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Your search keyword '"Mateos-Cáceres, Petra J."' showing total 2 results
Start Over Author "Mateos-Cáceres, Petra J." Publisher american chemical society
2 results on '"Mateos-Cáceres, Petra J."'

1. Relationship between vitamin D binding protein and aspirin resistance in coronary ischemic patients: a proteomic study.

Author

López-Farré AJ, Mateos-Cáceres PJ, Sacristán D, Azcona L, Bernardo E, de Prada TP, Alonso-Orgaz S, Fernández-Arquero M, Fernández-Ortiz A, and Macaya C

Subjects
Aged, Aspirin pharmacology, Blood Proteins analysis, Blood Proteins metabolism, Blood Proteins pharmacology, Coronary Disease drug therapy, Coronary Disease metabolism, Electrophoresis, Gel, Two-Dimensional, Female, Humans, Male, Middle Aged, Platelet Aggregation drug effects, Platelet Aggregation Inhibitors pharmacology, Protein Isoforms blood, Proteome metabolism, Proteomics, Thromboxane A2 antagonists & inhibitors, Thromboxane A2 metabolism, Vitamin D-Binding Protein metabolism, Vitamin D-Binding Protein pharmacology, Aspirin therapeutic use, Coronary Disease blood, Drug Resistance, Proteome analysis, Vitamin D-Binding Protein blood
Abstract

Our aim was to analyze the plasma proteome in aspirin (acetylsalicylic acid [ASA])-sensitive and ASA-resistant coronary ischemic patients. Plasma from 19 ASA-sensitive and 19 ASA-resistant patients was analyzed. For the proteomic study, two-dimensional electrophoresis was performed. The expression of one isotype of the fibrinogen gamma chain and three isotypes of haptoglobin was increased in ASA-resistant patients. Three vitamin D binding protein isotypes were increased in ASA-resistant patients. In vitro incubation of vitamin D binding protein (DBP) with blood from healthy volunteers reduced the inhibitory effect of ASA on thromboxane A2 production. DBP may be a new regulator of the inhibitory effect of ASA on platelets.

Published
2007
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2. Proteomic study of plasma from moderate hypercholesterolemic patients.

Author

Alonso-Orgaz S, Moreno L, Macaya C, Rico L, Mateos-Cáceres PJ, Sacristán D, Pérez-Vizcaíno F, Segura A, Tamargo J, and López-Farré A

Subjects
Amino Acid Sequence, Apolipoproteins blood, Blood Proteins genetics, Electrophoresis, Gel, Two-Dimensional, Fibrinogen analysis, Humans, Hypercholesterolemia drug therapy, Mass Spectrometry, Molecular Sequence Data, Simvastatin pharmacology, Simvastatin therapeutic use, Blood Proteins analysis, Gene Expression Regulation drug effects, Hypercholesterolemia blood, Proteomics methods
Abstract

Proteomics is a technology to detect and identify several proteins and their isoforms in a single sample. We used proteomics to analyze modifications in the protein map of plasma after simvastatin treatment of moderate hypercholesterolemic patients. Plasma from hypercholesterolemic patients (n = 9) was compared before and after 12 weeks of simvastatin treatment (40 mg/day). Patients with similar cardiovascular risk factors were used as controls (CR group). By using two-dimensional electrophoresis and mass spectrometry, we identified the different protein isoforms. The plasma expression of three fibrinogen gamma chain isoforms (FGG) was enhanced, whereas the expression of two isoforms of the fibrinogen beta chain (FGB) was reduced in the hypercholesterolemic patients compared with the CR group. The expression of apolipoprotein A-IV and three haptoglobin isoforms was higher in hypercholesterolemic patients. Simvastatin treatment modified the plasma expression of FGG chain isoform 1, FGB chain isoforms 1 and 2, vitamin D binding protein isoform 3, apo A-IV, and haptoglobin isoform 2. The modification of FGG chain isoform 1 and FGB chain isoforms 1 and 2 was positively correlated with total plasma cholesterol level. Proteomic analysis of plasma may help to know more in depth the molecular mechanism modified by simvastatin treatment.

Published
2006
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