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C C SELBY

Publications and source records attributed to C C SELBY.

11 recordsLinked to original sources
PubMed1958

Observations on the fine structure of the turtle atrium.

The general fine structure of the atrial musculature of the turtle heart is described, including; the nature of the sarcolemma; the cross-banded structure of the myofibrils; the character of the sarcoplasm, and the form and disposition of its organelles. An abundant granular component of the sarcoplasm in this species is tentatively identified as a particulate form of glycogen. The myocardium is composed of individual cells joined end to end at primitive intercalated discs, and side to side at sites of cohesion that resemble the desmosomes of epithelia. Transitional forms are found between desmosomes and intercalated discs. Both consist of a thickened area of the cell membrane with an accumulation of dense material in the subjacent cytoplasm. This dense amorphous component is often continuous with the Z substance of the myofibrils and may be of the same composition. The observations reported reemphasize the basic similarity between desmosomes and terminal bars of epithelia and intercalated discs of cardiac muscle. Numerous unmyelinated nerves are found beneath the endocardium. Some of these occupy recesses in the surface of Schwann cells; others are naked axons. No specialized nerve endings are found. Axons passing near the sarcolemma contain synaptic vesicles, and it is believed that this degree of proximity is sufficient to constitute a functioning myoneural junction.

Animals↗
PubMed1956

The structure of paramyosin fibrils according to x-ray diffraction.

From analysis of x-ray diffraction patterns obtained with improved small-angle techniques has been derived the following description for the structure of the fibrils of the fibrous protein, paramyosin, obtained in this case from "white" portions of the adductor muscle of the clam, Venus mercenaria: 1. About 25 significantly different diffraction maxima have been resolved and found accounted for as (hk) reflections of a net whose cell elements are, for the dry material: a = 250 A, b = 720 A (fibril axis identity period), and gamma = 90.5 degrees (angle included between a and b axes). For rehydrated material a is larger (ca. 325 A), b is essentially unchanged, and gamma is slightly larger. There remains an unresolved discrepancy between the electron-optically derived, cell's a dimension (193 A) and that here reported for dry samples. 2. The h = +/-1 row lines are crossed on the diagrams (because gamma is not 90 degrees ) and thus can be distinguished in spite of natural "rotation" of fibrils (within the massive fibrous specimens) about their commonly oriented axes. The observed reflections are then found to obey a selection rule which indicates that the net cell is non-primitive and contains 5 equivalent locations (nodes) arranged as shown in Fig. 5. The nodal distribution is the same as has been previously photographed electron-optically. 3. Analysis of reflection lengths indicates that the native fibrils are not noticeably ribbon-like, having dimensions normal to the ordered net layers approximating their width across the fibril in the plane of the net layers. Corresponding transverse, interlayer spacings (possibly ca. 100 A) have not been observed, however, and may be hidden in troublesome central scatter. 4. Since paramyosin's wide-angle diffraction is very probably of alpha-type, supercoiled alpha-helices must be involved according to current interpretations of alpha-diagrams. Physicochemical evidence suggests that cables of this type, ca. 1400 A in length, may extend over two cells. Of two possible nodal connections, a favored one is shown in Fig. 5 to join 5 nodes in this way. Considerations of space filling, of transverse distribution of small-angle x-ray scattering, and of nodal significance, suggest that the cable units may be further aggregated into supercables, essentially forming rather solid rods of ca. 100 A diameter. 5. An alternative interpretation of the paramyosin small-angle diffraction, in particular of the observed selection rule, would conclude that large particles are arranged in a helical way, with minimum helix diameter about 150 A (dry). The simplest (genetic) particle connection would have 5 particles in 2 coil turns along 720 A of fibril or helix axis. This view is distinctly different from the arrangement of "rods" in net-like layers as given above, even though the rods are said to be made of supercoils or cables. Reasons are given for preferring the net-of-rods explanation over the particulate-helix model. The helix- vs. true-net ambiguity arises whenever the two types of structure are conceivable, and decision between them is difficult on the basis of the diffraction data alone.

Muscle Proteins↗
PubMed1956

The structure of actin-rich filaments of muscles according to x-ray diffraction.

