switching them from a C3 grass diet to an isonitrogenous C4 grass diet. Breath samples as well as liver and muscle biopsies were collected and analyzed for up to 72 days to monitor the incorporation of the C4-derived carbon. The data suggest half-lives of 2.8, 37.3, and 178.7 days for alpaca breath CO2, liver, and muscle, respectively. Alpaca liver and muscle carbon half-lives are about 6 times longer than those of gerbils, which is about what would be expected given their size. In contrast, breath CO2 turnover does not scale readily with body mass. We also note that the breath CO2 and liver data are better described using a multiple-pool exponential decay model than a single-pool model.

Aging↗

The beta-agonist cimaterol directly enhances chronic protein accretion in skeletal muscle.

Our objective was to determine whether the chronic anabolic effects of beta-adrenergic agonists on skeletal muscle are direct and how long they are maintained. We studied acute (6 h) and chronic (1 to 20 d) effects of cimaterol (CIM) on skeletal muscle metabolism and protein accretion by use of close arterial infusion in the hindlimbs of six young steers. Surgical catheterizations were conducted to allow continuous infusion of CIM (.5 microg/min) or saline into the external iliac artery of contralateral hindlimbs and simultaneous sampling for arteriovenous difference measurements. Hindlimb blood flow and net flux of amino acids, glucose, lactate, and NEFA were determined during a basal period before infusion, at 6 h, and at 1, 3, 7, 14, and 20 d of infusion. Cimaterol infusion acutely stimulated blood flow and caused acute mobilization of nitrogen (alanine), NEFA, and lactate from the treated hindlimb. Cimaterol infusion increased net uptake of amino acids (P < .05) in treated and control hindlimbs after 1 d of CIM infusion, but a progressive increase between 1 and 14 d of infusion was observed only in the treated hindlimbs. Net uptake of total amino acids in the treated hindlimb was increased 50 and 80% (P < .05) at 7 and 14 d, respectively, when compared to the control hindlimb and was increased 260% at d 14 when compared with the basal period. Net amino acid uptake was not different between treated and control hindlimbs by d 20 of CIM infusion. Integration of net tyrosine and phenylalanine uptake over the entire infusion period predicted a 10% difference in skeletal muscle protein mass between treated and control hindlimbs. Semitendinosus and semimembranosus muscles in the treated hindlimb contained 9 and 11% greater protein content, respectively (P < .05), at the end of the infusion period. Results provide a quantitative description of the temporal pattern of transient effects of CIM on skeletal muscle metabolism and protein accretion and provide evidence that these are direct effects.

Adrenergic beta-Agonists↗

Temporal change in skeletal muscle IGF-I mRNA abundance and nitrogen metabolism responses to abomasal casein infusion in steers.

Skeletal muscle IGF-I and alpha-actin mRNA responses to increased amino acid availability were investigated in young, rapidly growing steers. Four Holstein steers (208 kg BW) were surgically implanted with an abomasal cannula and jugular catheters and allowed 2 wk to recover. Steers were offered hourly a 43:57 forage:concentrate diet at 95% of ad libitum intake supplemented with continuous abomasal infusion of glucose (to replace 12.5% of metabolizable ad libitum energy intake) for 13 d before the start of abomasal infusion of 67 g of casein N/d. Biopsies of the liver and both semimembranosus muscles were removed and frozen in liquid N, and casein infusion was begun. Muscle biopsies were collected at 8, 16, 24, and 48 h, and on d 7 and 14. Nitrogen balance increased from 23.6 to 71.5 g/d (P < .001) within 24 h and remained elevated (mean = 58.4 g/d) during the 14 d of casein infusion. Plasma urea N increased from 4 to 9.5 mg/dL at 24 h and remained unchanged to d 14. Muscle IGF-I mRNA abundance increased to 215% of basal values at 16 h (P < .01), 244% of basal values at 24 h, and 222% of basal values at 48 h after initiation of casein infusion. Values reached a maximum of 274% of basal values on d 7 and then declined to near preinfusion levels on d 14. The IGF-I mRNA abundance was approximately 100 times higher in liver than in skeletal muscle and was not different on d 0 and 14. Although plasma IGF-I concentrations were numerically higher during the first 24 h of abomasal casein infusion, they were not significantly higher during the chronic phase of treatment. Plasma IGF binding protein (BP)-2 concentrations were higher at 16, 24, and 48 h after casein infusion was begun, but IGFBP-3 concentrations were not altered at these sampling times. Neither acute (first 24 h) nor chronic (daily) plasma insulin concentrations were altered by abomasal casein infusion. Plasma somatotropin concentrations were lower (P = .008) at 24 h of casein infusion and beyond. Results suggest that enhanced amino acid availability may modulate skeletal muscle protein synthesis and accretion through an autocrine or paracrine IGF-I influence.

