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Biomedical subjects

P Elsbach

Publications and source records attributed to P Elsbach.

At least 109 records · Page 6Linked to original sources
PubMed1972

The appearance of lecithin- 32 P, synthesized from lysolecithin- 32 P, in phagosomes of polymorphonuclear leukocytes.

Rabbit polymorphonuclear leukocytes ingesting paraffin oil particles stabilized with albumin, converted more lysolecithin-(32)P (added to the medium as an albumin complex) to cellular lecithin than did control cells. Almost all of the increment in leukocyte lecithin-(32)P is found in association with the isolated phagocytic vacuoles. About half of lecithin-(32)P of granulocytes incubated first with lysolecithin-(32)P and then reincubated with paraffin particles in a nonradioactive medium is transferred from a sedimentable (presumably membrane) fraction to the phagosomes. Isolated phagosomes or granules by themselves are capable of acylating lysolecithin. The main source of lysolecithin-(32)P for synthesis of cellular lecithin-(32)P, however, appears to be extracellular rather than lysolecithin-(32)P within the cytoplasm or the phagocytic vacuole. We interpret our findings therefore as indicating that lecithin-(32)P in the phagosomes derives chiefly from the outer membrane.

Animals↗
PubMed1971

The interaction in vitro between polymorphonuclear leukocytes and mycoplasma.

The interaction, between mycoplasma (PPLO) and human or rabbit leukocytes was examined in vitro. Upon incubation of M. hominis or M. arthritidis for 2 hr with rabbit peritoneal exudate granulocytes or leukocytes from human peripheral blood, no killing of mycoplasma was observed either in the presence or absence of type-specific antiserum. However, (14)CO(2) production from glucose-1-(14)C was stimulated up to 10-fold in the presence of live or heat-killed PPLO. The extent of stimulation depended upon the number of organisms and the presence of type-specific antiserum. The stimulation of (14)CO(2) production seems not because of tight adherence of PPLO to the leukocytes, since PPLO were quantitatively recovered in the medium after sedimenting the granulocytes. The enhanced conversion of medium lysolecithin to cellular lecithin that accompanies phagocytosis of polystyrene particles was significantly reduced when PPLO were also present. Mycoplasma alone elicited no stimulation of lecithin formation. Killing of E. coli, a microorganism readily engulfed and killed by leukocytes in vitro, was diminished when the leukocytes were preincubated with mycoplasma. These findings indicate that M. hominis and M. arthritidis are not ingested by granulocytes to any detectable extent, but that these organisms affect the leukocytes' metabolism and also impair phagocytosis of E. coli.

Animals↗
PubMed1971

The effects of the morphine analogue levorphanol on leukocytes. Metabolic effects at rest and during phagocytosis.

Studies on bacteria have suggested that morphine-like drugs have effects on the cell membrane. To determine the effect of this class of drugs on a mammalian cell, we selected the rabbit peritoneal exudate granulocyte, which undergoes striking membrane changes during phagocytosis. We examined the effect in vitro of the morphine analogue, levorphanol on phagocytosis and metabolism by granulocytes incubated with and without polystyrene particles or live Escherichia coli. Levorphanol (1 or 2 mmoles/liter) decreased: (a) acylation of lysolecithin or lysophosphatidylethanolamine in the medium (which is stimulated about two-fold during phagocytosis) both at rest (40%) and during phagocytosis (60%); (b) uptake of latex particles and Escherichia coli, as judged by electron microscopy; (c) killing of live Escherichia coli (10-fold); (d) (14)CO(2) production from glucose-1-(14)C during phagocytosis by at least 80%; (e) K(+) content of granulocytes (35%); (f) oxidation of linoleate-1-(14)C by 50%, and its incorporation into triglyceride by more than 80%. However, levorphanol stimulated 2 to 3-fold the incorporation of linoleate-1-(14)C or palmitate-1-(14)C into several phospholipids. Glucose uptake, lactate production, and adenosine triphosphate (ATP) content are not affected by the drug. Thus, levorphanol does not appear to exert its effects through generalized metabolic suppression. Removal of levorphanol by twice resuspending the granulocytes completely reverses all inhibition. In line with observations on bacteria, it appears that the complex effects of levorphanol on granulocytes may be due at least in part to an effect on the cell membrane.

Animals↗
PubMed1969

Triglyceride formation and hydrolysis by toad bladder epithelium.

