Arteriosclerosis (Dallas, Tex.)最新文献

{"title":"Hemodynamics and low density lipoprotein metabolism. Rates of low density lipoprotein incorporation and degradation along medial and lateral walls of the rabbit aorto-iliac bifurcation.","authors":"S A Berceli,&nbsp;V S Warty,&nbsp;R A Sheppeck,&nbsp;W A Mandarino,&nbsp;S K Tanksale,&nbsp;H S Borovetz","doi":"10.1161/01.atv.10.5.686","DOIUrl":"https://doi.org/10.1161/01.atv.10.5.686","url":null,"abstract":"<p><p>We have investigated whether arterial wall low density lipoprotein (LDL) metabolism in areas of disturbed flow differs from the metabolism in adjacent regions of undisturbed flow. Using the rabbit aorto-iliac bifurcation as a model, we examined the rates of LDL incorporation and catabolism in vivo and correlated them to the arterial flow patterns in these regions. The trapped ligand method was used to quantitate the rates of LDL incorporation and degradation over a 20-hour period in three hemodynamic zones of the daughter iliac branch: 1) a region of flow separation where the shearing forces are elevated along the medial wall and reduced along the lateral wall, 2) a transition region where the flow patterns begin to approach the fully established situation, and 3) a unidirectional flow region with symmetric fluid shearing forces along the medial and lateral walls. Our results indicate an elevated rate of LDL incorporation into the lateral versus the medial wall in the proximal zone of flow separation (5.2 +/- 0.8 nl/mg/hr vs. 3.7 +/- 0.5 nl/mg/hr, p less than 0.01). A similar elevation in the degradation rate of the lateral over the medial wall of this most proximal zone was also observed (2.1 +/- 0.4 vs. 1.4 +/- 0.2, p less than 0.05). No such differences were observed regarding LDL incorporation and degradation in the transitional or unidirectional hemodynamic zones. These results suggest that modifications in arterial wall LDL incorporation and catabolism are induced by hemodynamic forces. The implications of these findings for the formation of the atherosclerotic lesion are discussed.</p>","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 5","pages":"686-94"},"PeriodicalIF":0.0,"publicationDate":"1990-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1161/01.atv.10.5.686","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13550485","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"44th Annual Meeting. Council on Arteriosclerosis. Dallas, Texas, November 1990. Abstracts.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 5","pages":"751a-871a"},"PeriodicalIF":0.0,"publicationDate":"1990-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13552511","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Isolation and characterization of several plasma apolipoproteins of common marmoset monkey.","authors":"D Crook,&nbsp;K H Weisgraber,&nbsp;S C Rall,&nbsp;R W Mahley","doi":"10.1161/01.atv.10.4.625","DOIUrl":"https://doi.org/10.1161/01.atv.10.4.625","url":null,"abstract":"<p><p>To explore the potential of the common marmoset monkey (Callithrix jacchus) as a model for human plasma lipoprotein metabolism, several marmoset apolipoproteins were isolated and characterized in this study. Based on several properties, including molecular weight, amino acid composition, and sequence, the marmoset apolipoproteins are strikingly similar to human apolipoprotein (apo) A-I, A-II, C-III, and A-IV. The first 54 residues of marmoset apo A-I showed 87% sequence identity with the corresponding region of human apo A-I. Amino-terminal sequence analysis of a minor basic apo A-I isoform revealed that it contained an amino-terminal hexapeptide extension (Arg-His-Phe-Gln-Gln-) identical to that found in human proapo A-I. Like apo A-II in most nonhuman primates, marmoset apo-A-II differed from human apo A-II in that it did not contain cysteine and therefore existed as a monomer. The complete amino acid sequence of marmoset apo A-II was deduced. The protein contains 77 amino acids, as does human apo A-II, and showed an 82% identity with its human equivalent. In both species, apo C-III and E had similar amino-terminal sequences and amino acid compositions. Like human apo E, marmoset apo E contained minor sialylated isoforms. However, unlike human apo C-III, no sialyated isoforms of marmoset apo C-III were observed. In addition, the marmoset possessed an apolipoprotein whose molecular weight and amino acid composition were similar to those of human apo A-IV. The close structural similarities between corresponding marmoset and human apolipoproteins indicate that the marmoset monkey will be useful as a model for human lipoprotein metabolism.</p>","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 4","pages":"625-32"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1161/01.atv.10.4.625","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13270310","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of growth factors on human vascular endothelial cell prostacyclin production.","authors":"A Ristimäki,&nbsp;O Ylikorkala,&nbsp;L Viinikka","doi":"10.1161/01.atv.10.4.653","DOIUrl":"https://doi.org/10.1161/01.atv.10.4.653","url":null,"abstract":"<p><p>Prostacyclin (PGI2) is an antithrombotic factor, which may prevent the initiation and the complications of arteriosclerosis. The most important site of PGI2 production is the vascular endothelium, but little is known about how this process is regulated. In this connection, there is special interest in the roles of various growth factors released from platelets, macrophages, vascular smooth muscle cells, and the endothelial cells themselves. We investigated the effects of transforming growth factor-beta (TGF-beta), platelet-derived growth factor (PDGF), and acidic and basic fibroblast growth factors (aFGF and bFGF) on the PGI2 production of cultured human umbilical vein endothelial cells by measuring the stable metabolite of PGI2, 6-keto-prostaglandin F1 alpha, by radioimmunoassay. TGF-beta induced dose- and time-dependent stimulation of PGI2 production. The lowest stimulatory concentration of TGF-beta was 0.1 ng/ml, and the maximal response, a 2.1-fold rise, was obtained with 1.0 ng/ml. The effect of TGF-beta lasted 48 hours and was blocked by inhibitors of transcription, translation, and cyclooxygenase. Maximal stimulation by TGF-beta was enhanced by epidermal growth factor. PDGF and bFGF had no effect on PGI2 production, but aFGF inhibited it. This is the first demonstration that TGF-beta enhances PGI2 production by human vascular cells, and this phenomenon may be part of negative feedback mechanisms that prevent thrombosis and arteriosclerosis.