Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arteriovenous fistulae between the external jugular vein and the common carotid artery were surgically fashioned in eight sheep. The altered hemodynamics produced morphological changes similar to those observed in human atherosclerosis. The elastica is a major mural component and undergoes considerable structural variation during lesion development. The most significant biochemical changes in the elastin occur in the experimental vein region. These include a quantitative loss particularly in the midregion of the vein and a decrease in the concentration of up to 20% of the crosslinks (desmosine and isodesmosine). There is an increase in the cholesterol content of the elastin purified from both experimental artery and vein. The bound phospholipid was higher in the experimental artery and in the dilated experimental vein. There was a significant time-dependent loss of elastin in the stressed venous tissue.
Exp Mol Pathol 1989 Oct
PMID:The biochemical composition of hemodynamically stressed vascular tissue: the insoluble elastin of experimental arteriovenous fistulae. 280 66

The connective tissue network in striated muscle, consisting principally of collagen is arranged in a three dimensional network and is intimately associated with muscle function. Previous studies have shown that animals maintained on a copper-deficient diet undergo myocardial hypertrophy and exhibit cardiovascular lesions such as ventricular aneurysms that eventually rupture. A deficiency of copper in the diet is known to inhibit lysyl oxidase, a metalloenzyme requiring copper as a cofactor and which is also responsible for collagen and elastin crosslinking. Examination by scanning and transmission electron microscopy of skeletal and cardiac muscle from rats maintained on copper-deficient diets showed both gross and microscopic lesions to the connective tissue network. Immunohistochemical staining by light microscopy with antibodies against lysyl oxidase showed that the enzyme was equally present in both control and experimental animals. Fluorescent staining for antibodies against collagen types I and III showed similar results. From these studies we concluded that the collagen secreted during hypertrophy was not crosslinked by lysyl oxidase due to the absence of the copper cofactor. This resulted in the failure of the connective tissue network to transmit and distribute the increased force associated with myocardial hypertrophy and resulted in myocardial aneurysms.
J Mol Cell Cardiol 1985 Dec
PMID:Alteration of the connective tissue network of striated muscle in copper deficient rats. 286 28

Dielectric measurements, as a function of hydration, are reported for collagen, cytochrome-c, elastin and lysozyme powders. The hydration dependence of the dispersion that occurs in the frequency range between 10 kHz and 10 GHz has been used to identify two classes of protein-bound water molecules (namely, rotationally hindered or unhindered), as well as the hydration level for the onset of an increasing protein flexibility. Such studies can aid an understanding of the relationship between enzyme activity and structural flexibility, and of hydration-induced changes in the structure and dynamics of protein structures.
J Mol Biol 1985 Jan 20
PMID:Dielectric studies of protein hydration and hydration-induced flexibility. 298 34

In an attempt to clarify the roles of proteases in the developmental mechanisms of hypertensive vascular lesions, changes in activities of aortic elastase, collagenase, and cathepsin D in spontaneously hypertensive rats (SHR) and renal hypertensive rats were biochemically investigated. In SHR, elastase activity initially showed a significant increase, once two-fold higher than that in the control; but the activity tended to decrease earlier than that in the control. In both SHR and normotensive control rats collagenase activities tended to increase with advancing age. The activity in SHR was two-fold higher than that in the control at all ages examined. In both younger SHR and normotensive rats cathepsin D activities proved to be increased with advancing age, while in old rats the activities tended to decrease. The activity in SHR was three- to fivefold higher than that in the control at all ages examined. In renal hypertensive rats, the activities of elastase, collagenase, and cathepsin D increased gradually with increasing blood pressure, at levels significantly higher than those in the control. These findings suggest that the metabolisms of proteins such as elastin and collagen, expressed by these enzyme activities, are accelerated under hypertensive conditions.
Exp Mol Pathol 1986 Apr
PMID:Elastase, collagenase, and cathepsin D activities in the aortas of spontaneously hypertensive and renal hypertensive rats. 300 14

In contrast to glutaraldehyde-fixed vascular tissue with or without staining with cationic dye, the nonfibrous extracellular matrix of fast-frozen, freeze-dried rabbit aorta and renal artery contained a continuous reticulum of fine filaments, closely associated with collagen, elastin, and smooth muscle cells. Three morphologically distinct types of filament were distinguished; one type was selectively sensitive to chondroitinase ABC degradation, and therefore contains chondroitin and/or dermatan sulfate. The remaining filaments of the reticulum may represent the protein core of the proteoglycan monomer, and the hyaluronic acid backbone of the aggregate. Filaments associated with the surface of smooth muscle cells were usually linked to a continuous filament parallel to the cell surface, which was degraded by heparitinase and therefore contains heparan sulfate. The filaments linked directly to the cell surface were not degraded by either enzyme. The preservation of PG in fast-frozen material provides a significant improvement over that obtained by any presently available technique.
J Ultrastruct Mol Struct Res 1988 Feb
PMID:Proteoglycan in fast-frozen, freeze-dried, plastic-embedded rabbit arteries. 337 71

