Developmental changes of soluble and membrane-bound aspartate aminopeptidase activities in rat brain. 1996

G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
Departamento de Fisiología, Facultad de Medicina, Universidad del País Vasco, Leioa-Vizcaya, Spain.

Specific soluble and membrane-bound aspartyl-naphthylamide hydrolyzing activities were assayed in brain subcellular fractions from rat fetuses (19-20 days of gestation), and from 1-week-old and 1-, 5- and 24-month-old rats. Both enzymatic activities showed a heterogeneous distribution, with highest concentrations mainly in the microsomal fraction. Membrane-bound activity was in most cases higher than soluble activity. With the exception of soluble activity in the nuclear and microsomal fractions, significant age-related changes were observed in all fractions for both enzymatic activities. Soluble activity showed a homogeneous developmental profile in most of the fractions, with the lowest levels in 1-month-old rats and the highest in 1-week and 5-month-old animals. However, changes in the microsomal fraction did not follow the pattern displayed by the rest of the fractions. No clear developmental profile in specific membrane-bound activity was observed, each fraction exhibiting a different sequence of changes. Whereas in 24-month-old-rats there was a significant increase in activity in homogenate, nuclear and microsomal fractions, a significant decrease was observed in the synaptosomal fraction. These results may reflect the functional status of the endogenous substrates of the enzymes.

UI MeSH Term Description Entries
D008297 Male Males
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D001921 Brain The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM. Encephalon
D000375 Aging The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time. Senescence,Aging, Biological,Biological Aging
D000626 Aminopeptidases A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11. Aminopeptidase
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001224 Aspartic Acid One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter. (+-)-Aspartic Acid,(R,S)-Aspartic Acid,Ammonium Aspartate,Aspartate,Aspartate Magnesium Hydrochloride,Aspartic Acid, Ammonium Salt,Aspartic Acid, Calcium Salt,Aspartic Acid, Dipotassium Salt,Aspartic Acid, Disodium Salt,Aspartic Acid, Hydrobromide,Aspartic Acid, Hydrochloride,Aspartic Acid, Magnesium (1:1) Salt, Hydrochloride, Trihydrate,Aspartic Acid, Magnesium (2:1) Salt,Aspartic Acid, Magnesium-Potassium (2:1:2) Salt,Aspartic Acid, Monopotassium Salt,Aspartic Acid, Monosodium Salt,Aspartic Acid, Potassium Salt,Aspartic Acid, Sodium Salt,Calcium Aspartate,Dipotassium Aspartate,Disodium Aspartate,L-Aspartate,L-Aspartic Acid,Magnesiocard,Magnesium Aspartate,Mg-5-Longoral,Monopotassium Aspartate,Monosodium Aspartate,Potassium Aspartate,Sodium Aspartate,Aspartate, Ammonium,Aspartate, Calcium,Aspartate, Dipotassium,Aspartate, Disodium,Aspartate, Magnesium,Aspartate, Monopotassium,Aspartate, Monosodium,Aspartate, Potassium,Aspartate, Sodium,L Aspartate,L Aspartic Acid
D012995 Solubility The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Solubilities
D017207 Rats, Sprague-Dawley A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company. Holtzman Rat,Rats, Holtzman,Sprague-Dawley Rat,Rats, Sprague Dawley,Holtzman Rats,Rat, Holtzman,Rat, Sprague-Dawley,Sprague Dawley Rat,Sprague Dawley Rats,Sprague-Dawley Rats
D043384 Glutamyl Aminopeptidase A ZINC-dependent membrane-bound aminopeptidase that catalyzes the N-terminal peptide cleavage of GLUTAMATE (and to a lesser extent ASPARTATE). The enzyme appears to play a role in the catabolic pathway of the RENIN-ANGIOTENSIN SYSTEM. Aminopeptidase A,Angiotensinase A,Aspartate Aminopeptidase,Aspartyl Aminopeptidase,Aminopeptidase, Aspartate,Aminopeptidase, Aspartyl,Aminopeptidase, Glutamyl

Related Publications

G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
January 1993, Brain research bulletin,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
January 1996, Reproduction, fertility, and development,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
September 1975, Journal of bacteriology,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
August 1993, Brain research,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
January 1995, Journal fur Hirnforschung,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
January 1996, Life sciences,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
February 1985, Neuropeptides,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
November 1990, Neurochemical research,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
May 1999, Biochemistry and molecular biology international,
G Arechaga, and B Sánchez, and F Alba, and J D Luna, and I Prieto, and J M Martínez, and M Ramírez
January 1990, Cellular and molecular biology,
Copied contents to your clipboard!