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1.
Article in English | MEDLINE | ID: mdl-1603822

ABSTRACT

In 19 patients with a malignant breast tumor, tumor tissue and blood were taken to determine the eicosanoid profile and platelet aggregation. Values were compared with those of patients with benign tumors (n = 4), or undergoing a mammary reduction (n = 7). Postoperatively, blood was taken as well in order to compare pre- and postoperative values. Eicosanoids were measured in peripheral blood monocytes and mammary tissue by means of HPLC; furthermore, TXA2, 6-keto-PGF1 alpha, and PGE2 were determined by RIA. Differences in pre- and postoperative values of cancer patients were seen in plasma RIA values: PGE2 and 6-k-PGF1 alpha were significantly higher preoperatively when compared with postoperatively, however, such differences were seen in the control groups as well. Compared to benign tumor or mammary reduction test material the eicosanoid profile of tissue obtained from malignant mammary tumors showed important differences. Except for PGF2 alpha, HHT and 15-HETE no detectable quantities of eicosanoids were found in the non-tumor material, whereas in the malignant tumor material substantial quantities of a number of eicosanoid metabolites were present. Statistically significant correlations could be established between patient/histopathology data and the results of the platelet aggregation assays, e.g. between menopausal status and ADP aggregation; oestrogen receptor (+/-) and collagen and arachidonic acid aggregation, inflammatory cell infiltration score and arachidonic acid aggregation and fibrosis score and ADP aggregation. The results show that eicosanoid synthesis in material from mammary cancer patients is different from that in benign mammary tissue. The implications, in particular, in relation to future prognosis of the patient, remain obscure.


Subject(s)
Breast Neoplasms/metabolism , Eicosanoids/metabolism , Breast Neoplasms/blood , Breast Neoplasms/surgery , Eicosanoids/blood , Female , Humans , In Vitro Techniques , Mastectomy , Menopause , Middle Aged , Monocytes/metabolism , Platelet Aggregation/drug effects , Receptors, Estrogen/metabolism
2.
Tijdschr Kindergeneeskd ; 57(4): 136-8, 1989 Aug.
Article in Dutch | MEDLINE | ID: mdl-2508264

ABSTRACT

We describe three children with an active rhesus antagonism. However, laboratory results and course were different than usual. The first child had blood-type O positive, while his mother had blood-type O positive as well. The mother of the second child had blood-type A negative, while the child seemed to be A negative too. The third child needed an exchange transfusion due to a 'regular' rhesus antagonism, but died shortly after. The mother of the first child turned out to have a rhesus D VI variant. The second child had a 'blocked' D-antigen due to excess anti-D antibodies. The illness of the third child looked like Graft versus Host disease clinically, but eventually appeared to have congenital myelofibrosis. A correct diagnosis in these children is of great importance in future pregnancies, blood transfusions and genetic counseling.


Subject(s)
Erythroblastosis, Fetal/immunology , Rh Isoimmunization/immunology , Antibody-Dependent Cell Cytotoxicity , Erythroblastosis, Fetal/complications , Humans , Infant, Newborn , Isoantibodies/analysis , Isoantibodies/genetics , Male , Pedigree , Primary Myelofibrosis/complications
3.
Intensive Care Med ; 14(5): 554-7, 1988.
Article in English | MEDLINE | ID: mdl-3256305

ABSTRACT

Albumin is a much abused and expensive drug in intensive care units. One of the motivations for its use is the prevention of pulmonary edema by enhancing the colloid osmotic pressure (COP). Fear of pulmonary edema has led to the formation of a magic (arbitrary) albumin value varying from one intensive care unit to another. Many intensive care units start substituting albumin when it is below 25 g/l. The objective of this paper is to look at the rationale of this policy. Our results show that in intensive care patients, with a variety of primary diagnoses, a poor correlation exists between COP and serum albumin concentration (r = 0.56; p less than 0.001). To get an index of the colloid osmotic status of the I. C.-patient measuring albumin concentration is useless and COP should be measured instead. From 19 patients with a COP in the 15.0-20.0 mmHg range (corresponding albumin range: 12.0-25.0 g/l) and from 10 patients with a COP in the 11.6-15.0 mmHg range (corresponding albumin range 10.5-19.2 g/l) none developed pulmonary edema. It is questionable if expensive, scarce albumin is the drug of choice with which to increase COP, for the mean increase (+/- SD) in COP after infusion of 100 grams albumin is 2.2 (+/- 1.5) mmHg (p less than 0.001). Adopting a COP action level of 15 mmHg can lead to considerable savings.


Subject(s)
Albumins/therapeutic use , Pulmonary Edema/physiopathology , Critical Care , Drug Utilization , Humans , Osmotic Pressure , Pulmonary Edema/prevention & control , Serum Albumin/analysis
4.
J Clin Chem Clin Biochem ; 19(5): 301-4, 1981 May.
Article in English | MEDLINE | ID: mdl-7264572

ABSTRACT

The quantitative determination of proteins in biological fluids, using Coomassie Brilliant Blue G-250, was evaluated. Compared with the biuret method, the Coomassie Blue G-250 method needs a much shorter time for analysis and has a greater sensitivity. The sensitivity of the dye for albumin is significantly greater than for globulins. The standard curves for the biuret method are more linear than those for the Coomassie Brilliant Blue G-250 method. The Coomassie Brilliant Blue G-250 method produces a precipitate, which sticks to the walls of the cuvet and results in an intolerable carry-over. Therefore, the use of the Coomassie Brilliant Blue G-250 method for the quantitative determination of proteins in urine and serum is not recommended.


Subject(s)
Proteins/analysis , Rosaniline Dyes , Chemical Phenomena , Chemistry , Globulins/analysis , Methods , Serum Albumin/analysis
5.
Clin Chim Acta ; 75(3): 377-85, 1977 Mar 15.
Article in English | MEDLINE | ID: mdl-852129

ABSTRACT

The generally accepted dimeric structure of creatine kinase (CK) is one in which M subunits and B subunits can occur. This paper reports the existence of three MM-bands and two MB-bands in human sera with increased CK-activity. These findings and supplementary data gathered from hybridisation experiments have led to the conclusion that there are two different M subunits, which can both occur in the enzyme in vivo. Further, findings are reported on the different CK-isozyme patterns of extracts from the cerebellum and from the cortex and the medulla of the cerebrum.


Subject(s)
Creatine Kinase , Brain/enzymology , Creatine Kinase/blood , Creatine Kinase/metabolism , Electrophoresis, Agar Gel , Humans , Isoenzymes/blood , Isoenzymes/metabolism , Macromolecular Substances , Organ Specificity , Protein Binding
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