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Biomedical subjects

I J Kaplin

Publications and source records attributed to I J Kaplin.

6 recordsLinked to original sources
PubMed1994

Formation of surface membranes in developing mammalian hair fibres.

Mammalian hair fibres result from complex mechanisms involving synthesis, assembly and stabilisation of keratin proteins in the follicle. The developing hair shaft consists of outer cuticle cells surrounding cortical and medullary (optional) cell types. Presumptive fibre cuticle (FC) is contained by the inner root sheath (IRS) consisting of IRS cuticle, Huxley and Henle cells which are in turn enclosed in an outer root sheath (ORS) of epidermal-like cells. In the current structural studies we have used energy filtered transmission electron microscopy (Zeiss 902A) on Merino sheep skin biopsies to examine the fine sequence of morphological changes involved in forming the fibre surface membrane and the associated underlying structural bands comprising the a-layer and exocuticle. Prior to the development of the exocuticle, FC cells demonstrate a typical plasma-membrane apposed to IRS cuticle plasma-membranes separated by an intercellular space. The formation of exocuticular lamellae is followed by degradation of the residual FC surface membrane and the appearance of intercellular laminae demonstrating a stained central band. As maturation continues cleavage between IRS cuticle and FC occurs along this central band liberating hair into the pilary canal. The mature surface consists of keratinized cells containing a well developed exocuticle and a-layer coated with paired lamina (presumably two lipid containing bilayers) of material approximately 10-12 nm thick derived from the intercellular laminae. The current observations show FC surface formation is similar to processes occurring in epidermal stratum corneum and that the cuticle surface membrane of mammalian fibres is not derived from a modified plasma-membrane as previously documented.

Animals↗
PubMed1991

Physicochemical characterization of dodecylphosphocholine/palmitoyllysophosphatidic acid/myelin basic protein complexes.

The stoichiometry of dodecylphosphocholine/palmitoyllysophosphatidic acid/myelin basic protein complexes and the location of the protein in the micelles have been investigated by electron paramagnetic resonance, ultracentrifugation, small-angle X-ray scattering, 31P, 13C, and 1H nuclear magnetic resonance spectroscopy, and electron microscopy. Ultracentrifugation measurements indicated that well-defined complexes are formed by association of one protein molecule with approximately 133 detergent molecules. The spin-labels 5-, 12-, and 16-doxylstearate have been incorporated into detergent/protein aggregates. Electron paramagnetic resonance spectral parameters and 13C and 1H nuclear magnetic resonance relaxation times showed that the addition of myelin basic protein does not affect the environment and location of the labels or the organization of the micelles. Previous results suggesting that the protein lies primarily near the surface of the micelles have been confirmed by comparing 13C spectra of the detergents with and without protein with spectra of detergent/protein aggregates containing the spin labels. Electron micrographs of the complexes taken by using the freeze-fracture technique revealed the presence of particles with an estimated radius about three times the radius of the micelles measured by small-angle X-ray scattering. The structural integrity of the complexes appears to be based on intramolecular protein interactions as well as protein-detergent interactions.

Animals↗
PubMed1990

Effect of quinidine on platelets.

The effects of quinidine on platelets over a wide range of concentrations of the drug were studied. It was found that quinidine at high concentrations (1 and 1.5 mM) induced platelets to undergo profound ultrastructural changes and 14C-serotonin release. In addition, the drug at these concentrations caused marked inhibition of platelet aggregation mediated by adenosine diphosphate, adrenaline, collagen and arachidonate but had no effect on ristocetin-induced agglutination. However, quinidine at 10 microM (a pharmacological concentration) had only a variable inhibitory effect on adrenaline-induced platelet aggregation.

Blood Platelets↗
PubMed1988

Characterization of dodecylphosphocholine/myelin basic protein complexes.

The stoichiometry of myelin basic protein (MBP)/dodecylphosphocholine (DPC) complexes and the location of protein segments in the micelle have been investigated by electron paramagnetic resonance (EPR), ultracentrifugation, photon correlation light scattering, 31P, 13C, and 1H nuclear magnetic resonance (NMR), and electron microscopy. Ultracentrifugation measurements indicate that MBP forms stoichiometrically well-defined complexes consisting of 1 protein molecule and approximately 140 detergent molecules. The spin-labels 5-, 12-, and 16-doxylstearate have been incorporated into DPC/MBP aggregates. EPR spectral parameters and 13C and 1H NMR relaxation times indicate that the addition of MBP does not affect the environment and location of the labels or the organization of the micelles except for a slight increase in size. Previous results indicating that the protein lies primarily near the surface of the micelle have been confirmed by comparing 13C NMR spectra of the detergent with and without protein with spectra of protein/detergent aggregates containing spin-labels. Electron micrographs of the complexes taken by using the freeze-fracture technique confirm the estimated size obtained by light-scattering measurements. Overall, these results indicate that mixtures of MBP and DPC can form highly porous particles with well-defined protein and lipid stoichiometry. The structural integrity of these particles appears to be based on protein-lipid interactions. In addition, electron micrographs of aqueous DPC/MBP suspensions show the formation of a small amount of material consisting of large arrays of detergent micelles, suggesting that MBP is capable of inducing large changes in the overall organization of the detergent.

Animals↗
PubMed1978

An electron microscope study of fibril: matrix arrangements in high- and low-crimp wool fibres.

The crimped structure of wool fibres is generally associated with a bilateral arrangement of ortho- and paracortical cells. The most obvious difference between these cell types is in the arrangement and relative proportions of microfibril and matrix proteins that constitute the fibre cortex. In the low-crimp fibres examined there is a poorer expression of bilateral cortical asymmetry compared with the high-crimp wools together with a higher proportion of intermediate-staining mesocortical cells. These mesocortical cells exhibit much more regular arrays of microfibrils than paracortical cells. It is suggested that the packing arrangement of microfibrils in all three cell types is basically hexagonal and the variation observed in mature cells is a function of the fibril:matrix ratio.

Animals↗