International journal of clinical & laboratory research最新文献

{"title":"Increased levels of lactoferrin in synovial fluid but not in serum from patients with rheumatoid arthritis.","authors":"D Caccavo,&nbsp;G D Sebastiani,&nbsp;C Di Monaco,&nbsp;F Guido,&nbsp;M Galeazzi,&nbsp;G M Ferri,&nbsp;L Bonomo,&nbsp;A Afeltra","doi":"10.1007/s005990050059","DOIUrl":"https://doi.org/10.1007/s005990050059","url":null,"abstract":"<p><p>Lactoferrin is a multifunctional immunoregulatory protein, stored in specific granules of neutrophil granulocytes, from which it is released following cell activation. As activated neutrophils play a crucial role in the destruction of synovial joints in rheumatoid arthritis, we evaluated lactoferrin concentration in synovial fluid and sera from 21 patients with rheumatoid arthritis and 11 patients with osteoarthritis. We also measured lactoferrin levels in sera from 12 healthy controls. Lactoferrin was measured by a solid-phase inhibition immunoassay. Median lactoferrin levels were significantly higher in synovial fluid from rheumatoid arthritis than from osteoarthritis patients (P = 0.0002). In contrast, no significant difference was found between serum lactoferrin from patients with rheumatoid arthritis or osteoarthritis compared with normal controls. In patients with rheumatoid arthritis, lactoferrin concentrations were higher in synovial fluid than in sera (P = 0.036). In both rheumatoid arthritis and osteoarthritis no correlation was found between serum and synovial fluid lactoferrin (P = 0.51 and P = 0.5, respectively). In synovial fluid from patients with rheumatoid arthritis, lactoferrin concentrations correlated with neutrophil granulocyte count (P < 0.0001), but neither serum nor synovial lactoferrin levels correlated with disease activity (P = 0.32 and P = 0.25, respectively). In conclusion, lactoferrin is a reliable marker of neutrophil activation at sites of inflammation in rheumatoid synovitis, but does not represent a marker of disease activity.</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 1","pages":"30-5"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050059","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21225097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Carnitine deficiency and hyperammonemia in children receiving valproic acid with and without other anticonvulsant drugs.","authors":"A Verrotti,&nbsp;R Greco,&nbsp;G Morgese,&nbsp;F Chiarelli","doi":"10.1007/s005990050060","DOIUrl":"https://doi.org/10.1007/s005990050060","url":null,"abstract":"<p><p>Plasma ammonia and total and free carnitine were measured in 84 children requiring anticonvulsant drugs: 32 patients (group A) on valproic acid alone, 28 children (group B) on polytherapy including valproic acid, and 24 patients (group C) on polytherapy without valproic acid. The other anticonvulsant drugs used in groups B and C were carbamazepine and phenobarbital. Plasma ammonia concentrations were elevated in both group A and B compared with controls. Group B patients showed significantly higher hyperammonemia than group A (59.9 +/- 16.3 micrograms/dl vs. 36.7 +/- 12.4 micrograms/dl; P < 0.05). Group C patients had plasma ammonia levels similar to those of controls (31.1 +/- 14.7 micrograms/dl vs. 29.7 +/- 12.1 micrograms/dl; NS). In both group A and group B patients, plasma ammonia levels were correlated with the valproic acid dosage (r = 0.32, P < 0.01) and with serum concentrations of valproic acid (r = 0.41, P < 0.001). Moreover, a significant correlation between plasma ammonia and duration of valproic acid therapy was found in the patients as a whole (r = 0.31, P < 0.01). Plasma total and free carnitine concentrations were significantly reduced in groups A and B (total carnitine 36.9 +/- 6.9 mumol/l vs. 32.9 +/- 9.7 mumol/l; free carnitine 28.9 +/- 5.1 mumol/l vs. 25.7 +/- 4.3 mumol/l, respectively) compared with group C patients who did not receive valproic acid and in whom values were similar to controls (total carnitine 46.1 +/- 9.0 mumol/l vs. 47.7 +/- 10.1 mumol/l; free carnitine 40.1 +/- 7.1 mumol/l vs. 42.9 +/- 8.0 mumol/l, respectively). Twenty-eight patients (18 of group A and 10 of group B) were re-evaluated and showed a complete normalization of plasma ammonia, and total and free carnitine levels which were similar to controls. Our data suggest that hyperammonemia is an important problem in patients receiving valproic acid, particularly in association with other anticonvulsant drugs. This increase of plasma ammonia and the concomitant reduction of carnitine seem to be transient and completely reversible.