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At least 703 records · Page 39Linked to original sources
PubMed1976

A convenient method for the identification and estimation of soluble elastin synthesis in vitro.

A method is described by which newly synthesized soluble elastin can be routinely and conveniently identified and estimated in vitro without the need for unlabelled carrier tropoelastin. Aortic tissue from 11 day old chick embryos is incubated in the presence of [14C] L-proline and [3H] L-valine and the distributions of [14C] proline-, [14C] hydroxyproline-and [3H] valine-labelled proteins on SDS-polyacrylamide gels are determined. Soluble elastin is identified as a [14C] hydroxyproline-labelled peak of molecular weight approximately 70,000 daltons which also incorporates large quantities of [3H] valine and has a [14C] hydroxyproline/[14C] proline ratio of about 0.2. Whereas the hydroxyproline label can be used to estimate newly synthesized soluble elastin even after several hours of incubation, similar use of the [3H] valine label is limited to short incubation times. Paradoxically, the quantity of [14C] hydroxyproline-labelled soluble elastin detected by the assay decreases with increased incubation time. This fall-off in labelled soluble elastin is not due to an increase in the rate of crosslinking of the protein over the course of the incubation. Soluble elastin is detectable both in tissue extract and medium fractions. The presence of hydroxyproline-labelled protein fragments in the medium fraction is evidence of proteolytic breakdown of collagen or elastin or both proteins. This proteolytic activity is augmented by the inclusion of serum in the incubation medium and is not inhibited by phenylmethylsulfonylfluoride. The method provides a convenient assay by which factors affecting the synthesis and secretion of soluble elastin may be studied.

Aminopropionitrile↗
PubMed1982

Lathyrism: aortic and cutaneous collagen in the rat.

In the rat the administration of lathyrogenic toxic agents at low doses over prolonged periods of time caused simultaneous alterations in aortic and cutaneous tissues. BAPN caused an increase in soluble collagen in the skin, but in aorta there was no increase in neutral salt soluble collagen, but an increase in the amount that could be solubilized with pepsin. Type III collagen was found to represent 7% in the control aorta samples and this level was not affected by BAPN. In skin Type III accounts for 11% of the extractable collagen in controls and 14% in lathyritic animals. Biochemical changes observed in this study show evidence for collagenous lesions by increases in solubility in both skin and aorta but in neither tissue was the percentage of Type III altered by lathyrism.

Aminopropionitrile↗
PubMed1991

Induction of lung lysyl oxidase activity and lysyl oxidase protein by exposure of rats to cadmium chloride: properties of the induced enzyme.

Inspiration of CdCl2 results in a focally fibrotic response in rat lungs and markedly increases the activity of lung lysyl oxidase. Western blot analyses of urea-extractable rat lung proteins revealed that the levels of an immunoreactive, 32,000-Da protein were markedly increased in the cadmium-exposed rat lung tissue, consistent with the induction of lysyl oxidase protein. Anion exchange chromatography revealed low levels of multiple peaks of catalytically functional lysyl oxidase in control rat lung extracts, while the profile of cadmium-exposed rat lung extracts displayed markedly elevated levels of multiple peaks of enzyme activity indicating that the charge heterogeneity is expressed in the activated enzyme. The cadmium-induced enzyme was purified as a species of 32 kDa, without resolving individual ionic variants. The catalytic and physical properties of the isolated enzyme were very similar to those of previously well characterized basal enzyme of bovine aorta, including the presence of a pyrroloquinoline quinone-like carbonyl cofactor. The copper and cadmium content of the cadmium-induced enzyme indicated little if any replacement of tightly-bound copper by cadmium in the exposed lung.

Aminopropionitrile↗
PubMed1976

[Incorporation of 32P-orthophosphate in aortic phospholipids in chronic lathyrims in the rat].

Study of 32P orthophosphate incorporation into rat aortic phospholipids after B.A.P.N. treatment, which was followed or not by a lipid-supplemented diet (4.5 p. 100 cholesterol and 37 p. 100 butter). The 32P orthophosphate turnover in the total phospholipid was twice as slow among B.A.P.N.-treated rat than among control-rat. Such a decrease of the 32P orthophosphate turnover could be found as well in phosphatidylethanolamines, phosphatidylcholines and lysophosphatidylcholines. Sphingomyelins showed a very weak metabolic activity among two groups of rats. 32P orthophosphate incorporation into inositolphosphatides was slowed down by B.A.P.N. treatment. Maximal specific activity of inositolphosphatides after injection of 32P orthophosphate was reached within 4 hours in control rats, and 8 hours in B.A.P.N.-treated rats. Three months after the end of B.A.P.N. treatment, no difference in specific activity could be found between control-rats and B.A.P.N.-treated rats. Lipid supplemented diet modified the metabolic activity of phospholipids equally in control rats and B.A.P.N.-treated rats. Specific activity decrease in total phospholipids, phosphatidylcholines, phosphatidylethanolamines, and increase in lysophosphatidylcholines were noted in both groups of animals under a high rat diet. These modifications of the metabolic activity of different phospholipids were most marked fourteen hours after 32P orthophosphate injection. B.A.P.N. treatment only slowed the incorporation of 32P phosphate into phospholipids. Administration of a single lipid supplemented diet or a diet associated with B.A.P.N. treatment induced a slower turnover of phosphatidylcholines and phosphatidylethanolamines, and a faster turnover of lysophosphatidylcholines.

Aminopropionitrile↗