{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,26]],"date-time":"2025-10-26T13:47:52Z","timestamp":1761486472255},"reference-count":23,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2001,5,21]],"date-time":"2001-05-21T00:00:00Z","timestamp":990403200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Arch Insect Biochem Physiol"],"published-print":{"date-parts":[[2001,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The midgut of most insects is lined with a peritrophic matrix, which is thought to facilitate digestion and protect the midgut digestive epithelial cells from abrasive damage and invasion by ingested micro\u2010organisms. The type 2 peritrophic matrix is synthesised by a complex and highly specialised organ called the cardia typically located at the junction of the cuticle\u2010lined foregut and midgut. Although the complex anatomy of this small organ has been described, virtually nothing is known of the molecular processes that lead to the assembly of the type 2 peritrophic matrix in the cardia. As a step towards understanding the synthesis of the peritrophic matrix, the synthesis and secretion of the intrinsic peritrophic matrix protein, peritrophin\u201015 has been followed in the cardia of <jats:italic>Lucilia cuprina<\/jats:italic> larvae using immuno\u2010gold localisations. The protein is synthesised by cardia epithelial cells, which have abundant rough endoplasmic reticulum, Golgi, and vesicles indicative of a general secretory function. Peritrophin\u201015 is packaged into secretory vesicles probably produced from Golgi and transported to the cytoplasmic face of the apical plasma membrane. The vesicles fuse with the plasma membrane at the base of the microvilli and release peritrophin\u201015 into the inter\u2010microvilli spaces. The protein then becomes associated with the nascent peritrophic matrix, which lies along the tips of the epithelial cell microvilli. It is proposed that peritrophin\u201015 binds to the ends of chitin fibrils present in the nascent peritrophic matrix, thereby protecting the fibril from the action of exochitinases.  Arch. Insect Biochem. Physiol. 47:76\u201385, 2001. \u00a9 2001 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/arch.1038","type":"journal-article","created":{"date-parts":[[2002,8,25]],"date-time":"2002-08-25T22:10:13Z","timestamp":1030313413000},"page":"76-85","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Secretion of the type 2 peritrophic matrix protein, peritrophin\u201015, from the cardia"],"prefix":"10.1002","volume":"47","author":[{"given":"Craig","family":"Eisemann","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gene","family":"Wijffels","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ross 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gene, \u2018C. b. peritrophin\u201048\u2019 from the myiasis fly Chrysomya bezziana","volume":"30","author":"Vuocolo T","year":"2001","journal-title":"Insect Mol Biol"},{"key":"e_1_2_1_23_1","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M009393200","article-title":"A novel family of chitin binding proteins from insect type 2 peritrophic matrix: cDNA sequences, chitin binding activity and cellular localization","author":"Wijffels G","year":"2001","journal-title":"J Biol Chem (in press"},{"key":"e_1_2_1_24_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.25.15123"}],"container-title":["Archives of Insect Biochemistry and 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