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Biomedical subjects

M B Mathews

Publications and source records attributed to M B Mathews.

At least 145 records · Page 8Linked to original sources

Conformation of hyaluronate in neutral and alkaline solutions.

Increasing the pH of a neutral salt solution of sodium hyaluronate to 12.5 produces a rapid drop in viscosity which is reversible upon restoring the pH to neutrality. Light scattering data showing a decrease in radius of gyration with no change in molecular weight and negative results with chondroitin and other acidic glycosaminoglycans suggest that the conformational change is specific for hyaluronate molecules.

Hyaluronic Acid↗

Comparative studies of water sorption of hyaline cartilage.

Vapor phase, water sorption isotherms were obtained for specimens of bovine, sturgeon and shark cartilage and for membranes composed of collagen and various proportions of cartilage proteoglycan. The data were interpreted in the light of an elementary model for swelling of gels which regards equilibrium swelling a resultant of a balance between contractile forces of an elastic matrix and expansive forces, principally osmotic in nature. Swelling ratios for bovine and sturgeon cartilage compared at the same water vapor pressure are nearly identical, whereas the swelling ratios for shark cartilage are elevated. These high values are due principally to a higher ratio of glycosaminoglycan to collagen but also reflect a higher salt and urea content and possibly also a different type of collagen fibril network.

Absorption↗

The gene and messenger RNA for adenovirus polypeptide IX.

A small RNA species, distinct from the VA RNAs, has been identified in HeLa cells infected with adenovirus type 2. The RNA, which has been purified using a novel screening procedure, is polyadenylated, sediments at 9S and has an estimated length of 550 nucleotides. In a cell-free translation system, the 9S RNA directs the synthesis of virion polypeptide IX, molecular weight 12,000 daltons. The location of its gene has been established by hybridization of the RNA to fragments of viral DNA produced by cleavage with restriction endonucleases: it spans position 10.0 on the r strand of the viral genome. These results unexpectedly place the gene for a "late" protein within a region of the genome which is transcribed early during infection

Adenoviruses, Human↗

Elastin and collagen accumulation in rabbit ascending aorta and pulmonary trunk during postnatal growth. Correlation of cellular synthetic response with medial tension.

Absolute and relative quantities of elastin, collagen, and DNA in anatomically defined segments of rabbit ascending aorta (AA) and pulmonary trunk (PT) were compared at intervals from birth to 2 months of age. Identical in size, weight, and composition at birth, the vessels maintained similar lengths and diameters at each age but diverged markedly in weight and scleroprotein content after 1 week. By 2 months, 3 times as much elastin and 1.7 times as much collagen had accumulated in the AA as compared to the PT. By contrast, the increase in total DNA content was the same for both segments. Differences in total fibrous protein accumulation, total elastin accumulation, and elastin content relative to DNA paralleled differences in estimated total medial tangential tension. Proportions of elastin and collagen relative to dry weight increased markedly only between 4 and 2 weeks of age and not thereafter despite continuing rapid growth, steadily increasing medial tension, and increasing total scleroprotein content. Thus, medial cells were capable of adapting their quantitative scleroprotein synthetic response to differences in medial tension throughout growth but established a fixed qualitative response within 2 weeks.

Animals↗

Cyclic stretching stimulates synthesis of matrix components by arterial smooth muscle cells in vitro.

Rabbit aortic medial cells were grown on purified elastin membranes, which were then subjected to repeated elongation and relaxation or to agitation without stretching. Cells remained attached to the membranes, and cyclic stretching resulted in a two- to fourfold increase in rates of collagen, hyaluronate, and chondroitin 6-sulfate synthesis over those in agitated or stationary preparations. Synthesis of types I and III collagen was increased to the same degree. Stretching did not increase rates of chondroitin 4-sulfate or dermatan sulfate synthesis. Differences were not attributable to differences in cell number, for DNA synthetic rates were not increased by stretching. The model system devised to demonstrate these effects provides a means for relating various modes of mechanical stimulation to cell metabolism.

