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Biomedical subjects

D Mazia

Publications and source records attributed to D Mazia.

At least 55 records · Page 3Linked to original sources

Bioelectric responses of the echinoderm egg to fertilization.

The fertilization reaction of echinoderm eggs (Lytechinus pictus, a sea urchin, and Dendraster excentricus, a sand dollar) was followed with intracellular electrodes. Membrane potential and K(+) activity were recorded. The unfertilized egg of Lytechinus has a membrane potential of -8 mV, inside negative. Within 5 sec after the addition of sperm, a fertilization action potential develops, going to +10 mV, inside positive. The time from the initial depolarization to a return to the original -8 mV is 120-150 sec. The repolarization continues until a potential of -10 to -14 mV is reached, at which point it pauses for 3-4 min. At 6-8 min after fertilization, a further and relatively rapid hyperpolarization begins, going to -60 to -65 mV by 15-25 min after fertilization and remaining constant at these values. The membrane potential of the unfertilized egg appears to depend on a general permeability to anions. The fertilization action potential seems to reflect a prolonged influx of sodium. The final depolarization to -60 mV is attributable to the development of potassium conductance. Simultaneous measurements with a K(+) ion-selective electrode gives constant readings of about 240 mM K(+) in the unfertilized eggs throughout the fertilization process. Similar results were obtained with Dendraster eggs. The resting potential of the unfertilized eggs was -7 mV; the action potential on activation attained +18 mV; the repolarization paused at -16 to -24 mV and the final potential attained was -70 mV. The electrical changes after fertilization with spermatozoa or activation with Pronase were identical.

Action Potentials↗

Abnormal membrane protein of red blood cells in hereditary spherocytosis.

We present evidence that the hereditable hemolytic disease, hereditary spherocytosis (HS), involves an abnormality in protein of the red cell membrane. Unlike that from normal red cells, lipid-free proteins extracted from HS red cell membranes fail to increase in sedimentation rate when treated with cations; such treatment of normal membrane proteins has been shown by others to cause the formation of microfilaments. That microfilament formation might be defective in HS red cell membranes is supported by observations with vinblastine. This compound, a potent precipitant of filamentous, structure proteins throughout phylogeny, precipitates significantly less HS membrane protein than normal. The resistance of HS membrane protein to changes in conformation by cations is observable at the cellular level as well. That is, both normal and HS red cells agglutinate after repeated washing and suspension in electrolyte-free media. Tiny concentrations of Ca(++) (5 x 10(-5) M) changes the surfaces of normal cells in such a way as to cause disagglutination; HS red cells resist this change and remain agglutinated unless Ca(++) concentrations are increased many-fold. We conclude that membrane ("structure") proteins of HS red cells are genetically altered in such a way as to interfere with their proper conformation, perhaps into fibrils. Potentially many mutations in membrane proteins might preclude this alignment, with the result that normal erythrocyte biconcavity and plasticity is prevented and the clinical syndrome of hereditary spherocytosis is manifest.

Blood Protein Disorders↗

Precipitation of proteins by vinblastine and calcium ions.

We have found that vinblastine sulfate can precipitate a number of proteins in addition to microtubule protein. Those proteins which precipitate with vinblastine sulfate, all of which were derived from structure, also precipitate with Ca(2+) ions. Our results suggest that vinblastine sulfate, presumably acting as a cation, precipitates proteins by combining with sites which can also combine with Ca(2+) ions.

Animals↗