Biomedical subjects

M W Orcutt

Publications and source records attributed to M W Orcutt.

4 recordsLinked to original sources

PubMed1992

Preparation of muscle samples for comparative electron microscopy.

The interpretation of muscle structure by scanning electron microscopy (SEM) has not been consistent among various studies. Consequently, the literature is confusing with respect to the identity of T-tubules, transverse ridges, Z-disks, and intermyofibrillar connections. The objective of this research was to evaluate the effects of different methods of sample preparation and imaging on ultrastructural details of previously identified transverse structures and intermyofibrillar connections and to verify or disprove the commonality of these structures under different viewing conditions. Scanning electron microscopy coupled with a cold stage, SEM at room temperature, and transmission electron microscopy (TEM) of thin sections were most appropriate for exposing detail of inter- and intracellular structures and for measuring sarcomere length and spacing of intermyofibrillar connections. Scanning electron microscopy of samples mounted on a cold stage, fractured, and sublimed provided excellent images of meat and muscle ultrastructure and may be used in correlative microscopy. Sarcomere length and spacing between intermyofibrillar connections were similar among most specimen preparation techniques and were affected similarly by heat treatments. Results indicate that the regularly spaced transverse structures viewed by conventional SEM and the intermyofibrillar connections viewed by low-temperature SEM are Z-disks.

Animals↗

PubMed1991

Effects of the beta-adrenergic agonist isoproterenol on protein accretion, synthesis, and degradation in primary chicken muscle cell cultures.

Seven-day-old primary myotube cultures derived from embryonic chicken limb muscles were used to determine the effects of the beta-adrenergic agonist isoproterenol (ISO) on muscle protein metabolism in vitro. Isoproterenol increased (P less than .05) total protein accumulation after 2 h of acute exposure and after chronic exposure for 24 and 48 h. Isoproterenol did not consistently retard rate of protein degradation of the total protein (TP), myofibrillar protein (MFP) pools, and myosin heavy-chain subunit (MHC); degradation of these protein pools tended to be slowed by inclusion of ISO in the culture medium. After acute treatment of 1 X 10(-4) M ISO for 2 h, TP, but not MFP and MHC, synthesis rate was increased, and after chronic exposure to 1 X 10(-4), 1 X 10(-5), and 1 X 10(-6) M ISO, TP, MFP, and MHC synthesis rates and net accumulation of TP, cytoplasmic protein, and MHC fractions were enhanced (P less than .05). The beta-adrenergic antagonist propranolol (1 X 10(-5) M) blocked chronic stimulatory effects of ISO. Furthermore, after 48 h of exposure to ISO, effects on protein synthesis were less pronounced than those observed after 24 h of exposure. Isoproterenol imparted a more pronounced effect on protein synthesis than on protein degradation, indicating that increased muscle protein accretion observed in animals after ISO treatment is likely a function of enhanced protein synthesis.

Animals↗

PubMed1990

Practical means for estimating pork carcass composition.

Three hundred sixty-one market-weight barrow and gilt carcasses were physically dissected into bone, skin, fat and muscle. A three-variable multiple linear regression equation containing the same independent variables (warm carcass weight, 10th rib loin muscle area and 10th rib fat depth) used (U.S.) to determine pork carcass lean weight was found to be the most practical means for predicting weight of muscle standardized to 10% fat. Multiple linear regression equations containing more than three independent variables produced only slight improvements in R2 values; however, the standard deviation about the regression line was not greatly improved by the addition of more independent variables to this three-independent-variable regression model. A single multiple linear regression equation using the three independent variables above may not be adequate to describe variation over the entire live-weight range for all hogs marketed in the U.S. For most accurate muscle weight prediction, different equations should be used for weight subclasses with one equation for carcasses under 100 kg and another for those heavier than 100 kg. A single prediction equation for muscle weight was adequate for carcasses of both barrows and gilts.

Adipose Tissue↗

PubMed1982

Cell differentiation, protein synthesis rate and protein accumulation in muscle cell cultures isolated from embryos of layer and broiler chickens.

Muscle cell cultures were prepared from the leg muscle of 12-d layer and broiler chicken embryos. Cultures were then compared over a 10-d period from their capacity to differentiate into multinucleated myotubes and to synthesize and accumulate protein. Differentiation was qualitatively similar in the two cell types as evidenced by myoblast fusion that occurred rapidly during the first 2 d and remained essentially constant between d 3 and 10. However, several quantitative differences were observed. Even though the number of myotubes per culture was comparable between layers and broilers throughout development, layer muscle cultures usually exhibited a higher percentage fusion and more myonuclei per culture than broiler muscle cultures. Additionally, the nuclear density (i.e., the number of nuclei per myotube segment) was approximately 25% greater in layer cultures than in broilers between d 2 and 10 in culture. The rate of incorporation of 3H-leucine into total protein during pulse labeling experiments was comparable in muscle cultures of layers and broilers; however, broiler muscle cells accumulated approximately 40% more total protein per nucleus between d 6 and 10. Myosin heavy chain synthesis rate was higher in layer than in broiler muscle cultures, but broiler muscle cultures accumulated approximately 30% more myosin heavy chain than layers between d 6 and 10. The half-life of myosin heavy chain was 45 h in layer muscle cultures and 103 h in broiler muscle cultures. Thus, the capacity of broiler cells to accumulate more muscle protein was primarily due to a drastically slower protein breakdown rate.

Animals↗