Animals↗

A new species of virus-coded low molecular weight RNA from cells infected with adenovirus type 2.

A virus-coded low molecular weight RNA (5.2S), which migrates slightly faster on polyacrylamide gels than the well characterized adenovirus-specific 5.5S RNA, has been isolated from cells infected with adenovirus type 2. Hybridization-competition experiments and RNA fingerprints indicate that the two virus-associated (VA) RNAs differ in their primary structures. The gene for 5.2S RNA is located to the right of the gene for 5.5S RNA, on the I strand of a DNA segment which extends between positions 30.3 and 32.2 on the map of adenovirus type 2 DNA. Both 5.5S and 5.2S RNA can be detected early after infection and also in the presence of cytosine-arabinoside or cycloheximide. After the onset of viral DNA replication, the synthesis of 5.2S RNA levels off, whereas 5.5S RNA is synthesized in increasing amounts. Both 5.2S and 5.5S RNAs are synthesized in isolated nuclei by an enzyme which resembles RNA polymerase III in its sensitivity to alpha-amanitin. In isolated nuclei, both RNA species are labeled with beta-32P-labeled GTP, which suggests that they are initiated at separate promotor sites.

Adenoviridae↗

Composition of fluid from the notochordal canal of the coelacanth, Latimeria chalumnae.

Fluid from the notochordal canal of the coelacanth, Latimeria chalumnae, was analyzed for major inorganic and organic constituents and compared with blood serum from the same fish. Significantly or suggestively lower levels of sodium, magnesium, calcium, bicarbonate, sulfate, total carbohydrates, glucose, lactate, cholesterol, bound phosphate and total proteins were found in notochordal fluid than in serum, whereas potassium, chloride, urea, trimethylamine oxide, and total free amino acids were higher and inorganic phosphorus essentially identical. Osmolarity of notochordal fluid (1058 mOsm) exceeds that of serum (942 mOsm). A whitish precipitate in the fluid consisted of a matrix of fibers 100 A in diameter and of indefinite length. It resembled a sialoglycoprotein in composition and was stabilized by disulfide bonds. The fluid contained cellular debris.

Amino Acids↗

Genes for VA-RNA in adenovirus 2.

VA-RNA from adenovirus 2 (Ad2) infected cells is shown to consist of two species. The gene coding for the major species maps at position 30 on the viral DNA, where it spans a site cleaved by the restriction enzyme Bam Hl. The minor species, constituting a few percent of the total VA-RNA, is distantly related in oligonucleotide composition to the major species. Its template maps within 700 base pairs to the right of the gene for the major species. The direction of transcription is from left to right on the conventional Ad2 map. These results, gained with a novel method for blotting (E. M. Southern, manuscript in preparation), have also led to the identification of the Bam Hl recognition sequence.

Adenoviridae↗

Interactions of an intact proteoglycan and its fragments with basic homopolypeptides in dilute aqueous solution.

The interactions between a proteoglycan and cationic polypeptides have been investigated by the use of circular-dichroism spectroscopy. The interaction produces an induced conformational change for poly(l-arginine) and poly(l-lysine), similar to the effects previously reported for mucopolysaccharide-polypeptide mixtures. For bovine nasal septum proteoglycan, the interactions are similar to those for chondroitin 4-sulphate, which comprises approximately 63% of the total polysaccharide. The results also suggest that the interactions produce a conformational change in the protein core. Similar studies for the Smith-degradation product show that the protein core can adopt a substantial alpha-helical content and is capable of interactions with poly-(l-arginine). The interactions for chondroitin sulphate ;doublets' are significantly different from those for the separated chains, indicating that the arrangement of the polysaccharide side chains in pairs (and larger groups) along the protein backbone contributes to the interaction properties of the intact proteoglycan.

Animals↗