</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 1","pages":"36-40"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050060","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21225098","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Introduction of the human PLTP transgene suppresses the atherogenic diet-induced increase in plasma phospholipid transfer activity in C57BL/6 mice.","authors":"A Y Tu,&nbsp;B Paigen,&nbsp;G Wolfbauer,&nbsp;M C Cheung,&nbsp;H Kennedy,&nbsp;H Chen,&nbsp;J J Albers","doi":"10.1007/s005990050056","DOIUrl":"https://doi.org/10.1007/s005990050056","url":null,"abstract":"<p><p>The human plasma phospholipid transfer protein (PLTP) has been shown to facilitate the transfer of phospholipids between lipoproteins and convert high-density lipoproteins into larger and smaller particles in vitro. To explore the lipid transport function in vivo, transgenic C57BL/6 mice that express the human PLTP gene, driven by its natural promoter, were generated. Little difference in PLTP activity and lipoprotein lipids was observed between transgenic mice and non-transgenic control mice fed the chow diet. In response to an atherogenic high-fat, high-cholesterol, cholic acid containing diet, the PLTP activity increased significantly with time in control mice (62% in males and 34% in females after the high-fat diet for 18 weeks). In contrast, the PLTP activity did not change appreciably in the transgenic mice fed the atherogenic diet. Thus, the introduction of the human transgene suppressed the diet-induced increase in plasma PLTP activity, as evidenced by a decrease in PLTP mRNA in a variety of tissues. High-density lipoprotein levels decreased in mice fed the atherogenic diet, but there was a proportionally greater decrease in transgenic animals than in controls. After 18 weeks on the atherogenic diet, the transgenic animals had high-density lipoprotein-cholesterol and PLTP activity approximately one-half of that of control animals. Non-denaturing gradient gel electrophoresis of plasma indicated that the atherogenic diet decreased the high-density lipoprotein size distribution in control mice. However, high-density lipoprotein particle size distribution of the transgenic mice was shifted to smaller particles compared with control animals (P < 0.001). These findings suggest that PLTP activity can modulate the effects of an atherogenic diet on high-density lipoproteins.</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 1","pages":"14-21"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050056","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21225213","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The rate of plasmin formation after in vitro clotting is inversely related to lipoprotein(a) plasma levels.","authors":"R Testa,&nbsp;S M Marcovina","doi":"10.1007/s005990050077","DOIUrl":"https://doi.org/10.1007/s005990050077","url":null,"abstract":"<p><p>Lipoprotein(a) levels are largely genetically determined and are linked to increased risk of coronary artery disease. The hypothesis that elevated lipoprotein(a) levels lead to decreased fibrinolysis, due to the close structural homology with plasminogen, could in part explain the genesis of this risk, although contrasting results have been obtained in different studies. The aim of our study was to evaluate whether the rate of plasmin formation, enhanced in vitro by a fixed amount of human tissue plasminogen activator after clotting, was related to plasma lipoprotein(a) levels in 45 healthy subjects. Aliquots of human plasma were clotted with calcium chloride and thrombin followed by addition of tissue plasminogen activator. We then measured the time course of plasmin formation, determined as hydrolysis of H-D-valyl-L-leucyl-L-lysine-p-nitroanilide dihydrocortide (S-2251). The log of lipoprotein(a) level was negatively related to the rate of plasmin formation (r(s)=-0.46, P=0. 002), and multiple regression analysis indicated that this relationship was not influenced by the amount of plasminogen, fibrinogen, plasminogen activator inhibitor-1, tissue plasminogen activator, or by the size of apo(a) isoforms. These data support the concept that lipoprotein(a) can inhibit plasminogen activation and plasmin formation and can thereby play an important role in the genesis of atherosclerosis as an antifibrinolytic agent.