{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T17:59:36Z","timestamp":1782755976231,"version":"3.54.5"},"reference-count":40,"publisher":"Walter de Gruyter GmbH","issue":"11","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,11,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n<jats:p>Beta-glucosidases (GBA) include GBA1, GBA2 and other \u03b2-glucosidases (non-GBA1-2). GBA1 is a lysosomal and GBA2 an extra-lysosomal enzyme. GBA1- and GBA2-deficient genetic conditions, with different phenotypes, are glucosylceramide (GC; the main GBA substrate) accumulating diseases. To study the activity profile of GBA, live fibroblasts were loaded with radioactive GC. The GC metabolism was measured in wild-type, GBA1-deficient (Gaucher disease) and GBA2-deficient (<jats:italic>Gba2<\/jats:italic><jats:sup><jats:italic>-\/-<\/jats:italic><\/jats:sup> mouse) cells. The differences found allowed the prediction of marked proportions of GBA1, GBA2, and particularly non-GBA1-2 (probably including GBA3, a cytosolic \u03b2-glucosidase) activity for wild-type cells. The high proportion of non-GBA1-2 suggests an important role of these enzymes.<\/jats:p>","DOI":"10.1515\/hsz-2015-0144","type":"journal-article","created":{"date-parts":[[2015,5,21]],"date-time":"2015-05-21T14:28:02Z","timestamp":1432218482000},"page":"1241-1246","source":"Crossref","is-referenced-by-count":6,"title":["High \u03b2-glucosidase (GBA) activity not attributable to GBA1 and GBA2 in live normal and enzyme-deficient fibroblasts may emphasise the role of additional GBAs"],"prefix":"10.1515","volume":"396","author":[{"given":"Klaus","family":"Harzer","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yildiz","family":"Yildiz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"374","reference":[{"key":"ref21","first-page":"282","article-title":"Boot Identification of the non - lysosomal glucosylceramidase as \u03b2 - glucosidase","author":"Verhoek","year":"2007","journal-title":"Biol Chem"},{"key":"ref101","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.ajhg.2012.11.021","article-title":"Loss of function of glucocerebrosidase is responsible for motor neuron defects in hereditary spastic paraplegia","author":"Martin","year":"2013","journal-title":"Am Hum Genet"},{"key":"ref241","first-page":"282","article-title":"Boot Identification of the non - lysosomal glucosylceramidase as \u03b2 - glucosidase","author":"Verhoek","year":"2007","journal-title":"Biol Chem"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1055\/s-2005-865608","article-title":"Prosaposin deficiency a rarely diagnosed rapidly progressing neonatal neurovisceral lipid storage disease Report of a further patient","author":"Elleder","year":"2005","journal-title":"Neuropediatrics"},{"key":"ref321","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.ajhg.2012.11.021","article-title":"Loss of function of glucocerebrosidase is responsible for motor neuron defects in hereditary spastic paraplegia","author":"Martin","year":"2013","journal-title":"Am Hum Genet"},{"key":"ref391","first-page":"113","article-title":"Glucosylceramide and glucosylsphingosine metabolism in cultured fibroblasts deficient in acid \u03b2 - glucosidase activity","volume":"115","author":"Sasagasako","year":"1994","journal-title":"Biochem"},{"key":"ref191","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0925-4439(93)90090-N","article-title":"Demonstration of the existence of a second non - 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glucosidase from human liver","author":"Matern","year":"1997","journal-title":"Biol Chem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bcmd.2010.07.009","article-title":"The cytosolic \u03b2 - glucosidase does not influence type disease manifestation","volume":"46","author":"Dekker","year":"2011","journal-title":"Blood Cells Mol Dis"},{"key":"ref171","first-page":"113","article-title":"Glucosylceramide and glucosylsphingosine metabolism in cultured fibroblasts deficient in acid \u03b2 - glucosidase activity","volume":"115","author":"Sasagasako","year":"1994","journal-title":"Biochem"},{"key":"ref261","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1055\/s-2005-865608","article-title":"Prosaposin deficiency a rarely diagnosed rapidly progressing neonatal neurovisceral lipid storage disease Report of a further patient","author":"Elleder","year":"2005","journal-title":"Neuropediatrics"},{"key":"ref271","first-page":"128","article-title":"Intrauterine onset of acute neuropathic type disease identification of a novel insertion sequence","author":"Felderhoff","year":"2004","journal-title":"Am J Med Genet"},{"key":"ref411","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0925-4439(93)90090-N","article-title":"Demonstration of the existence of a second non - 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