Browsing by Author "Strachan A.F."
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- ItemAcute phase response in bronchiectasis and bronchus carcinoma(1984) Nel A.E.; Strachan A.F.; Welke H.E.; de Beer F.C.Measurement of the acute phase response in patients suffering from bronchiectasis, emphysema, bronchus carcinoma and various benign space occupying lesions was undertaken, using sensitive immunoradiometric assays for C-reactive protein and serum amyloid-A protein. In some patients with bronchiectasis, clinically judged to be in remission, the results show a major ongoing acute phase response. Such a response could predispose these patients to the development of reactive secondary amyloidosis. In bronchus carcinoma, the application of these measurements to judge the extent of tumour growth is limited as infection complicating obstruction is a more potent initiator of the acute phase response than the neoplastic pocess per se.
- ItemCerebrospinal fluid C-reactive protein in infective meningitis in childhood(1985) Donald P.R.; Strachan A.F.; Schoeman J.F.; De Beer F.C.The value of cerebrospinal fluid C-reactive protein (CSF CRP) determination as a diagnostic aid in infective meningitis has been investigated in four groups of children. In a "no meningitis" group of 10 children, a median CSF CRP value of 0.08 μg/ml was obtained (range 0 to 0.31 μg/ml); in a viral meningitis group of 21 children a median value of 0.01 μg/ml (range 0 to 3.06 μg/ml); in a bacterial meningitis group of 27 children a median value of 9.6 μg/ml (range 0 to 31.5 μg/ml); and in a tuberculous meningitis group of 18 children a median value of 0.29 μg/ml (range 0 to 4.9 μg/ml). CSF CRP values in the bacterial meningitis group differed significantly from those of each of the other groups (P < 0.01), but considerable overlap between the groups detracted from the diagnostic value of the test. In six patients with bacterial meningitis with ambiguous conventional CSF chemistry results, normal CSF CRP values were found. Simultaneous serum CRP was determined in nine patients with tuberculous meningitis and 11 with bacterial meningitis, and the CRP response in both the serum and CSF appears subdued in tuberculous meningitis in comparison with bacterial meningitis. CSF CRP and total protein values were determined intermittently during a 24-hour period in ventricular CSF from two children with tuberculous meningitis who underwent temporary direct ventricular drainage. A considerable and apparently parallel diurnal variation in both values was seen. CSF CRP values have limited application in the etiologic diagnosis of meningitis. © 1985.
- ItemCirculating acute phase reactive proteins as indicators of infection in poorly controlled diabetes mellitus(1988) Van Eeden S.F.; Strachan A.F.; Hough S.F.Serum levels of six acute phase proteins (APP) - C-reactive protein (CRP), serum amyloid A (SAA), α1-antitrypsin, haptoglobin and complement fractions C3 and C4 - were serially studied in 24 patients with poorly controlled diabetes mellitus, ten of whom had unequivocal evidence of an underlying infection. In diabetic patients without infection, no change in APP levels was noted suggesting that hyperglycaemia per se does not quantitatively influence the acute phase response. No correlation between the presence of infection, and fever, leukocytosis, a raised erythrocyte sedimentation rate, or serum levels of α1-antitrypsin, haptoglobin or complement was apparent in these patients. However, serum CRP and SAA were initially increased 10-100 times above normal in diabetic patients with an underlying infection (P < 0.01); during the following week circulating levels of CRP and SAA decreased steadily in response to the infection being brought under control. We conclude that serial measurement of CRP and/or SAA is a sensitive, albeit non-specific, parameter to detect and monitor the activity of infection in patients with diabetes.
- ItemHuman serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production(1989) Strachan A.F.; Shephard E.G.; Bellstedt D.U.; Coetzee G.A.; Van Der Westhuyzen D.R.; De Beer F.C.Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (>90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at >7 M-urea. By immunizing with apo-SAA adsorbed to acid treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.
- ItemIdentification of three isoform patterns of human serum amyloid A protein(1988) Strachan A.F.; De Beer F.C.; Van Der Westhuyzen D.R.; Coetzee G.A.Three patterns of human apo-SAA (serum amyloid A protein) isoforms have been identified by electrofocusing. In pattern 1, six major apo-SAA isoforms of pI 6.0, 6.4, 7.0, 7.4, 7.5 and 8.0 were found. In pattern 2, the apo-SAA isoforms of pI 7.4 and 8.0 were not detected, whereas in pattern 3 the pI-7.0 and -7.5 isoforms were lacking. Six patients displayed apo-SAA isoform pattern 1, 11 displayed pattern 2 and one displayed pattern 3.
- ItemPhosphorylation of human serum amyloid A protein by protein kinase C(1988) Nel A.E.; De Beer M.C.; Shephard E.G.; Strachan A.F.; Vandenplas M.L.; De Beer F.C.Monokine-induced hepatic secretion of serum amyloid A protein (apo-SAA), an acute-phase reactant, is followed by rapid association with high-density lipoprotein (HDL) in plasma. Plasma clearance of apo-SAA is more rapid than any of the other HDL apolipoproteins. It has been shown that, of the acute-phase HDL3 apolipoproteins, apo-SAA preferentially associated with neutrophil membranes. HDL apolipoproteins have been shown to activate protein kinase C in endothelial cells. We therefore investigated potential phosphorylation of HDL3 apolipoproteins by protein kinase C. Apo-SAA was the only apolipoprotein phosphorylated (K(m) = 12 mM). Phosphorylation of the apo-SAA-containing HDL3 particle was selective for the more basic isoforms of apo-SAA (pI 7.0, 7.4, 7.5 and 8.0), with more acidic isoforms being phosphorylated when delipidated acute-phase apolipoproteins were used as substrate. However, phosphorylation was not in itself responsible for the establishment of the apo-SAA isoforms.