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1.
Neuroreport ; 7(2): 457-62, 1996 Jan 31.
Article in English | MEDLINE | ID: mdl-8730805

ABSTRACT

Altered dopamine (DA) transporter densities have been implicated in mechanisms of vulnerability and relapse in human alcoholics. The regional distribution and density of the DA transporter was studied in alcohol-preferring vervet monkeys to investigate baseline status and regulation of the DA transporter at different stages of chronic alcohol drinking. Combined ligand binding and in vitro autoradiography of the cocaine congener [125I]RTI-55 (beta-CIT) demonstrated a significant increase in DA transporter densities in abstinent alcohol-preferring monkeys over those in alcohol-avoiding monkeys. Chronic alcohol consumption down-regulated DA transporter densities, and this effect was reversed by acute withdrawal. These results demonstrate that the DA transporter is regulated by alcohol exposure and suggest that increased DA transporter densities may be a phenotypic marker of alcohol preference in vulnerable monkeys.


Subject(s)
Alcohol Drinking/metabolism , Brain Chemistry/physiology , Carrier Proteins/metabolism , Membrane Glycoproteins , Membrane Transport Proteins , Nerve Tissue Proteins , Alcohol Drinking/psychology , Animals , Autoradiography , Central Nervous System Depressants/adverse effects , Central Nervous System Depressants/pharmacology , Chlorocebus aethiops , Cocaine/analogs & derivatives , Dopamine Plasma Membrane Transport Proteins , Ethanol/adverse effects , Ethanol/pharmacology , Ligands , Phenotype , Substance Withdrawal Syndrome/metabolism
2.
Lab Anim Sci ; 34(5): 494-6, 1984 Oct.
Article in English | MEDLINE | ID: mdl-6513513

ABSTRACT

Secondary amyloidosis was diagnosed in five Rhesus monkeys with chronic indwelling venous catheters. Diagnostic enzymology demonstrated normal serum alanine aminotransferase concentration and consistently elevated serum alkaline phosphatase. Serum protein electrophoresis on all five animals showed a typical pattern of decreased albumin and increased gamma globulin. Necropsy or biopsy specimens verified the presence of amyloid deposits in all animals. The diagnostic usefulness of clinical enzymology, serum protein electrophoresis and liver biopsy were demonstrated and the importance of considering amyloidosis as a differential diagnosis in monkeys with indwelling vascular catheters is emphasized.


Subject(s)
Amyloidosis/veterinary , Catheters, Indwelling/veterinary , Macaca mulatta , Macaca , Monkey Diseases/etiology , Alanine Transaminase/blood , Alkaline Phosphatase/blood , Amyloidosis/diagnosis , Amyloidosis/etiology , Animals , Animals, Laboratory , Biopsy/veterinary , Blood Proteins/analysis , Catheters, Indwelling/adverse effects , Female , Hepatomegaly/veterinary , Male , Monkey Diseases/diagnosis , Spleen/pathology
3.
Lab Invest ; 45(1): 7-13, 1981 Jul.
Article in English | MEDLINE | ID: mdl-7253566

ABSTRACT

Tissue deposits of amyloid protein AA and a concomitant elevation of serum protein SAA have been demonstrated previously in mice and humans with secondary amyloidosis, but not in rhesus monkeys (Macaca mulatta). In this study, protein SAA was quantitated in normal and amyloidotic rhesus monkeys using an enzyme-linked immunosorbent assay. Protein AA was isolated from the liver of a rhesus monkey with secondary amyloidosis by a combination of water extraction and gel filtration chromatography. The purified material had rigid, nonbranching fibrillar structures typical of amyloid on electron microscopy and a molecular weight of 9000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The amino acid content and partial sequence were comparable to those reported previously for protein AA of rhesus monkeys. As measured by enzyme-linked immunosorbent assay, normal rhesus monkeys had SAA levels of 40 to 64 ng. of AA equivalents per ml., whereas amyloidotic rhesus monkeys had SAA levels of 1700 to 95,000 ng. of AA equivalents per ml. An elevation of protein SAA was also detected in an amyloidotic pigtailed macaque (Macaca nemestrina) using rabbit antirhesus protein AA. Rabbit antisera against human and mouse protein AA reacted strongly with rhesus protein AA and with amyloidotic rhesus serum, but only slightly with normal rhesus serum, indicating that rhesus proteins AA and SAA have antigenic determinants cross-reactive with protein AA of xenotypic species.


Subject(s)
Amyloid/analysis , Amyloidosis/immunology , Serum Amyloid A Protein/analysis , Amino Acid Sequence , Animals , Enzyme-Linked Immunosorbent Assay , Goats , Liver/pathology , Liver/ultrastructure , Macaca mulatta , Mice , Rabbits
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