K Andrikopoulos

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Dissecting aortic aneurysm is the hallmark of Marfan syndrome (MFS) and the result of mutations in fibrillin-1, the major constituent of elastin-associated extracellular microfibrils. It is yet to be established whether dysfunction of fibrillin-1 perturbs the ability of the elastic vessel wall to sustain hemodynamic stress by disrupting microfibrillar(More)
Aortic aneurysm and dissection account for about 2% of all deaths in industrialized countries; they are also components of several genetic diseases, including Marfan syndrome (MFS). The vascular phenotype of MFS results from mutations in fibrillin-1 (FBN1), the major constituent of extracellular microfibrils. Microfibrils, either associated with or devoid(More)
Development of the lymphoid system is dependent on the activity of zinc finger transcription factors encoded by the Ikaros gene. Differences between the phenotypes resulting from a dominant-negative and a null mutation in this gene suggest that Ikaros proteins act in concert with another factor with which they form heterodimers. Here we report the cloning(More)
The tissue-specific organization of collagen molecules into tridimensional macroaggregates determines the physiomechanical properties of most connective tissues, but the factors and mechanisms controlling this process are unknown. It has been postulated that quantitatively minor types V and XI collagen regulate the growth of type I and II collagen fibrils,(More)
Mice that are homozygous for the autosomal recessive chondrodysplasia (cho) mutation die at birth with abnormalities in cartilage of limbs, ribs, mandible, and trachea. Limb bones of newborn cho/cho mice are wider at the metaphyses than normal bones and only about half the normal length. By linkage analysis, the cho gene and the gene encoding the alpha 1(More)
Aiolos encodes a zinc finger DNA-binding protein that is highly expressed in mature B cells and is homologous to Ikaros. In the periphery of mice homozygous for an Aiolos-null mutation, B cells exhibit an activated cell surface phenotype and undergo augmented antigen receptor (BCR)-mediated in vitro proliferative responses, even at limiting amounts of(More)
Correct assembly of fibrillar collagen networks plays a critical role in animal morphogenesis. Very little is known about the contribution of the so-called minor fibrillar collagens (types V and XI) to fibrillogenesis. Here we examined the developmental expression of the mouse pro-alpha 2(V) collagen gene (col5a2) after the cloning and sequencing of cDNAs(More)
Several overlapping cDNA clones corresponding to the entire coding sequence of the mouse alpha 1(XI) collagen gene (Col11 a1) were isolated. The conceptual amino acid translation indicated a high degree of sequence identity (93%) with the human alpha 1(XI) chain. The cloning experiments also revealed alternative splicing of the sequence coding for 85(More)
We have isolated cDNA clones believed to encompass the full-length coding sequences for a subunit of bovine monoamine oxidase type A (MAO-A). The clones code for an apoprotein of 527 amino acid residues corresponding to a molecular mass of 59,806 Da. The inferred protein sequences show an overall similarity of 68% with partial amino acid sequences of bovine(More)
Type V collagen is a minor represented and poorly characterized fibrillar collagen type. Previous cDNA cloning experiments showed that the amino-propeptide of the pro-alpha 2(V) chain shares structural features in common with pro-alpha 1(I), pro alpha 1(II) and pro-alpha 1(III) collagens. In the present paper, this analysis was extended to the gene level.(More)