{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T06:59:40Z","timestamp":1761893980053,"version":"build-2065373602"},"reference-count":49,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2004,7,8]],"date-time":"2004-07-08T00:00:00Z","timestamp":1089244800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["pathsocjournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Journal of Pathology"],"published-print":{"date-parts":[[2004,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Numerous apolipoproteins associate with amyloid plaques. A minor high\u2010density lipoprotein\u2010associated protein, glycosylphosphatidylinositol\u2010specific phospholipase D (GPI\u2010PLD), has recently been described by the authors and others. Since GPI\u2010PLD is synthesized by, and secreted from, pancreatic islet \u03b2 cells, the present study examined the hypothesis that GPI\u2010PLD associates with islet amyloid. GPI\u2010PLD immunoreactivity was examined in pancreatic tissues from type 2 diabetic and non\u2010diabetic humans. GPI\u2010PLD binding to heparan sulphate proteoglycan was determined in the absence or presence of heparan sulphate or heparin. Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI\u2010PLD. In non\u2010diabetics, GPI\u2010PLD immunoreactivity was present and co\u2010localized with insulin, as opposed to co\u2010localizing with amyloid in diabetics. No immunoreactivity for apolipoprotein A\u2010I was present in islet cells or islet amyloid. Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI\u2010PLD <jats:italic>in vitro<\/jats:italic>. GPI\u2010PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide <jats:italic>in vitro<\/jats:italic>. GPI\u2010PLD is therefore present in islet amyloid and appears to derive from local production from islets. This localization likely derives from interaction between GPI\u2010PLD and heparan sulphate proteoglycan. Since GPI\u2010PLD also inhibited islet amyloid polypeptide fibril formation <jats:italic>in vitro<\/jats:italic>, it is concluded that GPI\u2010PLD may play a role in islet amyloid formation in type 2 diabetes. Copyright \u00a9 2004 Pathological Society of Great Britain and Ireland. 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