{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T11:46:11Z","timestamp":1773661571814,"version":"3.50.1"},"reference-count":33,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2004,2,19]],"date-time":"2004-02-19T00:00:00Z","timestamp":1077148800000},"content-version":"vor","delay-in-days":9545,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Supramol Struct"],"published-print":{"date-parts":[[1978,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>A rise in the intracellular concentration of Ca<jats:sup>2+<\/jats:sup>\u2010ions in human erythrocytes causes the formation of high\u2010molecular\u2010weight membrane protein polymers, cross\u2010linked by \u03b3\u2010glutamyl\u2010\u03f5\u2010lysine side chain bridges. Cross\u2010linking involves proteins at the cytoplasmic side of the membrane (band 4.1, spectrin, and band 3 materials) and the reaction is catalyzed by the intrinsic transglutaminase. This enzyme is regulated by Ca<jats:sup>2+<\/jats:sup>\u2010ions and it exists in a latent form in normal cells. The protein polymer, isolated from the membranes of Ca<jats:sup>2+<\/jats:sup>\u2010loaded intact human red cells, is heterogeneous in size and may contain as many as 6 moles of \u03b3\u2010glutamyl\u2010\u03f5\u2010lysine cross\u2010links per 100,000 gm of protein.<\/jats:p><jats:p>Synthetic compounds, which either compete against the \u03f5\u2010lysine cross\u2010linking functionalities of the protein substrates (eg, histamine, aminoacetonitrile, cystamine) or directly inactivate the transamidase (eg, cystamine), inhibit the membrane polymerization reaction in intact human erythrocytes. They also interfere with the Ca<jats:sup>2+<\/jats:sup>\u2010induced irreversible shape change from discocyte to echinocyte and inhibit the irreversible loss of membrane deformability. Thus, the transamidase\u2010catalyzed production of \u03b3\u2010glutamyl\u2010\u03f5\u2010lysine cross\u2010links in the membrane may be a common denominator in these cellular manifestations.<\/jats:p>","DOI":"10.1002\/jss.400090313","type":"journal-article","created":{"date-parts":[[2005,5,28]],"date-time":"2005-05-28T05:29:59Z","timestamp":1117258199000},"page":"427-440","source":"Crossref","is-referenced-by-count":72,"title":["Formation of \u03b3\u2010glutamyl\u2010\u03f5\u2010lysine bridges between membrane proteins by a Ca<sup>2+<\/sup>\u2010regulated enzyme in intact erythrocytes"],"prefix":"10.1002","volume":"9","author":[{"given":"L.","family":"Lorand","sequence":"first","affiliation":[]},{"suffix":"Jr","given":"G. 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