Abomasum↗

Effects of a dietary mixture of meat and bone meal, feather meal, blood meal, and fish meal on nitrogen utilization in finishing Holstein steers.

Our objective was to determine to what extent rate and efficiency of protein gain in finishing cattle can be enhanced by feeding an amino acid-balanced mixture of undegraded intake proteins. The Cornell Net Carbohydrate and Protein System (CNCPS) model was used to formulate a corn-based diet that would meet the rumen requirements for 410-kg large-framed steers with an estrogen implant and fed an ionophore. The CNCPS model was also used to formulate a highly undegradable intake protein (UIP) mixture from meat and bone meal, blood meal, fish meal, and hydrolyzed feather meal to provide the amino acids needed to supplement those derived from microbial protein to better meet amino acid requirements for growth. Four Holstein steers weighing 407 kg were offered a 90:10 concentrate-forage diet at hourly intervals at 95% of ad libitum intake. The steers were injected with 500 microg of estradiol-17beta at 12-h intervals to mimic the effects of an estrogenic implant. Treatments planned consisted of inclusion of the UIP mixture at 0, 2.5, 5, and 7.5% of the diet DM. Dry matter intake was fixed at 6.4 kg/d, and DM digestibility was not significantly affected by varying the amount of UIP addition. Apparent digestibility of N increased (P = .011) from 63.8 to 65.8, 70.7, and 71.5%, the amount of N absorbed increased (P = .001) from 73 to 84, 100, and 106 g/d, and N balance increased (P = .003) from 20 to 30, 33, and 39 g/d when UIP was fed at 0, 2.6, 5.2, and 7.8% of diet DM, respectively. The efficiency of N use increased 39.7%, and biological value increased 31.6% when the UIP mixture was added to the diet. Circulating concentrations of plasma urea N (PUN) were increased (P = .017) from 4.5 for the control diet to 5.7, 6.2, and 6.1 mg/dL when the UIP mixture was added at 2.6, 5.2, and 7.8%, respectively. Corresponding IGF-I concentrations were also increased from 491 to 558 and 624 ng/mL with 2.6 and 5.2% levels of UIP addition. Plasma glucose, NEFA, and insulin concentrations were not affected by feeding the UIP mix. The rate and efficiency of N use for growth improved with addition of an amino acid-balanced UIP mixture to the diet.

Amino Acids↗

Characterization of dose-dependent metabolic responses to close arterial infusion of cimaterol in the hindlimb of steers.

Dose-dependent effects of cimaterol (CIM) on hindlimb metabolism were determined in six steers (247 +/- 22 kg BW) using a close arterial infusion. The external iliac vessels of both hindlimbs were catheterized to accommodate measurement of blood flow, circulating concentrations, and net flux of NEFA, lactate, and alpha-amino nitrogen (AAN) during infusion of CIM at 0, .05, .1, .3, .7, 1 and 3 micrograms/ min. Close arterial infusion of CIM in the hindlimb of steers can be used to achieve a local concentration elevation that is required to differentiate local and systemic effects in vivo. Calculated plasma threshold CIM concentration required to initiate cardiovascular responses was 21 pg/mL, which resulted from an infusion rate of .3 microgram/min. Threshold concentrations of CIM for stimulation of NEFA and lactate net flux in the hindlimb were 38 and 34 pg/mL, respectively, and would be achieved with an infusion rate of .7 microgram/min. All measured responses except AAN net flux exhibited significant linear and quadratic dose effects, and responses in the treated hindlimb were always severalfold greater than in the contralateral control hindlimb. Maximal differences between treated and control hindlimb blood flow occurred with a CIM infusion rate of .7 microgram/min, but the highest infusion rate (3 micrograms/min) was required to maximize differences in NEFA and lactate flux. Therefore, to minimize cardiovascular and other systemic responses and optimize direct hindlimb responses, an infusion rate of .5 microgram of CIM/ min should cause significant stimulation of beta-adrenergic receptors only in the CIM-infused hindlimb of young, growing steers.