</p>","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 4","pages":"653-7"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1161/01.atv.10.4.653","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13270311","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Coronary atherosclerosis in the pig. Induced plaque injury and platelet response.","authors":"R L Reddick,&nbsp;M S Read,&nbsp;K M Brinkhous,&nbsp;D Bellinger,&nbsp;T Nichols,&nbsp;T R Griggs","doi":"10.1161/01.atv.10.4.541","DOIUrl":"https://doi.org/10.1161/01.atv.10.4.541","url":null,"abstract":"<p><p>The thrombogenic potential of atherosclerotic diet-induced coronary atherosclerotic plaques was investigated in normal swine and in bleeder swine with homozygous von Willebrand disease. Fourteen paired normal and bleeder swine were placed on a 1% cholesterol diet for 1 to 16 weeks. Serum cholesterol was elevated in all animals at sacrifice. Foam cell deposits developed in all major epicardial coronary arteries, and lesions progressed over time from small subendothelial foam cell deposits to fibrous cap lesions that contained foam cells, elastic fibers, collagen, degenerative material, and smooth muscle cells. Balloon catheter injury resulted in platelet deposition, largely in a monolayer or as small platelet clumps devoid of fibrin. Lipid debris was present in injured areas of the subendothelium but did not induce thrombus formation. When the injury involved the media, platelet-fibrin thrombi were formed. Lipid was not present in these thrombi. Morphometric analysis of platelet deposition on ballooned atherosclerotic vessels showed similar numbers of platelets in both phenotypes. However, the attached platelets in bleeder pigs showed significantly less spreading than did those in the normal animals. The results show that injury to intimal foam cell and mixed cellular lesions in coronary arteries of cholesterol-fed swine does not promote the development of platelet-fibrin thrombus formation. In contrast, when the injury extended to the media, mixed thrombi were formed.</p>","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 4","pages":"541-50"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1161/01.atv.10.4.541","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13518114","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Testosterone regulates metabolism of plasma chylomicrons in rats.","authors":"I Staprans,&nbsp;J H Rapp,&nbsp;X M Pan,&nbsp;D L Ong,&nbsp;K R Feingold","doi":"10.1161/01.atv.10.4.591","DOIUrl":"https://doi.org/10.1161/01.atv.10.4.591","url":null,"abstract":"<p><p>Previously we demonstrated a marked sex difference in the metabolism of chylomicrons in adult rats. In males, radiolabeled chylomicrons displayed a longer dwell time on endothelial surfaces, which resulted in a decreased chylomicron uptake by the liver. The increased rate of chylomicron metabolism in females was associated with increased postheparin lipoprotein lipase activity. In the present study, we have investigated the effects of physiological doses of sex steroid hormones on the metabolism of chylomicrons and postheparin lipoprotein lipase activity. No sex differences were found in prepubertal animals. We also found no difference in chylomicron metabolism in control female, castrated female, estrogen-treated female, castrated male, and estrogen-treated male rats. However, control male, testosterone-treated male, and testosterone-treated female rats showed increased endothelial binding of chylomicrons and decreased chylomicron uptake by the liver. Postheparin lipoprotein lipase activity also was decreased by testosterone administration. In parallel with the alterations in chylomicron metabolism, serum high density lipoprotein levels in male rats decreased with testosterone administration. These results indicate that the differences in chylomicron metabolism, postheparin lipoprotein lipase activities, and serum high density lipoprotein levels observed between male and female rats are due to testosterone.</p>","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 4","pages":"591-6"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1161/01.atv.10.4.591","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13518118","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"\"Portal\" adipose tissue as a generator of risk factors for cardiovascular disease and diabetes.","authors":"P Björntorp","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 4","pages":"493-6"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13350083","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ischemic heart disease risk in postmenopausal women. Effects of estrogen use on glucose and insulin levels.","authors":"E Barrett-Connor,&nbsp;M Laakso","doi":"10.1161/01.atv.10.4.531","DOIUrl":"https://doi.org/10.1161/01.atv.10.4.531","url":null,"abstract":"<p><p>We report the fasting and post-challenge plasma insulin and glucose levels in 469 nondiabetic postmenopausal women from the Rancho Bernardo cohort according to the current use of estrogen replacement therapy. In these older women, the use of noncontraceptive estrogen was not associated with impaired glucose tolerance. Estrogen-treated women had lower levels of insulin than women who were not taking estrogen; these differences were not explained by age, obesity, or differential hormone use by women with known glucose intolerance. There were no significant differences in glucose and insulin levels in those taking conjugated equine estrogen (Premarin) alone compared to those taking it with medroxyprogesterone acetate (Provera).