RESUMEN
A 22,500-Da antigen apparently specific to Mycobacterium avium, Mycobacterium intracellulare, and Mycobacterium scrofulaceum has been identified by Western immunoblotting. By use of a dot immunoassay, this antigen was found in the urine of 64% of patients with AIDS and disseminated M. avium disease. It was not found in the urine of healthy control subjects. Detection of antigenuria might provide the basis for rapid diagnosis of M. avium disease in patients with AIDS.
Asunto(s)
Síndrome de Inmunodeficiencia Adquirida/complicaciones , Antígenos Bacterianos/orina , Infecciones por Mycobacterium/inmunología , Mycobacterium avium/inmunología , Síndrome de Inmunodeficiencia Adquirida/inmunología , Síndrome de Inmunodeficiencia Adquirida/orina , Animales , Anticuerpos Antibacterianos/biosíntesis , Anticuerpos Antibacterianos/inmunología , Antígenos Bacterianos/inmunología , Western Blotting , Cabras , Humanos , Mycobacterium/inmunología , Infecciones por Mycobacterium/complicacionesRESUMEN
The 39-43 residue polypeptide (amyloid beta protein, beta A4) deposited as amyloid in Alzheimer's disease (AD) is derived from a set of 695-770 residue precursors referred to as the amyloid beta A4 protein precursor (beta APP). In each of the 695, 751, and 770 residue precursors, the 43 residue beta A4 is an internal peptide that begins 99 residues from the COOH-terminus of the beta APP. Each holoform is normally cleaved within the beta A4 to produce a large secreted derivative as well as a small membrane associated fragment. Neither of these derivatives can produce amyloid because neither contains the entire beta A4 peptide. In this study, we employ cells stably transfected with full length beta APP695, beta APP751, or beta APP770 expression constructs to show that phorbol ester activation of protein kinase C substantially increases the production of secreted forms from each isoform. By increasing processing of beta APP in the secretory pathway, PKC phosphorylation may help to prevent amyloid deposition.