Adrenergic beta-Agonists↗

Impact of composition manipulation on lean lamb production in the United States.

At present less than 30% of the market lambs slaughtered in the United States meet the requirements for leanness and muscling as specified in the "Certified Fresh American Lamb" program established in 1990 by the American Sheep Industry Association (ASI). Carcass composition of slaughter lambs is determined by stage of growth relative to mature size, genotype, sex, and matching dietary nutriment to nutrient requirements for lean tissue growth. On the average, current production strategies produce carcasses that contain excessive amounts of fat, impeding optimized efficiency at all levels of production. Use of large-mature-size terminal sires, feeding rumen-escape dietary protein, feeding intact males, and slaughtering at appropriate weights all improve composition of gain. Improvements of 10 to 20% in rates of gain and efficiency of nutrient use and similar reductions in feed cost can be achieved with each of these management strategies. Results from several experiments demonstrate that these effects are additive and provide a measure of the true genetic capacity for protein accretion rate in growing lambs. Adoption of these management strategies will allow lambs to be slaughtered at a younger age, which may improve meat quality and concurrently reduce the amount of nitrogen waste returned to the environment. Potential for further manipulation of composition exists through more accurately defining nutrient requirements of growing lambs and through use of metabolism modifiers. Maintaining a competitive, profitable, and sustainable sheep industry depends on continued improvement of production efficiency, preferably in systems with high reproductive rates.

Animal Feed↗

Analysis and pharmacokinetics of cimaterol in growing Holstein steers.

Pharmacokinetic parameters for the beta 2-adrenergic agonist, cimaterol (CIM), were determined in growing Holstein steers. Compartmental analysis was used after measurement of CIM in body fluids by affinity chromatography and HPLC using UV detection. Recoveries from spiked plasma and urine standards were 70 +/- 1.2% and 68 +/- 1.1%, respectively. The minimum detection level in plasma was 1 ng/mL and the average CV was 5.1% for concentrations that ranged from 1 to 30 ng/mL. Four steers (276 +/- 24 kg) received 15 mg of CIM by bolus intravenous injection. Plasma CIM levels declined in a biphasic manner with half-lives of 2.5 min for the distribution phase and 54 min for the elimination phase. A two-compartment open model was used to describe the disappearance of CIM and the following pharmacokinetic parameters were obtained: central compartment volume (Vc) = .76 L/kg, apparent volume of distribution (Vd) = 4.1 L/kg, and transfer rate constants from the central to peripheral compartment (k12) = .177/min, from the peripheral to central compartment (k21) = .054/min and elimination from the central compartment (kel) = .074/min. After 8 h, total urinary CIM accounted for only 18.3% of the administered dose. Results suggest that circulating concentrations of CIM in growing steers are influenced by its accumulation in an unidentified peripheral pool and its conversion into unknown metabolite(s) before elimination.

Adrenergic beta-Agonists↗

Abomasal casein infusion and exogenous somatotropin enhance nitrogen utilization by growing lambs.

Growing Dorset wether lambs (23 kg initial body weight) were used to determine whether the magnitude of nitrogen retention response to daily administration of exogenous somatotropin is limited by post-ruminal amino acid availability in growing ruminants. Eight lambs surgically fitted with abomasal cannulae were fed a total mixed ration of 85% of ad libitum intake. All lambs received a continuous abomasal infusion of 2 L of water or casein and twice daily subcutaneous injections of 0 or 100 micrograms recombinant bovine somatotropin (rbST)/kg body wt for 15 d per treatment in a 2 x 2 single reversal design. The casein solution was infused at a rate (4 to 5 g nitrogen/d) to achieve 25% of nitrogen intake observed with ad libitum feeding prior to initiation of treatments. Each lamb received all four treatments. Nitrogen balance was determined on d 8 to 14 of each treatment. Casein infusion increased nitrogen balance 43.4% (P less than 0.001), and rbST increased nitrogen balance 33.5% (P less than 0.001), without significant interaction (P less than 0.88). Combined effects of casein and rbST were additive, resulting in an 89% increase in nitrogen balance when compared with water plus excipient treatment. Results suggest that the quantity or composition of absorbed amino acids, or both, limit nitrogen retention by growing lambs, and that rbST increases the efficiency of utilization of absorbed amino acids for protein deposition.

