Disease relevance of Apcs

• Animals receiving antimannoprotein (anti-MP) and anti-aspartyl proteinase (Sap) Ab-containing vaginal fluids from rats clearing a primary C. albicans infection showed a highly significant level of protection against vaginitis compared to animals given Ab-free vaginal fluid from noninfected rats [1].
• Among the putative virulence factors of Candida albicans, secreted aspartic proteinases (Sap, encoded by a family of at least nine genes) continue to attract the attention of many investigators studying the pathogenesis of candidiasis [2].
• With these characteristics, rat serum amyloid P-component could prove to be an important model in the study of the relations between amyloid P-component and amyloidosis [3].

Psychiatry related information on Apcs

• Serum amyloid P component, a member of pentraxin serum protein family, has been suggested to contribute to the progression of neurodegeneration including Alzheimer's disease by binding to beta-amyloid fibrils leading to an increased stability of the deposits against proteolytic degradation and by inducing neuronal apoptosis [4].

High impact information on Apcs

• Analysis of the deduced amino acid sequence indicates homology to members of the pentraxin family of secreted lectins that include C-reactive protein and serum amyloid P component [5].
• Postinfectious administration of pepstatin A, a potent Sap inhibitor, greatly accelerated the clearance of C. albicans from rat vagina [1].
• Rat serum amyloid P component. Analysis of cDNA sequence and gene expression [6].
• cDNA clones for rat serum amyloid P component (SAP) were isolated, and the derived amino acid sequence for pre-SAP was determined from the complete nucleotide sequence [6].
• While the efficacy of the inhibition on the serum amyloid P component-induced cell death increases with the uronic acid content, the inhibitory activity on the serum amyloid P component-beta-amyloid interaction decreases with the increasing uronic acid content of the glycosaminoglycans [4].

Chemical compound and disease context of Apcs

• A degree of protection against vaginitis was also conferred by postinfectious administration of anti-Sap and anti-MP monoclonal antibodies (provided the latter were directed against mannan rather than protein epitopes of MP) and by intravaginal immunization with a highly purified, polysaccharide-free Sap preparation [1].

Biological context of Apcs

• The inhibitory effect of glycosaminoglycans on the interaction between the first component of the complement cascade (C1q) and beta-amyloid shows a similar structure-activity relationship as on the serum amyloid P component-beta-amyloid interaction [4].
• This suggests that glycosaminoglycans interfere with the binding site on beta-amyloid for serum amyloid P component and C1q [4].

Anatomical context of Apcs

• Serum amyloid P component-induced cell death in primary cultures of rat cerebral cortex [7].
• Induction of C-reactive protein, serum amyloid P component, and kininogens in the submandibular and lacrimal glands of rats with experimentally induced inflammation [8].
• The exact mechanisms of each Sap involvement in any particular Candida disease, with special regard to human infections, and how the immune system deals with Sap, are critical issues for future research [2].

Associations of Apcs with chemical compounds

• The functional consequence of this binding has been demonstrated by heparin which promotes the proteolysis of beta-amyloid in vitro in the presence of serum amyloid P component [4].
• Here, we show that glycosaminoglycans inhibit both the serum amyloid P component-beta-amyloid interaction and the neurotoxic effect of serum amyloid P component [4].
• Previously we have reported serum amyloid P component (SAP) induced cell death in cerebro-cortical cultures of rat brain [9].
• In contrast, high intensity stimulation induced less c-Fos-immunopositive neurons in the VcI/II and Vo of rats treated with SP-Sap compared with those in Sal- or Bl-Sap-treated controls [10].
• We have called this protein rat serum amyloid P-component since it has all the properties typical of human serum amyloid P-component: it is made up to 10 subunits, it contains sialic acid and hexoses, it forms macroscopic polymers and its does not precipitate with pneumococcal C-polysaccharide [3].

Analytical, diagnostic and therapeutic context of Apcs

• C-reactive protein (RP) and serum amyloid P component (SAP) have been identified for the first time in rat serum and isolated by calcium-dependent affinity chromatography [11].

References