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A third major locus for autosomal dominant hypercholesterolemia maps to 1p34.1-p32.
- M. Varret, J. Rabès, +18 authors C. Boileau
- Biology, MedicineAmerican journal of human genetics
- 1 May 1999
The results show that ADH is genetically more heterogeneous than conventionally accepted, and contains four candidate genes at 1p34.1-p32, outside the critical region, showing no identity with FH3.
Paraoxonase PON1 polymorphism leu-Met54 is associated with carotid atherosclerosis: results of the Austrian Stroke Prevention Study.
The data suggest that the paraoxonase LL genotype may represent a genetic risk factor for carotid atherosclerosis.
Apolipoprotein E4allele in the normal elderly: neuropsychologic and brain MRI correlates
It is concluded that the apolipoprotein E e4 allele is associated with subtle learning and memory deficits in normal elderly persons and may therefore be suggested a marker for accelerated cognitive aging.
Undifferentiated human mesenchymal stem cells (hMSCs) are highly sensitive to mechanical strain: transcriptionally controlled early osteo-chondrogenic response in vitro.
- G. Friedl, H. Schmidt, I. Rehák, G. Kostner, K. Schauenstein, R. Windhager
- Chemistry, MedicineOsteoarthritis and cartilage
- 1 November 2007
Undifferentiated hMSCs are highly sensitive to mechanical strain with a transcriptionally controlled osteo-chondrogenic differentiation response in vitro, and follow a coordinated expression pattern.
Studies on the role of specific cell surface receptors in the removal of lipoprotein (a) in man.
- F. Krempler, G. Kostner, A. Roscher, F. Haslauer, K. Bolzano, F. Sandhofer
- Chemistry, MedicineThe Journal of clinical investigation
- 1 May 1983
The binding of 125I-lipoprotein (a) [Lp(a)] to cell surface receptors was studied on cultured human fibroblasts and turnover studies are consistent with the assumption that L p(a) is removed from the plasma by similar mechanisms as LDL.
Human plasma phospholipid transfer protein accelerates exchange/transfer of alpha-tocopherol between lipoproteins and cells.
- G. Kostner, K. Oettl, M. Jauhiainen, C. Ehnholm, H. Esterbauer, H. Dieplinger
- Chemistry, MedicineThe Biochemical journal
- 15 January 1995
It is concluded that human PLTP catalyses exchange/transfer processes of alpha-T between lipid compartments, which may be of relevance in atherogenesis and tumour initiation and growth.
Influence of n-3 fatty acids on the growth of human breast cancer cellsin vitro: Relationship to peroxides and Vitamin-E
- V. Chajès, W. Sattler, Alfred Stranzl, G. Kostner
- Biology, MedicineBreast Cancer Research and Treatment
- 1 June 1995
PUFA's significantly interfere with cell proliferation of breast cancer cells in vitro due to the formation of oxidation products, indicating that there must be other factors involved in the differential metabolism of PUFA's in tumor cells.
Lipoprotein(a) in health and disease.
- F. Kronenberg, A. Steinmetz, G. Kostner, H. Dieplinger
- Biology, MedicineCritical reviews in clinical laboratory sciences
Large studies and those including apo(a) phenotype analysis came to the conclusion that Lp( a) levels are not or only moderately elevated in insulin-dependent patients, and in noninsulin-dependent diabetics, Lp (a) is not elevated.
Turnover of lipoprotein (a) in man.
- F. Krempler, G. Kostner, K. Bolzano, F. Sandhofer
- Medicine, ChemistryThe Journal of clinical investigation
- 1 June 1980
The results of this study indicate that Lp(a) is not converted to other serum lipoproteins, and from the correlations between serum concentration and kinetic parameters of L p(a), it is concluded that an elevated Lp (a) level is the consequence of an increased Lp-a) apoprotein synthesis.
Enhanced Association of Platelet-activating Factor Acetylhydrolase with Lipoprotein (a) in Comparison with Low Density Lipoprotein (*)
- C. Blencowe, A. Hermetter, G. Kostner, H. Deigner
- Chemistry, MedicineThe Journal of Biological Chemistry
- 29 December 1995
The results suggest that PAF acetylhydrolase exhibits an enhanced association with Lp (a) due to an increased affinity to Lp(a) apolipoprotein B.