Abomasum↗

Localization of types I, III and IV collagen mRNAs in rat heart cells by in situ hybridization.

Previous studies investigating the cellular origins of several collagens in young adult rat hearts (Eghbali et al., 1988) demonstrated that the mRNAs for types I and III collagen occurred in non-myocyte cells, mostly fibroblasts, whereas the mRNA for type IV collagen was observed in both myocytes and non-myocyte cells. In the present study, cellular localization of collagen mRNAs has been achieved by in situ hybridization in rat heart tissue and in isolated heart cells. Frozen tissue sections, isolated cardiomyocytes, cultured neonatal cardiomyocytes and fibroblasts were hybridized with DNA probes for type-specific collagens, actin, and myosin heavy chain. Silver grains were visualized by dark field imaging. In heart sections, types I and III mRNAs were observed predominantly adjacent to myocytes and in the interstitium, where fibroblasts are known to be present. In contrast, type IV collagen mRNA was identified both within the myocytes and the interstitium. In freshly isolated adult cardiomyocytes and in cultured neonatal cardiomyocytes, collagen type IV mRNA was observed but type I collagen mRNA was not. In cultured neonatal fibroblasts, both types IV and I collagen mRNAs were abundant.

Animals↗

Collagen accumulation in heart ventricles as a function of growth and aging.

Increase in resting tension of left ventricular papillary muscle with age has been attributed to the amount of collagen present. We therefore studied the total amount and structure of myocardial collagen as a function of age in the hearts of male Fischer 344 rats. Using amino acid analysis and quantification of hydroxyproline, we showed that collagen accumulates in relation to ventricular protein after 3 months of age and continues in that mode with increased age of the animal, levelling off at 22 months. In this strain of rats, collagen increased in the left ventricle from 5.5% of total protein in a 1 month old animal to approximately 12% in 22 and 26 month old animals; in the right ventricle the increase was from 7% in the 1 month old animal to approximately 19.5% in 22-26 month old animals. The larger percentages of collagen in the right ventricle relative to the left agree with findings of others. Collagen accumulates in intrinsic collagenous structures where the pre-existing fibres are thickened and are more extensive. These structures were detected with light microscopy and scanning electron microscopy and include perimysial weaves, coiled perimysial fibres and struts. Regions of fibrosis were also increased in size and volume in older animals.

Aging↗

Alterations in collagen cross-linking impair myocardial contractility in the mouse heart.

A number of genetic disorders in humans are associated with defects in the synthesis and metabolism of collagen, which are accompanied by multiple cardiovascular disease processes. To determine whether genetically determined cross-linking abnormalities of collagen may alter cardiac function, left ventricular papillary muscles of mice with a genetic defect in the cross-linking of collagen (Movbr) were studied in vitro. With respect to controls, increases in time to peak tension, from 102 +/- 1.4 to 125 +/- 5.4 msec (p less than 0.001), and time to one-half relaxation, from 76 +/- 3.0 to 98 +/- 6.1 msec (p less than 0.05), were measured. Moreover, resting tension at the length associated with maximum developed isometric force (L) was elevated, from 11.1 +/- 1.7 to 19.3 +/- 1.1 mN/mm2 (p less than 0.001), and a similar difference was also seen throughout the physiological range of muscle lengths. In contrast, developed tension was depressed at 93-97% of L. Peak rate of tension rise and decay were diminished whereas time to peak rate of tension rise was prolonged. Isotonically, a decrease in the magnitude of peak shortening at L, from 4.0 +/- 0.5 to 2.0 +/- 0.2% (p less than 0.04), and an increase in time to peak shortening, from 100 +/- 2.3 to 129 +/- 2.8 msec (p less than 0.001), were seen. In addition, peak velocities of shortening and relengthening were diminished in the Movbr mouse heart. In conclusion, the impairment in collagen cross-linking alters cardiac mechanics by a reduction in force-generating ability and a prolongation of the timing parameters of the systolic and diastolic phases of contraction in vitro.

