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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]
Il Tamburro Notturno
No full textIL TAMBURRO NOTTURNO
Il Tamburro Notturno ([1])
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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
Evaluation of prophylactic antibiotic treatment in dogs underwent tibial plateau levelling osteotomy
No full textBacterial 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
Application of the tibial tuberositity transposition tool (4T) for the treatment of grade 2 medial patellar luxation in dogs
No full textInvestigating by circular dichroism some amyloidogenic elastin-derived polypeptides
No full textTamburro and coworkers have demonstrated that some elastin-derived polypeptide sequences are able to give rise, in vitro, to amyloid-like fibers. The biological relevance of this finding could be explained by the recent detection of some amyloidogenic material found in arteries of old patients affected by atherosclerosis and demonstrated to be elastin derived. In this context, the comprehension of the mechanism responsible for the amyloid-like fibrillogenesis of elastin-derived sequences is of crucial importance for the design of drugs that could inhibit the amyloidogenic process. To gain further insights into the elastin amyloidogenic process, we studied the polypeptide sequences encoded by Exon 7 and Exon 32 of the human tropoelastin gene, and we demonstrated that only Exon 32 is able to aggregate in amyloid-like fibers. Vis-UV Thioflavin T circular dichroism (CD) spectroscopy rapidly and unambiguously detected the amyloidogenic propensity of the polypeptides. To gain additional insights into the aggregation mechanism of elastin-derived amyloidogenic peptides, we carried out the kinetics of EX32 amyloid-like aggregates by using ThT dye. CD spectroscopy was also used for investigating the secondary structure of the polypeptides, thus giving useful insights into the conformations involved in amyloid-like fiber formation. Furthermore, complementary techniques such as fluorescence spectroscopy, spectral shift, and binding Congo red UV assays as well as atomic force microscopy were also used to confirm the amyloidogenic behavior of the studied polypeptides
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