The Electrophoretic α;1-Globulin Pattern of Serum in α;1-Antitrypsin Deficiency

Laurell, C.‐B.; Eriksson, Sten

doi:10.3109/00365516309051324

Cited by 611 publications

(299 citation statements)

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“…19 So far, emphasis has been placed on alpha-1 proteinase inhibitor (alpha1Pi) in this context since plasma deficiency of this elastase inhibitor has been identified in association with the development of emphysema in patients homozygous for the alpha-1Pi gene mutation (ZZ). 20 Clinical trials are currently underway using an alpha-1 Pi gene transfer approach in ZZ and cystic fibrosis patients. 21 Although this strategy is entirely logical in correcting hereditary lack of alpha-1Pi, there is much controversy regarding the role of alpha-1Pi in the development of emphysema in smokers with apparently normal genes for alpha-1Pi.…”

Section: Discussionmentioning

confidence: 99%

Adenovirus-mediated expression of an elastase-specific inhibitor (elafin): a comparison of different promoters

et al. 1998

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This report describes the design and construction of three between MCMV and MLP was HCMV which was able to recombinant adenoviruses of serotype 5 (Ad5) expressing induce significant amounts of elafin, particularly in human elafin (EL), also called elastase-specific inhibitor. Three A549 cells. When compared in vivo in rat lungs, results promoters were chosen to drive the synthesis of elafin: the were similar; MCMV was the only promoter which induced small (380 bp) human cytomegalovirus promoter (HCMV), significant amounts of elafin as assessed by Northern blot the Ad2 major late promoter (MLP) and the mouse cytoanalysis and ELISA, even with a low dose of virus megalovirus (MCMV) promoter. Human alveolar epithelial (3 x 10 8 p.f.u.). Our data indicate that the MCMV promoter cells (A549), as well as rat and human primary pulmonary is the promoter of choice for the strong induction of fibroblasts were infected with Ad5-HCMV-EL, Ad5-MLPadenovirus-mediated transgenes in the lung, and suggest EL, Ad5-MCMV-EL and with the control Ad5-dl70/3. The its suitability both in rodent experimental models and in MCMV promoter was the most efficient promoter in all cells humans for investigative and therapeutic purposes. studied. MLP was the least efficient promoter. Intermediate

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Section: Discussionmentioning

confidence: 99%

Adenovirus-mediated expression of an elastase-specific inhibitor (elafin): a comparison of different promoters

et al. 1998

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“…For example, Clinh deficiency is associated with hereditary angioneurotic edema (30), a1-anti-trypsin deficiency with pulmonary emphysema and hepatic disease (31), and antithrombin III deficiency with thrombosis (32). Thus, the physiologic role of each inhibitor appears to be quite specific, whereas each inhibitor demonstrates a broad in vitro specificity.…”

Section: Methodsmentioning

confidence: 99%

Inhibitory spectrum of alpha 2-plasmin inhibitor.

Saito¹,

Goldsmith²,

Moroi³

et al. 1979

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

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ABSTRACTarPlasmin inhibitor (a2PI) has been recently characterized as a fast-reacting inhibitor of plasmin in human plasma and appears to play an important role in the regulation of fibrinolysis in vivo. We have studied the effect of purified a2PI upon various proteases participating in human blood coagulation and kinin generation. At physiological concentration (50 ;sg/ml), a2PI inhibited the clot-promoting and prekallikrein-activating activity of Hageman factor fragments, the amidolytic, kininogenase, and clot-promoting activities of plasma kallikrein, and the clot-promoting properties of activated plasma thromboplastin antecedent (PTA, Factor XIa) and thrombin. a2PI had minimal inhibitory effect on surface-bound activated PTA and activated Stuart factor (Factor Xa). a2PI did not inhibit the activity of activated Christmas factor (Factor IXa) or urinary kallikrein. Heparin (1.5-2.0 units/ml) did not enhance the inhibitory function of a2PI. These results suggest that, like other plasma protease inhibitors, a2PI possesses a broad in vitro spectrum of inhibitory properties.a2-Plasmin inhibitor (a2PI) has been recently identified as a fast-reacting inhibitor of plasmin in human plasma (1-3). a2PI has strong inhibitory activity against plasmin and is the first inhibitor that reacts with plasmin, whether plasminogen activation occurs in vitro or in vivo (4-6).Although the action of a2PI on plasmin is well characterized, relatively little information is available about the effect of this newly isolated inhibitor upon other plasma proteases (7,8). This paper reports the effect of physiologic concentrations of a2PI upon various proteases participating in blood coagulation and kinin generation and defines the in vitro spectrum of this inhibitor. We also compare the action of a2PI with that of some other plasma protease inhibitors in these systems. MATERIALS AND METHODSInhibitors. Human a2PI was prepared as described (1) and was judged greater than 95% homogeneous on disc gel electrophoresis, sodium dodecyl sulfate gel electrophoresis, and immunoelectrophoresis. The concentration of purified a2PI was determined by using 7.03 as extinction coefficient El% at 280 um. a2-Macroglobulin (a2M), isolated from human plasma (9), gave a single band by sodium dodecyl sulfate gel electrophoresis after reduction with 2-mercaptoethanol (Mr, approximately 180,000). The concentration of a2M was determined by single radial immunodiffusion on Immuno-plates (Hyland, Costa Mesa, CA). Normal serum contains approximately 2 mg of a2M per ml. a2M at 2 mg/ml was essentially free of a2PI (<0.2 ,g/ml) when tested by a sensitive radioitnmunoassay for a2PI (unpublished data). a2M (8 mg/ml) contained no detectable C1 esterase inhibitor (Clinh), a1-antitrypsin, or antithrombin III as assayed by immunodiffusion using monospecific antiserum. Purified Clinh and monospecific antiserum against Clinh were generous gifts of J. Pensky

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“…172 Patients with this disorder have a low level of plasma α 1 -antitrypsin (an α-globulin) and a high incidence of pulmonary complications. 173 In 1969, Sharp et al 174 demonstrated a variable association of the α 1 -antitrypsin deficiency with liver disease, an observation that has had overwhelming confirmation. 175,176 It is now accepted that α 1 -antitrypsin deficiency is a common cause of chronic liver disease both in the pediatric and in the adult populations.…”

Section: Portal Diversion For α 1 -Antitrypsin Deficiencymentioning

confidence: 99%

The ECK fistula in animals and humans

Starzl¹

1983

Current Problems in Surgery

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The Electrophoretic α;1-Globulin Pattern of Serum in α;1-Antitrypsin Deficiency

Cited by 611 publications

References 0 publications

Adenovirus-mediated expression of an elastase-specific inhibitor (elafin): a comparison of different promoters

Adenovirus-mediated expression of an elastase-specific inhibitor (elafin): a comparison of different promoters

Inhibitory spectrum of alpha 2-plasmin inhibitor.

The ECK fistula in animals and humans

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