</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 3","pages":"128-32"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050077","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21450502","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analysis of three genetic polymorphisms as risk factors for thrombosis.","authors":"P Giordano,&nbsp;M Micelli,&nbsp;B Coppola,&nbsp;P Trerotoli,&nbsp;D De Lucia,&nbsp;A Iolascon","doi":"10.1007/s005990050086","DOIUrl":"https://doi.org/10.1007/s005990050086","url":null,"abstract":"","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 4","pages":"174-5"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050086","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21633104","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Na(+)/Ca(2+) exchange inhibitors modulate thapsigargin-induced Ca(2+) and Na(+) influx in human lymphocytes.","authors":"J R Nofer,&nbsp;E Pulawski,&nbsp;R Junker,&nbsp;U Seedorf,&nbsp;G Assmann,&nbsp;W Zidek,&nbsp;M Tepel","doi":"10.1007/s005990050070","DOIUrl":"https://doi.org/10.1007/s005990050070","url":null,"abstract":"<p><p>Thapsigargin has been shown the elevate intracellular Na(+) concentration in human lymphocytes, but mechanisms underlying thapsigargin-induced Na(+) entry are little understood. In the present study we investigated thapsigargin-induced changes in cytosolic free Na(+) and Ca(2+) concentration in human lymphocytes after inhibition of the Na(+)/Ca(2+) exchange with two structurally unrelated compounds, dimethylthiourea ad bepridil. The intracellular Na(+) increase induced by 5 microM thapsigargin was significantly enhanced in the presence of 5 mM dimethylthiourea or 40 microM bepridil. In contrast, both compounds significantly decreased the thapsigargin-induced intracellular Ca(2+) elevation. No effect of dimethylthiourea or bepridil on thapsigargin-induced Ca(2+) influx was observed in the absence of extracellular Na(+). These observations are consistent with the hypothesis that thapsigargin stimulates Na(+)/Ca(2+ )exchange in human lymphocytes. However, Na(+)/Ca(2+) exchange does not mediate Na(+) influx in human lymphocytes.</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 2","pages":"89-92"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050070","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21301020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Activities of copper,zinc-superoxide dismutase in erythrocytes and ceruloplasmin in serum in chronic ischemia of lower limbs.","authors":"M Iskra,&nbsp;W Majewski","doi":"10.1007/s005990050065","DOIUrl":"https://doi.org/10.1007/s005990050065","url":null,"abstract":"<p><p>Cu,Zn-superoxide dismutase is an endogenous scavanger of superoxide radicals (O(2)(*-)) which also induce the synthesis of this enzyme. Ceruloplasmin is an antioxidant and acute-phase reactant. Changes in the synthesis of both enzymes are related to the metabolism of copper and zinc. Concentrations of copper and zinc were previously found to be increased in the serum and arterial wall of atherosclerotic subjects. The aim of this study was to investigate the Cu,Zn-superoxide dismutase activity in erythrocytes and ceruloplasmin activity in serum, and to measure serum concentrations of copper, zinc, and malonyldialdehyde in patients with moderate and critical chronic ischemia of the lower limbs. A group of 26 patients with chronic arterial occlusion of the lower limbs was divided into two groups depending on the degree of ischemia: moderate and critical. Cu,Zn-superoxide dismutase activity in erythrocytes was measured using the RANSOD kit, the serum ceruloplasmin oxidase activity was determined with o-dianisidine as a substrate. Copper and zinc concentrations in serum were determined by atomic absorption spectrometry. There was an increase in the ceruloplasmin activity and serum copper concentration in critical ischemia (194.4+/-51.94 U/l and 23.5+/-4.2 micromol/l, respectively) compared with moderate ischemia (139.1+/-34.9 U/l and 18.5+/-2.0 micromol/l, respectively). The Cu,Zn-superoxide dismutase activity in erythrocytes was higher in moderate ischemia (2,657+/-1,564 U/g hemoglobin) than in controls (1,205+/- 353 U/g hemoglobin), but not different from critical ischemia. There was a negative correlation for Cu,Zn-superoxide dismutase and ceruloplasmin (r=-0.60, P</=0.05) in critical ischemia.</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 2","pages":"64-7"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050065","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21301139","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biliary bile acid composition in gastric cancer.","authors":"M Fracchia,&nbsp;S Pellegrino,&nbsp;P Secreto,&nbsp;M Calgaro,&nbsp;S Taraglio,&nbsp;A Pera,&nbsp;G Galatola","doi":"10.1007/s005990050062","DOIUrl":"https://doi.org/10.1007/s005990050062","url":null,"abstract":"<p><p>Bile reflux into the stomach has been considered carcinogenic. Secondary bile acids, and in particular deoxycholic acid, have been shown to act experimentally as co-carcinogens in the colon and are increased in patients with colorectal adenocarcinoma. No information is available with respect to biliary bile acid composition in patients with gastric cancer. We studied biliary bile acid composition in 11 patients with gastric cancer and 23 healthy controls. Bile acids were measured using high-performance liquid chromatography. The site of gastric cancer was the antrum in 6 