Animals↗

Visualization of collagenase-sensitive acetylcholinesterase in isolated cardiomyocytes and in heart tissue.

Previous studies have indicated that the asymmetric form of acetylcholinesterase (collagen-tailed) is localized in the basal lamina of the neuromuscular junction of skeletal muscle. The present study shows localization of the asymmetric acetylcholinesterase in the heart of the rat. Antiserum to 14 + 18 S acetylcholinesterase of the electric eel was raised in rabbits. The purified antibody did not react with collagen type I or laminin. Collagenase reduced the immunoreactivity of the enzyme with the purified antibody. Isolated cardiomyocytes and frozen sections of the heart were stained for acetylcholinesterase with the antibody. Diffuse immunofluorescence appeared over the surface of the cardiomyocytes. In the frozen sections, the immunofluorescence was most intense at the cell boundaries. These data suggest that collagenase-sensitive acetylcholinesterase in the heart is present in the myocytes and occurs in the vicinity of the basal lamina.

Acetylcholinesterase↗

Differentiating cardiac elastin, collagen and microfibrils with NaOH at the ultrastructural level.

NaOH solutions extract elastin and collagen from epoxy-embedded thin sections containing rat cardiac connective tissue. Extraction results in a reverse staining effect of elastin and collagen ultrastructure. Microfibril contrast is enhanced by NaOH treatment. This phenomenon finds application in the possibility of differentiating elastin, collagen, and microfibrils at the ultrastructural level.

Actin Cytoskeleton↗

The effects of acutely increased ventricular cavity pressure on intrinsic myocardial connective tissue.

Studies of normal hearts have revealed a variety of intrinsic connective tissue structures that surround and interconnect myocytes and ventricular mural layers. Among these structures, springlike coiled perimysial fibers, arrayed parallel to myocytes in the interstitial space, have been described in papillary muscle and ventricle. To evaluate the role of the coiled perimysial fibers under perturbed conditions, rat ventricles were filled with barium-gelatin under different pressures and fixed, and then the myocardium was impregnated with silver to visualize the connective tissue. Ventricles were filled at 30, 70 and 100 to 120 mm Hg. The coiled perimysial fibers were studied for their orientation, stretch, integrity and relation to sarcomere length. The coils were noted to embed within the fibrous anulus and to knot into an umbilical-like mass at the apex, thus anchoring them at both ends of the ventricle. They underwent focal straightening even at 30 mm Hg, with generalized straightening and disruption at the highest pressure; changes were most pronounced in the midventricle. Sarcomeres were maintained below 2.2 micron at 30 and 70 mm Hg of cavity pressure in regions of coiled perimysial fiber stretch; only with fiber disruption at 100 to 120 mm Hg were sarcomeres significantly lengthened. Other findings included connective tissue disruption between ventricular wall layers that allowed slippage of myocytes and mural thinning. These observations suggest that coiled perimysial fibers may act as a buffer to protect myocytes from damage under the effects of high cavity pressure.

Animals↗

Coiled perimysial fibers of papillary muscle in rat heart: morphology, distribution, and changes in configuration.

The morphology, distribution, and configuration of coiled perimysial fibers of rat heart papillary muscle were studied. Methods included bright-field light microscopy of silver-stained sections, scanning and transmission electron microscopy, and differential interference contrast light microscopy of unfixed and unstained specimens. Coiled fibers, elliptical in cross section, are arranged in a branched network that diverges from the muscle-tendon junction and is continuous throughout the length of the muscle and into the ventricle wall. Most fibers range in diameter from less than 1 micron to 10 micron and are parallel with the long axis of the muscle, although branching is common and oblique orientations are seen. Several myocytes are associated with each coiled perimysial fiber. Constituent fibrils (diameter, 40-50 nm) occur in bundles twisted within the fiber. Small satellite elastic fibers are parallel to the collagen fiber axes. Stereo analysis of the coiled perimysial fibers reveals helical configurations, as opposed to planar waviness, that become less convoluted or even straighten as the resting muscle is stretched. Calculations based on cross-sectional areas of fibers, changes in fiber configurations, and tensile moduli reported for collagen fibers of other tissues show that the potential tensile strength of the network of coiled perimysial fibers is sufficient to contribute significantly to the mechanical properties of papillary muscle. Detailed evaluations of possible roles of the coiled perimysial collagen fiber system as a function of passive stretch and contraction in ventricular wall, as well as in papillary muscle, warrant further study.