The human protease inhibitor genes alpha 1 antitrypsin (alpha 1-PI) and alpha 1-antichymotrypsin (alpha 1-ACT) are acute-phase proteins which are induced in response to inflammation. These inhibitors function to limit the activity of serine proteases in vivo. alpha 1-PI acts as an inhibitor of neutrophil elastase to protect the elastin fibers of the lung. Genetic deficiencies of alpha 1-PI result in development of chronic pulmonary emphysema. The physiologic role of alpha 1-ACT has not been clearly defined, but it also appears to function in the maintenance of protease-protease inhibitor equilibrium in the lung. Nucleic acid and protein sequence homologies detected between alpha 1-PI and alpha 1-ACT suggested an evolutionary relationship. Gene mapping experiments were performed to determine if these protease inhibitor genes reside at the same chromosomal locus in man. In situ hybridization data demonstrate that both alpha 1-PI and alpha 1-ACT map to the same region, q31-q32.3, on chromosome 14.
Somat Cell Mol Genet 1986 Mar
PMID:Regional location of alpha 1-antichymotrypsin and alpha 1-antitrypsin genes on human chromosome 14. 348 24

Proteolytic activity for [3H]elastin, pyro-Glu-Pro-Val-pNA(S-2484), and Suc-(Ala)3-pNA(AAApNA) was demonstrated in the bound fraction extracted with 2 M KSCN + 0.1% Triton X-100 from hypersensitivity-type murine lepromas in C57BL/6N mice, while elastase-inhibitor activity was separately observed in the soluble fraction extracted with a Tris-saline buffer. Sephacryl S-200 gel chromatography showed a peak of elastolytic activity with approximately 20,000 in molecular weight. The following DEAE-Sepharose chromatography demonstrated three fractions of elastolytic activity (E-I, II, III). The inhibitory profile showed that E-I is a thiol proteinase, while E-II and E-III belong to serine proteinase-type elastases. Both E-II and E-III showed different properties with neutrophil elastase or elastase secreted from cultured macrophages, but identical characteristics to membrane bound-type elastase of monocytes. A lower level of elastolytic activity was detected in the bound fraction of nonhypersensitivity-type murine lepromas in CBA/N mice, suggesting a more involvement of membrane bound-type elastase from monocytes/macrophages during the tissue remodelings of hypersensitivity-type granulomas.
Exp Mol Pathol 1986 Aug
PMID:Elastase activity in granulomatous inflammation in experimental murine leprosy. 353 Aug 2

In this study, a rabbit antiserum directed against a 35K glycoprotein (35K-GP), extracted from connective tissue, was used to examine the localisation of this antigen within foetal bovine ligamentum nuchae at stages of development preceding (4th month) and coinciding with (7th month) active elastin biosynthesis. In these tissues the antibody, detected by a colloidal gold conjugate technique, localised specifically to 11-nm fibrils, identified as the microfibrillar component, present both in the form of independent bundles and in association with elastin in the developing elastic fibres. No other connective tissue component was recognised by the antibodies which had been purified by affinity chromatography. The ability of the antibodies to bind to the microfibrils appeared to be dependent on embedding in LR White resin, as colloidal gold binding was greatly reduced in tissue embedded in epoxy resin. These results are discussed with respect to the role that 35K-GP may play in the morphogenesis of the elastic fibre.
J Ultrastruct Mol Struct Res
PMID:Immunolocalization of a 35K structural glycoprotein to elastin-associated microfibrils. 361 48

The effect of elastase on the extracellular matrix of neonatal rat aortic smooth muscle cell cultures was monitored both chemically and ultrastructurally. Porcine pancreatic elastase was shown to decrease the elastin content in these cultures. Although chemically no distinction could be made between the elastin remaining in the culture matrix after elastase when compared to that in the nontreated cultures, the elastin was dramatically altered morphologically. The elastin assumed a "mottled" appearance after elastase treatment similar to that seen in vivo in emphysema models. A highly sensitive immunogold staining technique was used to detect elastin at the earliest stages of accumulation. Pulse experiments demonstrated an increase in protein synthesis by the cells 20 hr after elastase exposure. The culture system described here provides a model for probing in vivo elastase effects on elastin-containing tissues.
Exp Mol Pathol 1986 Oct
PMID:Elastase effect on the extracellular matrix of rat aortic smooth muscle cells in culture. 363 21

In order to study the role of elastin in arteries with respect to hypertension and hypertensive arterial disease, aortic elastin content and elastase-like enzyme activity were examined and compared in stroke-prone spontaneously hypertensive rats (SHRSP), which show malignant hypertension, and Wistar-Kyoto normotensive rats (WKY). The elastin content was lower, whereas the elastase-like activity was higher at 20 weeks of age in SHRSP than in WKY, so that the aortic elastin/enzyme ratio of SHRSP was lower than that in WKY. These differences were not found at 6 weeks of age (prehypertensive stage). For SHRSP anti-hypertensive treatment resulted in lowering the elastase-like activity and in increasing the elastin content in comparison to untreated animals. The subcellular distribution of the elastase-like activity closely correlated with that of 5'-nucleotidase activity, a plasma membrane marker enzyme. The results indicate involvement of a smooth muscle plasmalemmal elastase-like enzyme in vascular connective tissue metabolism in health and possibly also its participation in hypertensive arterial diseases.
Exp Mol Pathol 1987 Aug
PMID:Elastin and elastase-like enzyme change in aorta of rat with malignant hypertension. 364 94


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