Triglycerides of toad bladder epithelium have been labeled in vitro with either palmitate-1-(14)C or linoleate-1-(14)C, during incubation of bladders that had been cut in halves. Hydrolysis with pancreatic lipase of triglycerides labeled in this fashion revealed that palmitate-1-(14)C appeared predominantly in the 1- and 3-position, whereas half of linoleate-1-(14)C was located in the 2-position. The hydrolysis of palmitate-1-(14)C or linoleate-1-(14)C labeled triglycerides was examined in homogenates of isolated bladder mucosal cells. Lipase activity was evident from pH 3.5 to 8.0, but clearly greatest at pH 4.5. Below pH 6.0 the products of hydrolysis were fatty acid and monoglyceride and the 1- (or 3-) position was preferentially attacked; above pH 6.0 complete deacylation occurred. Acid-optimum hydrolysis of triglycerides with production of monoglycerides was linear for about 30 min. After 2 hr most of the labeled triglycerides were hydrolyzed. Repeated freezing and thawing of the homogenate enhanced lipase activity. Added Ca(++), previously shown to be required for phospholipase A activity in toad bladder, had no effect on hydrolysisof triglycerides. This lipase activity directed at the considerable store of triglycerides present in toad bladder epithelium may provide fatty acid for energy production or for synthesis of other esters such as in phospholipids.

Animals↗
PubMed1968

Increased synthesis of phospholipid during phagocytosis.

Incorporation in vitro of (32)P-labeled lysolecithin (LPC) or lysophosphatidylethanolamine (LPE) into respectively lecithin (PC) and phosphatidylethanolamine (PE) of rabbit granulocytes and alveolar macrophages was compared in the absence and in the presence of ingestible particles. Maximal synthesis of PC by intact cells occurred at added LPC concentrations of less than 0.05 mmole/liter, i.e., at levels found in plasma. Accumulation of PC-(32)P proceeded linearly for at least 30 min and varied directly with cell concentration. While per cell granulocytes and macrophages converted comparable amounts of medium LPC to cellular PC, per milligram of protein, the granulocytes were approximately four times more active than the much larger macrophages. After 30 min newly synthesized PC-(32)P represented as much as 5% of total granulocyte PC. For macrophages this fraction did not exceed 1%. Addition of polystyrene or zymosan particles to the cell suspension resulted in up to 3-fold stimulation of incorporation of LPC-(32)P or LPE-(32)P into their respective diacyl derivatives. This stimulation did not occur when the cells were homogenized. Breakdown of LPC to water-soluble products during phagocytosis of polystyrene particles was the same as at rest. By use of doubly labeled LPC, the mechanism of PC synthesis by the two cell types has been identified as direct acylation of medium LPC, both at rest and during engulfment. Evidence presented in the case of granulocytes suggests that the increased translocation of medium LPC-(32)P during phagocytosis and its conversion to PC represents net synthesis. The findings indicate that LPC, a normal constituent of plasma, can serve as substrate in PC synthesis by phagocytic cells. This mechanism of PC synthesis can account for appreciable addition of membrane PC, especially by granulocytes. It is proposed that stimulation of this pathway provides building blocks for increased membrane formation during phagocytosis.

Amino Alcohols↗
PubMed1967

Metabolism of lysophosphatidyl ethanolamine and lysophosphatidyl choline by homogenates of rabbit polymorphonuclear leukocytes and alveolar macrophages.

A comparison has been made between the conversion of (32)P-labeled lysophosphatidyl ethanolamine (LPE) and lysophosphatidyl choline (LPC) to their respective acylated and deacylated derivatives by homogenates of rabbit polymorphonuclear leukocytes and alveolar macrophages. Synthesis of PE by both homogenates and of PC by macrophage homogenates proceeded to about the same extent and is attributed to direct acylation of the lyso compounds. At higher LPC concentrations formation of PC by leukocytes is far greater than by macrophages. The mechanism of this enhanced synthesis of PC, which is brought out by higher substrate concentrations, is believed to be a transfer of the acyl group of one LPC molecule to another. Under optimal conditions macrophage homogenates deacylated LPE to a greater extent than LPC, while the reverse was true for leukocyte homogenates. Albumin inhibited deacylation of LPC and its conversion to PC by leukocytes, perhaps by binding the substrate (2 moles of LPC per mole of albumin). Other effects of albumin-stimulation of deacylation and acylation of LPE by macrophages, inhibition of deacylation and acylation of LPE by leukocytes-remain unexplained.

Albumins↗