| 1. |
- Näsström, Birgit, et al.
(author)
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Lower plasma levels of lipoprotein lipase after infusion of low molecular weight heparin than after administration of conventional heparin indicate more rapid catabolism of the enzyme
- 2003
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In: Journal of Laboratory and Clinical Medicine. - 0022-2143 .- 1532-6543. ; 142:2, s. 90-99
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Journal article (peer-reviewed)abstract
- The functional pool of lipoprotein lipase (LPL) is anchored to heparan sulfate at the vascular endothelium. Injection of heparin releases the enzyme into the circulating blood. Animal experiments have shown that the enzyme is then extracted and degraded by the liver. Low molecular weight (LMW) heparin preparations are widely used in the clinic and are supposed to release less LPL. In this study, we infused a LMW heparin into healthy volunteers for 8 hours. The peak of LPL activity was only about 30% and the subsequent plateau of LPL activity only about 40% compared with those seen with conventional heparin. When a bolus of heparin was given after 4 hours' infusion of LMW or conventional heparin, only relatively small, and similar, amounts of LPL entered plasma. This suggests that the difference between LMW and conventional heparin lay in the ability to retain LPL in the circulating blood, not in the ability to release the lipase. Triglycerides (TGs) decreased when the heparin infusion was started, as expected from the high circulating LPL activities. After 1 to 2 hours, TG levels increased again, and after 8 hours they were about twice as high as before the heparin infusion. This indicates that the amount of LPL available for lipoprotein metabolism had become critically low in relation to TG transport rates. This study indicates that LMW heparin compared with conventional heparin causes as much or more depletion of LPL and subsequent impairment of TG clearing.
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| 2. |
- Solomon, A, et al.
(author)
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Calcifying epithelial odontogenic (Pindborg) tumor-associated amyloid consists of a novel human protein
- 2003
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In: Journal of Laboratory and Clinical Medicine. - 0022-2143 .- 1532-6543. ; 142:5, s. 348-355
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Journal article (peer-reviewed)abstract
- Calcifying epithelial odontogenic tumors (CEOTs), also known as Pindborg tumors, are characterized by the presence of squamous-cell proliferation, calcification, and, notably, amyloid deposits. On the basis of immunohistochemical analyses, the amyloidogenic component had heretofore been deemed to consist of cytokeratin-related or other molecules, however, its chemical composition had never been elucidated. We have used our microanalytic techniques to characterize the protein nature of CEOT-associated amyloid isolated from specimens obtained from 3 patients. As evidenced by the results of amino-acid sequencing and mass spectrometry, the fibrils were found to be composed of a polypeptide of approximately 46 mer. This component was identical in sequence to the N-terminal portion of a hypothetical 153-residue protein encoded by the FLJ20513 gene cloned from the human KATO III cell line. That the amyloid protein was derived from this larger molecule was demonstrated by reverse transcription-polymerase chain reaction amplification of tumor-cell RNA where a full-length FLJ20513 transcript was found. Furthermore, immunohistochemical analyses revealed that the amyloid within the CEOTs immunostained with antibodies prepared against a synthetic FLJ20513-related dodecapeptide. Out studies provide unequivocal evidence that CEOT-associated amyloid consists of a unique and previously undescribed protein that we provisionally designate APin.
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| 3. |
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| 4. |
- Larsson, Jörgen, et al.
