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Results for “AMINOPROPIONITRILE”

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At least 667 records · Page 37Linked to original sources
PubMed1987

A biophysical and histological analysis of factors that lead to aortic rupture in normal and lathyritic turkeys.

These experiments were designed to determine if local differences in elastic properties or wall structure contributed to the development of aortic rupture in turkeys. Static elastic properties were measured from pressure-volume curves of cylindrical segments of upper and lower thoracic aorta and innominate artery in two groups of lathyritic birds and two age-matched control groups. The biggest changes were in the young lathyritic group that was on 0.04% beta-aminoproprionitrile at 3 weeks of age and continued for 2, 3, or 4 weeks. Much smaller changes were seen in the older group that started on 0.05% beta-aminoproprionitrile at 6 weeks of age for 10 days and then 0.02% beta-aminoproprionitrile for the next 9-12 weeks. The biggest changes were seen in the abdominal aorta, which ruptured spontaneously in 50% of the young lathyritic group. The birds had a marked decrease in the number of elastin layers per unit wall thickness. Analysis of the elastic diagrams showed that the elastance of both elastin and collagen were altered in the young lathyritic group. Rupture appeared to follow partial dissection of plaques, but true longitudinal dissection did not occur.

Aminopropionitrile↗
PubMed2006

The lysyl oxidase LOX is absent in basal and squamous cell carcinomas and its knockdown induces an invading phenotype in a skin equivalent model.

Lysyl oxidase initiates the enzymatic stage of collagen and elastin cross-linking. Among five isoforms comprising the lysyl oxidase family, LOX is the better studied. LOX is associated to an antitumor activity in ras-transformed fibroblasts, and its expression is down-regulated in many carcinomas. The aim of this work was to shed light on LOX functions within the epidermis by studying its expression in human basal and squamous cell carcinomas and analyzing the effect of its enzymatic activity inhibition and protein absence on human keratinocytes behavior in a skin equivalent. In both carcinomas, LOX expression by epidermal tumor cells was lacking, while it was up-regulated around invading tumor cells in association with the stromal reaction. Lysyl oxidase activity inhibition using beta-aminoproprionitrile in a skin equivalent model prepared with both primary human keratinocytes and HaCaT cell line affected keratin 10 and filaggrin expression and disorganized the collagen network and the basement membrane. In spite of all these changes, no invasion phenotype was observed. Modelization of the invasive phenotype was only noticed in the skin equivalent developed with LOX antisense HaCaT cell line, where the protein LOX is specifically absent. Our results clearly indicate that lysyl oxidase enzymatic activity is essential not only for the integrity maintenance of the dermis but also for the homeostasis of the epidermis. Moreover, LOX protein plays a role in the skin carcinomas and invasion but not through its enzymatic activity.

Aminopropionitrile↗
PubMed1983

Autoradiographic and liquid scintillation assessment of beta-amino-propionitrile-induced inhibition of collagen maturation using 3H-proline and 3H-lysine.

BAPN (0.1 mg/day) was injected into chick embryos for 4 days starting on the 7th day of incubation. On the 11th day, the embryos were administered either 3H-proline or 3H-lysine. 36 h later, the incorporation of each isotope by the periosteal osteogenic cells as well as into bone matrix was investigated by autoradiography. The incorporation of the two isotopes into whole bones was assessed by liquid scintillation counting. 3H-proline incorporation into the cellular or matrical compartments was unaffected by treatment. As compared to the controls, 3H-lysine label in BAPN-treated embryonic bones was significantly higher in the cellular compartment but was reduced over the bone matrix. The data provide the first direct morphological evidence that BAPN probably induces certain changes in the maturation of collagen involving lysyl residues which result in an inhibition of cross-linkage formation in collagen.

Aminopropionitrile↗
PubMed1969

Lathyrism.

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Acidosis↗