</p>","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 4","pages":"531-4"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1161/01.atv.10.4.531","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13317862","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Differential effect of Photofrin II on growth of human smooth muscle cells from nonatherosclerotic arteries and atheromatous plaques in vitro.","authors":"P C Dartsch,&nbsp;T Ischinger,&nbsp;E Betz","doi":"10.1161/01.atv.10.4.616","DOIUrl":"https://doi.org/10.1161/01.atv.10.4.616","url":null,"abstract":"<p><p>The effect of dihematoporphyrin-ester or -ether (DHE), a photosensitizing porphyrin with different amounts of aggregates, on the growth of cultured smooth muscle cells obtained from nonatherosclerotic arteries and from atheromatous plaques (primary stenosing and restenosing lesions) was examined without photoactivation of the drug. Clinically relevant DHE concentrations ranging from 0.1 to 25 micrograms/ml were used. In all proliferation studies with cells of second and third passage (approximately 10 cumulative population doublings in vitro), the growth rates decreased in a dose-dependent manner. Smooth muscle cells from atherosclerotic lesions were significantly more sensitive than smooth muscle cells from normal arteries. Cells derived from restenosing lesions retained their increased sensitivity even after eight passages in culture (approximately 20 cumulative population doublings). Cell size measurements showed that the decreased proliferative activity mainly occurred in smooth muscle cell subpopulations consisting of small cells. A cytotoxic effect of DHE was observed at concentrations above 5 micrograms/ml, causing cytoplasmic protrusions, vacuoles, and even complete cell lysis. At a DHE concentration of 5 micrograms/ml, the number of viable cells was 73% +/- 14% (means +/- SD) for smooth muscle cells from nonatherosclerotic arterial media and only 38% +/- 11% (means +/- SD) for smooth muscle cells from atherosclerotic plaques. In all experiments, no significant difference in response to DHE treatment was observed between cells from primary stenosing and restenosing lesions, suggesting a specific mechanism for plaque-derived cells causing an increased sensitivity in comparison to smooth muscle cells from nonatherosclerotic arteries. The pronounced sensitivity of plaque cells against DHE treatment suggests that this drug--even without photoactivation--is potentially valuable in vivo as a therapeutic approach to vascular stenoses.</p>","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 4","pages":"616-24"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1161/01.atv.10.4.616","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13296379","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Retroendocytosis of high density lipoproteins by the human hepatoma cell line, HepG2.","authors":"A M Kambouris,&nbsp;P D Roach,&nbsp;G D Calvert,&nbsp;P J Nestel","doi":"10.1161/01.atv.10.4.582","DOIUrl":"https://doi.org/10.1161/01.atv.10.4.582","url":null,"abstract":"<p><p>When human HepG2 hepatoma cells were pulsed with 125I-labeled high density lipoproteins (HDL) and chased in fresh medium, up to 65% of the radioactivity released was precipitable with trichloroacetic acid. Cell-internalized 125I-HDL contributed to the release of acid-precipitable material; when cells were treated with trypsin before the chase to remove 125I-HDL bound to the outer cell membrane, 50% of the released material was still acid-precipitable. Characterization of the radioactive material resecreted by trypsinized cells revealed the presence of particles that were similar in size and density to mature HDL and contained intact apolipoproteins (apo) A-I and A-II. The release of internalized label occurred at 37 degrees C but not at 4 degrees C. Monensin, which inhibits endosomal recycling of receptors, decreased the binding of 125I-HDL to cells by 75%, inhibited the release of internalized radioactivity as acid-precipitable material by 80%, and increased the release of acid-soluble material by 90%. In contrast, the lysosomal inhibitor chloroquine increased the association of 125I-HDL to cells by 25%, inhibited the release of precipitable material by 10%, and inhibited the release of acid-soluble radioactivity by 80%. Pre-incubation with cholesterol caused a 50% increase in the specific binding, internalization, and resecretion of HDL label. Cholesterol affected the release of acid-precipitable label much more (+90%) than that of acid-soluble material (+20%). Taken together, these findings suggest that HepG2 cells can bind, internalize, and resecrete HDL by a retroendocytotic process. Furthermore, the results with cholesterol and monensin indicate that a regulated, recycling, receptor-like molecule is involved in the binding and intracellular routing of HDL.</p>","PeriodicalId":77492,"journal":{"name":"Arteriosclerosis (Dallas, Tex.)","volume":"10 4","pages":"582-90"},"PeriodicalIF":0.0,"publicationDate":"1990-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1161/01.atv.10.4.582","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13518117","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}