(author)
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Distribution of iodine 125-labeled alpha1-microglobulin in rats after intravenous injection
- 2001
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In: Journal of Laboratory and Clinical Medicine. - : Elsevier BV. - 0022-2143 .- 1532-6543. ; 137:3, s. 165-175
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Journal article (peer-reviewed)abstract
- The 28-kd plasma protein alpha(1)-microglobulin is found in the blood of mammals and fish in a free, monomeric form and as high-molecular-weight complexes with molecular masses above 200 kd. In this study, iodine 125-labeled free and high-molecular weight rat alpha(1)-microglobulin (a mixture of alpha(1)-microglobulin/alpha(1)-inhibitor-3 and alpha(1)-microglobulin/fibronectin complexes) were injected intravenously into rats. The distribution of the proteins was measured by using scintillation camera imaging. Both forms of (125)I-labeled alpha(1)-microglobulin were rapidly cleared from the blood, with a half-life of 2 and 16 minutes for the initial and late phase, respectively, for free alpha(1)-microglobulin; and a half-life of 3 and 130 minutes for the initial and late phase, respectively, for the complexes. After 45 minutes, 6%, 16%, 27%, 13%, and 34% of the free (125)I-labeled alpha(1)-microglobulin and 18%, 21%, 6%, 10%, and 42% of the (125)I-labeled alpha(1)-microglobulin complexes were found in the blood, gastrointestinal tract, kidneys, liver, and the remainder of the body, respectively. The local distribution of injected (125)I-labeled alpha(1)-microglobulin in intestines and kidneys was investigated by microscopy and autoradiography. In the intestine, both forms were distributed in the basal layers, villi, and luminal contents. The results also suggested intracellular labeling of epithelial cells. Well-defined local regions containing higher concentrations of injected protein could be seen in the intestine. In the kidneys, both forms were found mostly in the cortex. Free (125)I-labeled alpha(1)-microglobulin was found predominantly in epithelial cells of a subset of the tubules, whereas the (125)I-labeled complexes were more evenly distributed. Intracellular labeling was indicated for both alpha(1)-microglobulin forms. The results thus indicate a rapid transport of (125)I-labeled alpha(1)-microglobulin from the blood to most tissues.
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| 5. |
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| 6. |
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| 7. |
- Näsström, Birgit, et al.
(author)
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Lipoprotein lipase during continuous heparin infusion : Tissue stores become partially depleted
- 2001
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In: Journal of Laboratory and Clinical Medicine. - : Elsevier BV. - 0022-2143 .- 1532-6543. ; 138:3, s. 206-213
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Journal article (peer-reviewed)abstract
- Lipoprotein lipase (LPL) and hepatic lipase (HL) are located at vascular surfaces in extrahepatic tissues and in the liver, respectively. Heparin displaces the enzymes into the circulating blood. Animal studies have shown that the liver takes up and degrades LPL. To explore whether heparin leads to a depletion of tissue stores, we followed the lipase activities in plasma during an 8-hour primed infusion of heparin in 10 healthy subjects. After an initial peak, the HL activity decreased slowly after a time curve similar to that for activated partial thromboplastin time. The time curve for LPL was different. After the initial peak, the activity dropped by almost 80%, from 30 to 120 minutes, and then leveled off to a plateau that corresponded to about 15% of the peak level. A second bolus of heparin was given to 4 subjects after 4 hours. The plasma LPL activity increased, but only to about 35% of the original peak level. We conclude that when heparin releases LPL into plasma, the lipase becomes liable to be taken up and degraded by the liver. After less than 1 hour, the stores of LPL have been exhausted, and recruitment of lipase into plasma depends on a slow but stable delivery of newly synthesized molecules.
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| 8. |
- Lindberg, B, et al.
(author)
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High prevalence of thyroid autoantibodies at diagnosis of insulin-dependent diabetes mellitus in Swedish children
- 1997
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In: Journal of Laboratory and Clinical Medicine. - 0022-2143. ; 130:6, s. 585-589
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Journal article (peer-reviewed)abstract
- The prevalence of thyroglobulin autoantibodies and that of thyroid peroxidase autoantibodies were studied in serum samples from 52 children with insulin-dependent diabetes mellitus, sampled at diagnosis and before the start of insulin treatment, with 386 non-diabetic schoolchildren (11 to 13 years of age) serving as control subjects. Using exactly the same sensitive solid-phase immunosorbent radioassay for both thyroid autoantibodies, with comparable sensitivity, we found the prevalences of both autoantibodies to be higher in the insulin-dependent diabetes mellitus group than in the control group, the difference being most pronounced for thyroid peroxidase autoantibodies. Thyroglobulin autoantibodies were positive in 33% of the diabetics versus 14% in the control group (p = 0.002), and thyroid peroxidase autoantibodies were positive in 38% versus 6% (p = 0.0001). The high prevalence of thyroid autoantibodies already at diagnosis stresses the importance of early screening for thyroid disease in patients with insulin-dependent diabetes mellitus.
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