Connective tissue amine oxidase II. Purification and partial characterization of lysyl oxidase from chick aorta

Harris, Edward D.; Gonnerman, Wayne A.; Savage, J. E.; O’Dell, Boyd L.

doi:10.1016/0005-2744(74)90226-5

Cited by 135 publications

(35 citation statements)

References 27 publications

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“…Accordingly, this suggests that abnormality of elastin evolves a loss of arterial elasticity and an increase in fragility, which may induce circulatory disorder. An abnormality of the elastin architecture may be caused by the impaired activity of a Cu-containing enzyme (lysyl oxidase) involved in the formation of peptide cross-linking in the process of elastin synthesis [3,5,6,9,22,23]. As observed by scanning electron microscopy, thinning and irregular arrangement of the arterial elastic fibers of the deer affected with CEA were similar to those observed in the 6-month-old healthy deer, and it strongly suggests that the arterial elastic fibers of the CEA deer were immature [10].…”

mentioning

confidence: 99%

Ultrastructure of Aortic Elastic Fibers in Copper-Deficient Sika Deer(Cervus nippon Temminck).

Yoshikawa

Wang²,

Seo

et al. 2001

The Journal of Veterinary Medical Science

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ABSTRACT. Light microscopic and transmission and scanning electron microscopic observations were performed on the aortas of two 4-and 6-year-old deer affected with cervine ataxia and two 6-month-and 4-year-old healthy deer. Examination of the aortas from affected deer by transmission electron microscopy revealed the absence of distinct elastic laminae in the internal elastic lamina and tunica media, but discontinuous and irregular clumps of elastin were present. Scanning electron microscopy disclosed immature architecture of elastic fibers in the aortas from the copper-deficient deer, and the architecture was similar to that of a 6-month-old healthy deer.

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mentioning

confidence: 99%

Ultrastructure of Aortic Elastic Fibers in Copper-Deficient Sika Deer(Cervus nippon Temminck).

Yoshikawa

Wang²,

Seo

et al. 2001

The Journal of Veterinary Medical Science

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“…Reagent salts and buffers, made to concentration, were treated with dithizone (0.005% weight/volume in CC14, 3 Assay of Lysyl Oxidase Activity. The procedure of Pinnell and Martin (13) was followed with some modifications as noted previously (15). Aortic proteins labeled with [4,5-3H]lysine (New England Nuclear, specific activity 35 Ci/ mmol) were the source of the substrate.…”

Section: Methodsmentioning

confidence: 99%

“…Lysyl oxidase is present in aortic tissue of several animal species, appearing predominantly in association with fibrous components of the tissue (14). Because of its insolubility in salt solutions, high concentrations of urea have been used to extract the enzyme from aortic tissue (15,14). The enzyme has been purified to near homogeneity (15-17), and copper has been found to be present in the protein structure and essential for catalytic function (15).…”

mentioning

confidence: 99%

“…Because of its insolubility in salt solutions, high concentrations of urea have been used to extract the enzyme from aortic tissue (15,14). The enzyme has been purified to near homogeneity (15)(16)(17), and copper has been found to be present in the protein structure and essential for catalytic function (15). However, it now appears that copper is also a key regulator of the steady-state levels of lysyl oxidase in aorta.…”

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confidence: 99%

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Copper-induced activation of aortic lysyl oxidase in vivo.

Harris¹

1976

Proc. Natl. Acad. Sci. U.S.A.

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Raising day-old chicks on diets lacking copper severely depressed the activity of lysyl oxidase, a copper metalloenzyme in connective tissue. Administration of CuS04 either through the diet or through intraperitoneal injections restored the lysyl oxidase activity in aortic tissue. Two hours after the chicks received CuS04 (1 mg/kg) the activity of lysyl oxidase rose rapidly to attain, within 4-6 hr, a new steady-state level which was five to 20 times higher than the basal (saline-injected) activity. Twenty hours after copper administration, activity was still higher, in some experiments double that achieved at 6 hr. Very low amounts of cycloheximide injected intraperitoneally 45 min before and 3 hr after copper suppressed the activation response by two-thirds. Cycloheximide given 2 or 4 hr after the copper was only onehalf as effective. Actinomycin D caused only a 10-15% inhibition of the copper-induced activation. The data suggest that copper is a key regulator of lysyl oxidase activity in aorta and may in fact be a major determinant of the steadystate levels of the enzyme in that tissue.The biochemical basis for the essentiality of most trace metals lies in their unique ability to bind and form specific complexes with enzymes. Metal ions perform not only catalytic roles but serve to give shape and stability to the protein structure (1, 2). The consequences of protein-metal interactions are realized in enhanced catalytic prowess of enzymes and, perhaps, increased stability of the protein moiety to metabolic turnover (3).Although specific examples of metal ions controlling turnover rates of enzymes are unknown, numerous reports suggest that certain metal cations can influence the steadystate concentrations of metal transport and storage proteins. For example, iron induces the synthesis of apoferritin (4, 5) and reportedly stabilizes this protein against metabolic degradation (6). Both a zinc (7) and a cadmium (8) binding protein in rat liver cytosol appear to fluctuate at levels corresponding to the tissue levels of zinc and cadmium, respectively. Treatment of intact rats with cycloheximide and/or actinomycin D inhibits the apparent induction of these binding proteins by their respective metal ions. Ceruloplasmin, the major copper-binding protein in serum, undergoes rapid metabolic turnover in response to nutritional copper deficiency (9). Moreover, the metal-free as opposed to the metal-bound form of the protein is rapidly taken up and degraded by the liver (10). Thus the control of metalloprotein levels may be a general property of trace metals in biological systems.Copper deficiency in growing animals grossly impairs the integrity and functioning of connective tissue, most notably the collagen and elastin network in aorta. The cause of the impairment resides in a failure to synthesize the crosslinking compounds that stabilize. the peptide chains of collagen and elastin (11,12). Copper is a cofactor for lysyl oxidase, the enzyme that catalyzes the oxidation of select peptidyl lysine (or hydroxylysine) ...

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“…In vascular tissues, synthesis of elastin and collagen was suppressed (Waisman and Carnes, 1967;Coulson and Carnes, 1962;Starcher et al, 1964;Hill et al, 1967) as a result of an inhibition of lysyl oxidase activity (Chou et al, 1968;Harris et al, 1974Harris et al, , 1977 leading to the rupture of the heart and large arteries in copper-deficient animals. Lysyl oxidase, an amine oxidase, is copper dependent and is thought to be a key enzyme in elastin and collagen cross-linking.…”

Section: Membrane and Contractile Properties Of Rat Vascular Tissue Imentioning

confidence: 99%

Membrane and contractile properties of rat vascular tissue in copper-deficient conditions.

Kitano¹

1980

Circulation Research

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Connective tissue amine oxidase II. Purification and partial characterization of lysyl oxidase from chick aorta

Cited by 135 publications

References 27 publications

Ultrastructure of Aortic Elastic Fibers in Copper-Deficient Sika Deer(Cervus nippon Temminck).

Ultrastructure of Aortic Elastic Fibers in Copper-Deficient Sika Deer(Cervus nippon Temminck).

Copper-induced activation of aortic lysyl oxidase in vivo.

Membrane and contractile properties of rat vascular tissue in copper-deficient conditions.

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