{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,4]],"date-time":"2026-03-04T09:23:15Z","timestamp":1772616195846,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1979,6,15]]},"abstract":"<jats:p>Removal of the terminal sialic acid residues from many serum glycoproteins results in exposure of their penultimate galactose residues and rapid clearance from circulation by the liver. Low-density lipoprotein is a glycoprotein containing 21 galactose and 9 sialic acid residues per particle. Studies in this laboratory and others have shown that both the liver and extrahepatic tissues contribute to the degradation of low-density lipoprotein. This study was undertaken to determine whether desialylation of pig low-density lipoprotein alters its removal from circulation. Low-density lipoprotein was incubated at 37 degrees C with an agarose-bound neuraminidase, proteinase-free, from Clostridium perfringens. After 18 h at pH 5.0, 70% of the sialic acid residues were removed. The desialylated 131I-labelled and native 125I-labelled low-density lipoproteins were simultaneously injected into a pig, and their disappearance from plasma was followed for 96 h. The turnovers of the two were identical. In contrast, neuraminidase-treated fetuin was cleared about 200-fold faster than native fetuin. Studies were also performed in cultured rat hepatocytes. Rates of degradation of native and neuraminidase-treated low-density lipoprotein were similar, whereas asialo-fetuin was degraded at six to ten times the rate of native fetuin. Thus desialylation does not appear to alter low-density-lipoprotein catabolism by hepatic or extrahepatic cells.<\/jats:p>","DOI":"10.1042\/bj1800647","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:16:46Z","timestamp":1439237806000},"page":"647-654","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":52,"title":["Unaltered catabolism of desialylated low-density lipoprotein in the pig and in cultured rat hepatocytes"],"prefix":"10.1042","volume":"180","author":[{"given":"A D","family":"Attie","sequence":"first","affiliation":[]},{"given":"D B","family":"Weinstein","sequence":"additional","affiliation":[]},{"given":"H H","family":"Freeze","sequence":"additional","affiliation":[]},{"given":"R C","family":"Pittman","sequence":"additional","affiliation":[]},{"given":"D","family":"Steinberg","sequence":"additional","affiliation":[]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/180\/3\/647\/572742\/bj1800647.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/180\/3\/647\/572742\/bj1800647.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T13:03:27Z","timestamp":1637931807000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/180\/3\/647\/4183\/Unaltered-catabolism-of-desialylated-low-density"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1979,6,15]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1979,6,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1800647","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1979,6,15]]}}}