Biomedical subjects

R Tenni

Publications and source records attributed to R Tenni.

42 records · Page 3Linked to original sources

PubMedDate not supplied

Localization of a structural defect in type I procollagen in a patient affected with the severe non-lethal form of Osteogenesis imperfecta.

A case of severe non-lethal Osteogenesis imperfecta was studied. The patient's cultured skin fibroblasts synthesised a mixed population of type I collagen chains some of which showed abnormal behaviour on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Further analysis revealed that two types of alpha 1(I) chains were synthesised, both an abnormal, slower migrating and a normal species. A small defect in one allele of one of the type I procollagen chains could lead to the larger size of the abnormal chains, probably caused by overmodifications of the triple helical region. CNBr peptide mapping allowed us to localise the defect midway along the triple helix: the defect site could be assigned to the region between the alpha 1(I)CB-3 and CB-7 peptides. The abnormal alpha 1(I) chains synthesised by the patient's cells had a melting temperature which was about 2 degrees C lower than normal chains. The results appear to be in agreement with the defect localisation and the phenotype.

Amino Acids↗

PubMedDate not supplied

A simple method for quantitative estimation of collagen type III to type I ratio in soft tissues.

In the present paper a relatively rapid and simple method for estimating the ratio of collagen type III to type I in soft tissues is proposed. The ratio Gly/Ala is determined in pure collagen samples obtained from pepsin digests of the tissues. Since this ratio varies linearly depending on the composition of the mixtures of the two collagen types, it is shown that the percentage content of the two collagen types is easily calculated.

Adult↗

PubMedDate not supplied

Influence of flavonoid-copper complexes on cross linking in elastin.

A protective and curative effect of some flavonoids on collagen maturation in lathyrism has been previously demonstrated. This action appeared to involve cross linking of collagen. This paper deals with the effect in vitro of flavonoids and flavonoid-copper complexes on the oxidative deamination of lysine epsilon-amino groups in [4,5-3H]-lysine-labelled elastin. Flavonoids alone do not affect the reaction but it is evident that some flavonoid copper complexes are strongly effective: the aldehyde groups that are quickly formed then enable cross linking to occur. The lysine epsilon-amino groups of elastin are specifically concerned: in fact no effect was observed on free [4,5-3H]-lysine or on [4,5-3H]-lysine-labelled proteins obtained from mouse liver. The lysyl oxidase seems to interfere with the flavonoid-copper complees to regulate the oxidative deamination of lysine epsilon-amino groups.

Animals↗

PubMedDate not supplied

Hypothesis on the role of hydroxylysyl glycosides in collagen fibre organization.

Hydroxylysine (Hyl) glycosides were determined both on the collagen produced by in-vitro cultures of human skin fibroblasts and pig articular chondrocytes and on the insoluble collagen extracted from bovine cornea and sclera. The disorganized collagen present in the culture medium showed a Hyl di- to mono-glycoside ratio markedly higher than the molecules extracted from the cell layer, where electron microscopy investigations demonstrated the real presence of collagen fibres. Moreover in bovine cornea the insoluble collagen showed a ratio Hyl di- to mono-glycoside significantly higher than in sclera, which, on the contrary, possesses fibres with larger mean diameter. The possible conversion of Hyl diglycoside to monoglycoside was suggested by the demonstration of an alpha (1----2) glucosidase activity on Hyl diglycoside , in an enzyme extract from cultured human skin fibroblasts. A role for the processes of collagen glycosylation and deglycosylation was thus considered.

Animals↗

PubMedDate not supplied

Hydroxylysine glycosides: preparation and analysis by reverse phase high performance liquid chromatography.

Hydroxylysine diglycoside was prepared from hydrolyzed sponge by a combination of ion-exchange chromatography and gel filtration. The product obtained was chemically pure on amino acid analyzer and was active as substrate of the enzyme alpha-(1----2)glucosidase. Hyl monoglycoside was prepared by mild acid hydrolysis from diglycoside. A reverse phase HPLC system was devised for Hyl glycosides, hydroxylysine and other basic amino acids. The separation was achieved using an octadecyl bonded silica column on the compounds derivatized with dabsyl chloride to produce di-dabsyl derivatives. Elution was followed in the visible region at 436 nm. In the conditions used no or very low amount of mono-dabsyl derivatives was observed. Hyl di- and monoglycoside resulted a mixture of two diastereoisomers, which form during the alkaline hydrolysis. The separation of the diastereoisomers of each compound depended on pH and ionic strength of the eluent in the HPLC column, whereas they were not separated by our short column on amino acid analyzer. The HPLC system was also used for the analysis of Hyl glycosides on two collagen preparations.

Animals↗

PubMedDate not supplied

Glycosaminoglycan alterations in osteogenesis imperfecta.

Urinary GAGs from patients affected with Osteogenesis Imperfecta (O.I.) type I, type II and type III - according to Sillence et al. (1979) - have been investigated. Galactosamine to glucosamine ratio resulted significantly decreased in O.I. type II and III, whereas smaller differences in the mildest type of the disease were observed. Cellulose polyacetate electrophoresis of urinary GAGs purified from some patients showed the presence of a slowly moving polysaccharide substance, which did not appear in normal subjects. Moreover some pathological fractions, mainly constituted of ChS on the basis of chemical analysis and electrophoretic behaviour, were not digested by testicular hyaluronidase and presented anomalous structures as compared with the corresponding normal ones. These results seem to indicate that in some forms of O.I. the metabolic defect(s) not only affects the synthesis or the catabolism of a particular type of collagen, but also involves the proteoglycan component of the connective tissue.

Adolescent↗