From analysis of moderate- to small-angle x-ray diffraction patterns, in the light of similar experience with paramyosin, has been derived the following description for the structure of actin-rich filaments in "tinted" portions of the adductor muscle of the clam, Venus mercenaria: 1. Some 11 diffraction maxima, widely streaked along layer lines and occurring at moderate diffraction angles (spacings 7 to 60 A) appear to be accounted for as (hk) reflections of a net whose cell elements are, for dry material: a =... 82 A, b = 406 A (filament axis identity period), and gamma =... 82 degrees (angle between a and b axes). These reflections follow a selection rule which indicates that the net cell is non-primitive and contains 15 equivalent locations (nodes) arranged as shown in Fig. 5. An alternative net has b' = 351 A and 13 nodes per cell. 2. Another interpretation rolls the net into a large-scale helix and places the 15 (or 13) nodes along 7 (or 6) turns of a helical locus projecting 406 (or 351) A along the filament axis. Whether considered to be built of planar-net or helix-net cells, the individual filament contains a single cell width transverse to its axis. Transverse filament dimensions are, therefore, in either case similar (50 to 100 A). 3. Consideration of existing electron-optical, physicochemical, and x-ray diffraction data regarding isolated actin suggests that the net cell is built of rods, each containing in cross-section from one to four actin molecules which run parallel to or twisted about rod axes that extend at 12 degrees to the filament axis along the (21) diagonals of the cell. Depending on monomer shape, 2 to 15 monomers furnish length to reach across two cells, and the actin molecules are built into each rod in such a way as to repeat (or nearly repeat) structure 15 (or 13) times along the double cell length. Further details of intra-rod structure cannot be suggested because of lack of wide-angle diffraction information. 4. The actin system is sensitive to treatment of the muscle with ethanol. Concentrations of 5 per cent or greater abolish the net reflections. Other solvents-water, benzene, ether, pyridine, acetone-do not alter the pattern materially. 5. Two other reflections, occurring at the first and second layer lines of an axial periodicity of about 400 A, do not clearly belong to the actin-net system. They represent either a superstructure built upon the filaments by parts of the actin molecules themselves or by incorporated other molecular species, or they arise from an additional macromolecular component (possibly myosin, or its homologues or fractions) of similar axial periodicity.

Actin Cytoskeleton↗
PubMed1955

An electron microscope study of the epidermis of mammalian skin in thin sections. I. Dermo-epidermal junction and basal cell layer.

1. Basal epidermal cells and their junction with the dermis, as revealed in thin sections of osmium-fixed human and rodent skin, were studied with the electron microscope. Phosphotungstic acid staining was occasionally used to increase the electron density of membranous and filamentous structures. 2. Along the dermo-epidermal junction in all skin specimens there is a sub-microscopic ( approximately 350 A thick) membrane following the basal contours of the epidermal cells, but separated from them by an approximately 300 A space. No epidermal or dermal filaments can be seen to cross it and except in embryonic skin it has no associated band of amorphous material. It is called the "dermal membrane" to distinguish it from the thicker membrane and associated material commonly called the "basement membrane." 3. In adult human skin the basal cell membrane facing the dermal membrane is continuous with, or adjacent to regularly spaced groups of small dense rodlets at which tonofilaments are attached and appear to terminate. Less dense spherical granules are also found in the cellular ectoplasm and are unattached to filaments. 4. The connective tissue fibers in the upper dermis were narrower (>==300 A) than, but displayed the same period (>==350 A) as the collagen fibers in the deeper dermis. The related fibers in embryonic human skin were even narrower (150 to 250 A). In accordance with the views of others that these are "young" collagen with great affinity for polysaccharide, they are called collagen fibers. 5. The same cytoplasmic components are found in all basal epidermal cells: mitochondria, many filaments, many submicroscopic particulates, and only very occasional vesicles of the endoplasmic reticulum. Adult human cells possess pigment granules and intercellular bridges, in addition. Before keratinization is evident, no intercellular bridges and little or no cytoplasmic filaments are visible. The scarcity of vesicles of the endoplasmic reticulum and the prevalence of submicroscopic particulates (80 to 150 A) distributed at random through the cytoplasm, support the view (19) that basophilia and cytoplasmic nucleoprotein are associated with the particulates. 6. Cytoplasmic filaments are <100 A wide and are directed toward the dermo-epidermal junction and to intercellular bridges (when they occur). Because of their obvious identity as the submicroscopic constituents of tonofibrils, they were called "tonofilaments" and believed to represent the keratin-like fibrous protein "epidermin" (29). Bundles of them appear identical with Herxheimer fibers when, particularly in thick skin, they extend from the outer nuclear membrane to the granules spaced along the dermo-epidermal junction. 7. In human skin, adjacent basal cells are separated by simple cell membranes and connected by intercellular bridges. The filaments of one cell are attached to dense elongate granules in these bridges which are separated by a narrow less electron-dense space from a matching granule to which the filaments of the neighboring cell are attached. No filaments have been observed to cross the space in these bridges. In between the bridges adjacent cell membranes may separate from each other leaving an intercellular space. Although occasional basal cells possess a large perinuclear area devoid of cytoplasmic filaments, none following the classical histological description of "clear" cells were noted. 8. Pigment granules are extremely electron-dense with irregular angular outline. Their smallest diameter was significantly greater in Negro than in white skin while the lengths also appeared greater in the former skin type.

Electrons↗