1,016 research outputs found
Synthesis of and conformational studies on polypeptide sequences coded by human tropoelastin exons: the putative KP cross-link domains
No full textThe Mentor Marsh, 1901-1903: A Standoff! Peter M. Hitchcock vs. United States Steel
No full textSam Tamburro discusses Northeast Ohio as an area of interest to U.S. Steel during 20th century industrialization. The author focuses on industrialist Peter M. Hitchcock’s refusal to sell his land to U.S. steel, preserving the marsh wetlands of Mentor, Ohio in the process. Abstract; originally published in Western Reserve Studies Symposium (11th: 1996: Cleveland, Ohio)
The Dissection of Human Tropoelastin: Exon-By-Exon Chemical Synthesis and Related Conformational Studies
No full textPolypeptide sequences encoding the single exons of human tropoelastin were synthesized and
their conformations were studied in different solvents and at different temperatures by CD and 1 H NMR.
The results demonstrated the presence of labile conformations such as poly-proline II helix (PPII) and
â-turns whose stability is strongly dependent on the microenvironment. Stable, periodic structures, such
as R-helices, are only present in the poly-alanine cross-linking domains. These findings give a strong
experimental basis to the understanding of the molecular mechanism of elasticity of elastin. In particular,
they strongly support the description of the native relaxed state of the protein in terms of trans-
conformational equilibria between extended and folded structures as previously proposed [Debelle, L.,
and Tamburro, A. M. (1999) Int. J. Biochem. Cell. Biol. 31, 261-272]
Bacterial peptide methionine sulphoxide reductase: co-induction with glutathione S-transferase during chemical stress conditions.
No full textPeptide methionine sulphoxide reductase (MsrA; EC 1.8.4.6) is a ubiquitous enzyme catalysing the reduction of methionine sulphoxide to methionine in proteins, while the glutathione S- transferases (GSTs) are a major family of detoxification enzymes. A gene homologous to MsrA was identified in a chromosomal fragment from the bacterium Ochrobactrum anthropi, and this gene is located just downstream of a GST gene identified previously (OaGST) [Favaloro, Tamburro, Angelucci, De Luca, Melino, Di Ilio and Rotilio (1998) Biochem. J. 335, 573–579]. This raises the question of whether the products of these two genes may be involved in a common cellular protection function. To test this hypothesis, the hypothetical MsrA protein has been overexpressed in Escherichia coli as a functional 51 kDa GST fusion protein. Following cleavage with thrombin and purifi- cation, the soluble 24 kDa protein showed MsrA activity with N- acetylmethionine sulphoxide as substrate, as well as with other sulphoxide compounds. Therefore polyclonal antibodies were raised against the recombinant protein, and the modulation of MsrA in this bacterium, grown in the presence of different stimulants simulating several stress conditions, was investigated. The level of expression of MsrA was detected both by measuring the mRNA level and by immunoblotting experiments, in addition to measuring its catalytic activity. MsrA is a constitutive enzyme which is also inducible by chemical stress involving phenolic compounds such as phenol and 4-chlorophenol. Recently we reported that the GST of this bacterium, like MsrA, is only modulated by toxic chemical compounds [Favaloro, Tamburro, Trofino, Bologna, Rotilio and Heipieper (2000) Biochem. J. 346, 553–559] ; therefore this is the first indication of a co-induction of the MsrA and GST enzymes during chemical stress
Polipeptidi sintetici quali biomateriali in relazione a collagene ed elastina
No full textPolipeptidi sintetici quali biomateriali in relazione a collagene ed elastin
Localizing alpha-Helices in Human Tropoelastin: Assembly of the Elastin “Puzzle”
No full textPolyalanine cross-linking domains encoded by exons 6, 15, 17, 19, 21, 23, 25, 27, 29, 31 of
human tropoelastin were synthesized, and their conformations were studied in different solutions and at
different temperatures by CD and 1 H NMR. The results demonstrated the presence of poly-proline II
helix (PPII) in aqueous solvent and of R-helical conformation in TFE. The 1 H NMR results allowed the
precise localization of the helices along the peptide sequence. These data were further refined by prediction
algorithms in order to take into account the reduced helix stability at the end of the peptides. Furthermore,
the influence of flanking residues was checked by synthesizing and by determining the structure of a
peptide spanning exon 31 coded domain and the first five residues of the following exon 32 coded domain.
These studies, together with those previously published [Tamburro, A. M., Bochicchio, B., and Pepe, A.
(2003) Biochemistry 42, 13147-62], are used to propose a coherent recomposition of the elastin pieces
(domains) in order to give an acceptable solution to the elastin structure-function problem
The elastase-catalyzed hydrolysis of elastin, a-elastins and synthetic oligoalanines
No full textThe elastase-catalyzed hydrolysis of elastin, a-elastins and synthetic oligoalanine
Involvement of elastin in atherogenesis. A possible role of lipids and aging
No full textInvolvement of elastin in atherogenesis. A possible role of lipids and agin
- …