Animals↗

Comparative connective tissue structure-function relationships in biologic pumps.

A complex connective tissue framework exists in mammalian hearts that surrounds and interconnects individual myocytes and fascicles of cells. Recent evidence suggests that this connective tissue plays a role in maintaining shape, modulating contractile forces, and mediating elastic recoil during cavity filling and contraction. In order to analyze the involvement of connective tissue in pump contraction and recoil, we examined silver impregnated connective tissue in rat hearts which spontaneously jet through fluid ex vivo by contracting their cavities forcefully and then sucking fluid for the next cycle, and compared them to frog hearts which beat actively under the same conditions, but do not demonstrate jet propulsion. A further analysis was carried out in unrelated but analogous models: the squid and octopus. The former jets rapidly through the ocean, while the latter moves sinuously along the seabed. We observed highly interconnected myocytes in the rat heart, whereas frog myocytes are individually wrapped by connective tissue but are not interconnected. The squid mantle muscle is surrounded by a complex connective tissue grid that is tethered to each muscle cell, whereas the octopus mantle muscle cells are surrounded by connective tissue but are not tethered. These observations suggest that myocyte connective tissue tethering may be necessary for muscle cavities to generate forceful and coordinated contractions sufficient for rapid ejection and suction of fluid.

Animals↗

Structure and function of connective tissue in cardiac muscle: collagen types I and III in endomysial struts and pericellular fibers.

Heart myocytes and capillaries are enmeshed in a complex array of connective tissue structures arranged in several levels of organization: epimysium, the sheath of connective tissue that surrounds muscles; perimysium, which is associated with groups of cells; and endomysium, which surrounds and interconnects individual cells. The present paper is a review of work in this field with an emphasis on new, unpublished findings, including composition of endomysial fibers and disposition of newly described perimysial fibers. The role of scanning electron microscopy in the development of current understanding is also outlined. Biaxially arranged epimysial fibers form a sheath around papillary muscles and trabeculae that becomes increasingly well-oriented with the muscle axis during stretch. Perimysial structures are associated with groups of cells, and include weaves and septa of collagen, tendon-like fibers between weaves, ribbon-like fibers perpendicular to myocytes, and the newly described coiled perimysial fibers, which form an array in parallel with the myocytes and the epimysial net. The endomysium includes struts that bridge cells and pericellular fibers; both contain collagen types I and III. The evidence for the latter is presented in this paper and depends upon the use of antibody localization with fluorescent markers in light microscopy and colloidal gold for scanning electron microscopy. The implications of the composition of collagen fibers for myocardial function are discussed in relation to intra-cellular and other extra-cellular structures.

Animals↗

Morphology, composition, and function of struts between cardiac myocytes of rat and hamster.

The morphology, composition, and function of struts that interconnect the lateral surfaces of cardiomyocytes were examined in the hearts of rats and hamsters. Methods included brightfield and fluorescent light microscopy, secondary and backscatter scanning electron microscopy, and transmission electron microscopy in conjunction with silver stain, cationic dye, and antibody to type-I collagen. These studies reveal a twisted, beaded appearance and a complex substructure of collagen fibrils embedded in a ground substance that has a positive reaction with cationic dye. A hierarchy of patterns of branching and attachment was seen among intercellular struts ranging in diameter from 0.1 micron to several micron. The hypothesis that struts tether not only the surfaces but the contractile lattices of laterally adjacent myocytes is supported by the following: (a) the attachments of struts to the collagen weave of the sarcolemma, often lateral to the level of Z bands, (b) the presence of collagen type I in a composite material arrangement, (c) the relative dispositions and configurational changes of struts and myocyte surfaces in various physiological states and induced, non-physiological perturbations of cardiac muscle, (d) the corrugated sarcolemmas with infoldings near Z bands, and (e) the continuity of intracellular filaments from Z bands to the inner aspect of the sarcolemma in relaxed and contracted myocytes. Implications of struts acting as tethers and sites for storage of energy in the motions of myocytes during the cardiac cycle are discussed.

Animals↗