patients and body in 5. There were 6 intestinal-type and 5 diffuse adenocarcinomas. Only 2 patients had Helicobacter pylori infection. Deoxycholic acid constituted 24% +/- 2% of biliary bile acid in gastric cancer patients versus 22% +/- 2% in healthy controls (NS). Similarly, no differences were found between the two groups for all other bile acids. Deoxycholic acid constituted 23% +/- 3% of biliary bile acid (NS vs. controls) in patients with antral adenocarcinoma and 25% +/- 2% (NS vs. controls) in patients with intestinal-type gastric adenocarcinoma. Gastric adenocarcinoma is not associated with an increase in the more-toxic secondary bile acids, and deoxycholic acid in particular. This reduces the importance of bile acid composition as a promotor in gastric carcinogenesis.</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 1","pages":"46-8"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050062","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21225100","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Myoglobin, creatine kinase MB, troponin T, and troponin I - rapid bedside assays in patients with acute chest pain.","authors":"K Penttilä,&nbsp;H Koukkunen,&nbsp;A Kemppainen,&nbsp;M Halinen,&nbsp;T Rantanen,&nbsp;K Pyörälä,&nbsp;I Penttilä","doi":"10.1007/BF02874135","DOIUrl":"https://doi.org/10.1007/BF02874135","url":null,"abstract":"<p><p>Three new rapid, qualitative bedside immunoassays were evaluated in the diagnosis of patients with acute chest pain. The subjects, 122 patients in group 1 (bedside tests for myoglobin, creatine kinase MB) and 233 patients in group 2 (bedside tests for troponin I and sensitive troponin T) were admitted to hospital with acute chest pain for less than 12 h. The bedside tests were performed on admission, and 2, 4, and 6 h later. The correlation between the two parts of the rapid creatine kinase MB/myoglobin test during the first 12 h after the onset of chest pain was moderate in all patients (kappa=0.401, 95% confidence interval 0.321-0.483). The highest correlation was seen with the patients with definite and probable myocardial infarction. The correlations were smaller but significant also in other diagnostic groups (unstable angina pectoris, prolonged chest pain, and non-cardiac chest pain). The correlation between the rapid sensitive test for troponin T and rapid test for troponin I was significant in all groups (kappa=0.776, 95% confidence interval 0.711-0.841). The myoglobin part of the rapid creatine kinase MB/myoglobin test may be too non-specific for clinical diagnostic purposes [in non-infarct patients the myoglobin part was significantly more often positive than creatine kinase MB or troponin tests (P<0.001)].</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 2","pages":"93-101"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02874135","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21301022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The beneficial effect of 2'-deoxycoformycin in renal ischemia-reperfusion is mediated both by preservation of tissue ATP and inhibition of lipid peroxidation.","authors":"M V Bor,&nbsp;O Durmuş,&nbsp;A Bilgihan,&nbsp;C Cevik,&nbsp;N Türközkan","doi":"10.1007/s005990050067","DOIUrl":"https://doi.org/10.1007/s005990050067","url":null,"abstract":"<p><p>Renal ischemia injures the renal tubular cell by disrupting the vital cellular metabolic machinery. Further cell damage is caused when the blood flow is restored by oxygen free radicals that are generated from xanthine oxidase. Oxygen radicals cause lipid peroxidation of cell and organelle membranes, disrupting the structural integrity and capacity for cell transport and energy metabolism. In the present study, the possible therapeutic usefulness of the adenosine deaminase inhibitor, 2'-deoxycoformycin (DCF), during renal ischemia and reperfusion injury was investigated. The effects of DCF on renal malondialdehyde (MDA) and ATP levels were studied after 45 min ischemia and 15 min subsequent reperfusion in rat kidneys. MDA levels remained unchanged during ischemia, but increased after the subsequent reperfusion. DCF pretreatment (2.0 mg/kg i.m.) decreased MDA and increased ATP levels during the ischemia-reperfusion period. DCF exerts a dual protective action by facilitating purine salvage for ATP synthesis and inhibiting oxygen radical-induced lipid peroxidation. These results suggest that DCF therapy could be beneficial in the treatment of ischemia-reperfusion renal injuries.</p>","PeriodicalId":77180,"journal":{"name":"International journal of clinical & laboratory research","volume":"29 2","pages":"75-9"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s005990050067","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21301141","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}