Biomedical subjects

J Megerman

Publications and source records attributed to J Megerman.

4 recordsLinked to original sources

PubMed1992

Magnetic resonance imaging of small arteries.

Magnetic resonance imaging (MRI) with receive-only surface coil technology was used to visualize and quantitative luminal diameters of small arteries in the rat. MRI measurements of normal and aneurysmal aortas, over a diameter range of 1-3 mm, were closely correlated with direct measurements made visually at laparotomy: measured differences averaged 0.16 mm, and the least-squares regression line (R2 = 0.97, P < 0.001) compared favorably to the line of equivalence, X = Y. This noninvasive but precise imaging modality demonstrates the potential value of using MRI to evaluate the diameter of small vessels, including the postoperative monitoring of arterial bypass graft patency in peripheral regions.

Abdomen↗

PubMed1979

In vivo measurement of blood vessel wall thickness.

To understand the mechanical properties of arteries and vascular grafts, it is crucial that the wall thickness in these vessels be known. Unfortunately, all availble methods for measuring this parameter require the removal of the vessel, which precludes the study of such vessels as a function of time. A new radiographic technique for measuring the wall thickness of arteries and vascular grafts in vivo, utilizing contrast materials injected into the vessel lumen and applied to the outer surface of the vessel, is described. Radiographs are obtained with a portable X-ray machine and analyzed using a calibrated microscope. The technique has been successfully applied to the in vivo measurement of wall thickness in canine arteries, veins, and experimental vascular grafts. It is concluded that the method provides better than 95% accuracy in a variety of vessels and that it can be used to study changes in vascular grafts after their implantation into the arterial circulation.

Angiography↗

PubMed1977

Assembly of smooth muscle myosin into side-polar filaments.

The in vitro assembly of myosin purified from calf aorta muscle has been studied by electron microscopy. Two types of filament are formed: short bipolar filament similar to those formed from skeletal muscle myosin, and longer "side-polar" filaments having cross bridges with a single polarity along the entire length of one side and the opposite polarity along the other side. Unlike the case with skeletal myosin filaments, antiparallel interactions between myosin molecules occur along the whole length of side-polar filaments. The side-polar structure may be related to the in vivo form of myosin in vertebrate smooth muscle.

Animals↗

PubMed1975

Myosin from arterial smooth muscle: isolation following actin depolymerization.

The contractile proteins from arterial smooth muscle are highly soluble, and can be extracted at I = 0.05. However, they can be precipitated by a prolonged dialysis at pH 6 to give an actomyosin with a high, although variable, actin:myosin ratio. The sedimentation behavior of this actomyosin at high ionic strength was examined as a function of pH, protein concentration and composition by preparative ultracentrifugation. Comparisons with synthetic skeletal muscle actomyosins of similar composition demonstrated significant differences in the behaviors of these two systems. It was found that much smooth muscle actomyosin is not dissociated by normally relaxing conditions, and that it sediments at a slower rate than F-actin. The solubility of the supernatant protein (a myosin-enriched actomyosin) in 0.2 M K Cl (pH 7) depended on the pH during centrifugation. A lower solubility was associated only with a higher actin concentration in the supernatant, suggesting a dependence on actin repolymerization. Pure myosin was selectively precipitated from the supernatant by polyethylene glycol-6000, but only when the protein was soluble at low ionic strength. The solubility of purified myosin was similar to that of myosin from striated muscles. A relationship between the presence of depolymerized actin and the high solubility of smooth muscle contractile proteins is suggested.

Actins↗