Biomedical subjects

R D Moreno

Publications and source records attributed to R D Moreno.

23 records · Page 2Linked to original sources

PubMed1996

Tetrameric (G4) acetylcholinesterase: structure, localization, and physiological regulation.

Acetylcholinesterase (AChE), a highly conserved enzyme in the animal kingdom, is distributed throughout a wide range of vertebrate tissues where it is expressed as multiple molecular forms comprising different arrangements of catalytic and structural subunits. The major AChE form in the CNS is an amphiphilic globular tetramer (G4 AChE) consisting of four identical catalytic subunits attached to cellular membranes by a hydrophobic noncatalytic subunit (P-subunit). This study focuses primarily on current data involving the structure of the G4 AChE P-subunit, the expression and regulation of G4 AChE during development and adulthood, and its role(s) in certain neurological disorders including Alzheimer's disease.

Acetylcholinesterase↗

PubMed1995

Mitosis of Schwann cells and demyelination are induced by the amyloid precursor protein and other protease inhibitors in the rat sciatic nerve.

We studied the cytological alterations produced in the rat sciatic nerve by the amyloid precursor protein (APP) containing the Kunitz insert (APP K+) and other protease inhibitors. Conditioning of nerve segments with APP K+, aprotinin or leupeptin for 5 days or more resulted in mitosis of Schwann cells, demyelination of fibres, and a < 10-fold increase in Schwann cells, associated with demyelinated fibres. Altered fibres nevertheless involved a small part of the population. Nerve segments proximal and distal to the conditioned region showed almost no alteration. Conditioning with saline, heated APP K+, or APP without the Kunitz insert was not effective. We conclude that APP K+ and other protease inhibitors induce Schwann cells to enter the cell cycle, and once committed to proliferate they resorb their myelin. These functional properties of APP may be relevant to the pathogenesis of Alzheimer's disease.

Amyloid beta-Protein Precursor↗

PubMed1994

Monomeric amphiphilic forms of acetylcholinesterase appear early during brain development and may correspond to biosynthetic precursors of the amphiphilic G4 forms.

We have studied the development of mouse brain acetylcholinesterase (AChE). Only tetrameric (G4) and monomeric (G1) forms were detected both in vivo and in vitro. The amphiphilic G4 form increased continuously during development, whereas an amphiphilic G1 form appears transiently around embryonic day 17. A causal relationship between the monomers and tetramers was established using pulse-chase experiments with paraoxon, a reversible AChE inhibitor. We report here, for the first time, the presence of an amphiphilic monomer possibly involved in the assembly of the amphiphilic G4 AChE form during mouse brain development.

Acetylcholinesterase↗

PubMed1992

Axonal sprouting induced in the sciatic nerve by the amyloid precursor protein (APP) and other antiproteases.

Protease inhibition is the mechanism by which some trophic factors promote the extension of neurites. In the rat sciatic nerve, we assessed the ability to induce sprouts of the APP isoform that embodies the Kunitz antiprotease domain and other antiproteases. With the electron microscope, axonal sprouts were found when antiproteases were supplied but not after administration of inactive substances. We conclude that axons have a drive to sprout which can be released by the unbalance of an extracellular protease-antiprotease system. We propose that this system is involved in the pathogenesis of Alzheimer's disease.

Amyloid beta-Protein Precursor↗

PubMed1991

Effect of Test-yolk upon human sperm acrosome reaction.

Human spermatozoa stored in Test-yolk buffer show an increased rate of fusion with zona-free hamster oocytes as compared with freshly ejaculated spermatozoa. Therefore, in this work, we studied the kinetics of the acrosome reaction and fertilization using fresh and TEST-yolk stored human spermatozoa in order to determine whether the rate fertilization was related to the rate of acrosome reaction. The semen samples were divided in two aliquots, one was used fresh (control) and the other stored for 48 hours at 4 degrees C in TEST-yolk buffer (experimental). Spermatozoa of each aliquot were evaluated every two hours for: a) the incidence of acrosome reaction, as studied by scanning electron microscopy, and b) their ability to fuse with zona-free hamster oocytes. The results showed that--as a function of the incubation time--there was an increase in the percentage of acrosome reaction, both in controls (zero to 28.3%) and in the experimental ones (5 to 27.8). It was also found that there were no significant differences between the incidence of the acrosome reaction when using fresh or TEST-yolk treated spermatozoa. On the other hand the rate of fertilization was significantly (p < 0.05) higher when TEST-yolk stored (experimental) spermatozoa were used as compared with the use of fresh (control) spermatozoa. These results suggest that the increase in the rate of fertilization when using TEST-yolk stored spermatozoa is not associated with an increase in the rate of the acrosome reaction, but most probably to an improvement in the efficiency of the gamete membrane fusion.

Acrosome↗