cutis laxa/protease

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AiltTrialacha cliniciúlaPaitinní

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Leathanach 1 ó 42 torthaí

Characterization and partial purification of a neutral protease from the serum of a patient with autosomal recessive pulmonary emphysema and cutis laxa.

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Logáil Isteach / Cláraigh

Serum enzyme activity in 81 patients with various medical and dermatologic problems was determined with succinyl-(L-alanyl)3-p-nitroanilide as substrate. Values exceeding the limit of mean +/- 3 SD in healthy controls were detected in 16 patients. The highest activity, greater than 80 times the mean

Alveolar macrophage-mediated elastolysis: roles of matrix metalloproteinases, cysteine, and serine proteases.

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Logáil Isteach / Cláraigh

Chronic obstructive pulmonary disease (COPD) is a common lung disease with cigarette smoking as the major etiological factor, but only 15% of smokers develop COPD. Destruction of lung elastin observed in COPD is mediated by many enzymes, including cysteine, serine, and matrix metalloproteinases

Elastase-like protease and elastolytic activities expressed in cultured dermal fibroblasts derived from lesional skin of patients with pseudoxanthoma elasticum, actinic elastosis, and cutis laxa.

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Logáil Isteach / Cláraigh

Functional consequence of fibulin-4 missense mutations associated with vascular and skeletal abnormalities and cutis laxa.

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Logáil Isteach / Cláraigh

Fibulin-4 is a 60kDa calcium binding glycoprotein that has an important role in development and integrity of extracellular matrices. It interacts with elastin, fibrillin-1 and collagen IV as well as with lysyl oxidases and is involved in elastogenesis and cross-link formation. To date, several

The cell-elastin-elastase(s) interacting triade directs elastolysis.

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Logáil Isteach / Cláraigh

Human elastases have been identified within serine, cysteine and metallopeptidase families. These enzymes are able to adsorb rapidly onto elastin, but they can also bind onto cell surface-associated proteins such as heparan sulfate proteoglycans, both interactions involving enzyme exosites distinct

Elastolysis by proteinase 3 and its inhibition by alpha(1)-proteinase inhibitor: a mechanism for the incomplete inhibition of ongoing elastolysis.

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Logáil Isteach / Cláraigh

An excess of proteinase 3 (Pr3) is an assumed risk factor for elastin loss in chronic obstructive pulmonary disease. This study compared the degradation of [(14)C]elastin by Pr3 and its inhibition by alpha(1)-proteinase inhibitor (alpha(1)-PI) with the analogous reactions involving two other

Primary structure of human pancreatic protease E determined by sequence analysis of the cloned mRNA.

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Logáil Isteach / Cláraigh

Although protease E was isolated from human pancreas over 10 years ago [Mallory, P. A., & Travis, J. (1975) Biochemistry 14, 722-729], its amino acid sequence and relationship to the elastases have not been established. We report the isolation of a cDNA clone for human pancreatic protease E and

Middermal Elastolysis: Dermal Fibroblasts Cooperate with Inflammatory Cells to the Elastolytic Disorder.

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Logáil Isteach / Cláraigh

Little is known about the cause and pathophysiology of middermal elastolysis (MDE). In this condition, variable inflammatory infiltrate may be present or not together with loss of elastic fibres in the middermis that spares both papillary and lower reticular dermis. MDE may be a consequence of

Possible mechanisms of emphysema in smokers: cigarette smoke condensate suppresses protease inhibition in vitro.

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Logáil Isteach / Cláraigh

To study the possible role of suppression of antiproteases by cigarette smoke in the pathogenesis of pulmonary emphysema in smokers, the following experiments were carried out. Elastin-agarose gels were impregnated with cigarette smoke condensate dissolved in dimethyl sulfoxide or with the solvent

Ceruloplasmin: plasma inhibitor of the oxidative inactivation of alpha 1-protease inhibitor.

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Logáil Isteach / Cláraigh

When leukocyte lysosomal extracts are used as a source of elastase and are combined with a fraction of plasma containing sufficient alpha 1-protease inhibitor (alpha 1-Pi) to inhibit all but 30 to 40% of the elastase amidase activity, elastolysis occurs at 69% of the rate of the uninhibited elastase

Sweet's syndrome leading to acquired cutis laxa (Marshall's syndrome) in an infant with alpha 1-antitrypsin deficiency.

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Logáil Isteach / Cláraigh

BACKGROUND Marshall's syndrome is a rare pediatric skin disease that is characterized by acquired, localized neutrophilic dermatitis (Sweet's disease), followed by loss of elastic tissue in the dermis and cutis laxa. The cause of this syndrome is unknown. alpha 1-Antitrypsin (alpha 1-AT) deficiency

Trophoblast- and vascular smooth muscle cell-derived MMP-12 mediates elastolysis during uterine spiral artery remodeling.

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Logáil Isteach / Cláraigh

During the first trimester of pregnancy, the uterine spiral arteries are remodeled, creating heavily dilated conduits that lack maternal vasomotor control but allow the placenta to meet an increasing requirement for nutrients and oxygen. To effect permanent vasodilatation, the internal elastic

Lysosomal cysteine proteases in atherosclerosis.

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Logáil Isteach / Cláraigh

Atherosclerosis is an inflammatory disease characterized by extensive remodeling of the extracellular matrix architecture of the arterial wall. Although matrix metalloproteinases and serine proteases participate in these pathologic events, recent data from atherosclerotic patients and animals

Pathogenesis of COPD. Part I. The role of protease-antiprotease imbalance in emphysema.

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Logáil Isteach / Cláraigh

This review covers protease-antiprotease imbalance in the development of emphysema in smokers. This imbalance is likely to play a major pathogenic role in the development of emphysema in subjects with severe alpha1-antitrypsin deficiency who smoke because of a deficient antiprotease protection

Secreted LasA of Pseudomonas aeruginosa is a staphylolytic protease.

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Logáil Isteach / Cláraigh

Full expression of the elastolytic phenotype of Pseudomonas aeruginosa depends on LasA, an extracellular protease with restricted specificity whose mode of action on elastin and biological role is not understood. LasA exhibits amino acid sequence homology to some bacteriolytic proteases and shares

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