About: Assembly of the silk fibroin elementary unit in endoplasmic reticulum and a role of L‐chain for protection of α1,2‐mannose residues in N‐linked oligosaccharide chains of fibrohexamerin/P25

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About: Assembly of the silk fibroin elementary unit in endoplasmic reticulum and a role of L‐chain for protection of α1,2‐mannose residues in N‐linked oligosaccharide chains of fibrohexamerin/P25 Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Assembly of the silk fibroin elementary unit in endoplasmic reticulum and a role of L‐chain for protection of α1,2‐mannose residues in N‐linked oligosaccharide chains of fibrohexamerin/P25
Creator	Inoue, Satoshi Taira, Hideharu Nakajima, Tasuku Yamashita, Tetsuro Imamura, Morikazu »more»
source	Medline; PMC
abstract	Silk fibroin of Bombyx mori is secreted from the posterior silk gland (PSG) as a 2.3‐MDa elementary unit, consisting of six sets of a disulfide‐linked heavy chain (H‐chain)–light chain (L‐chain) heterodimer and one molecule of fibrohexamerin (fhx)/P25. Fhx/P25, a glycoprotein, associates noncovalently with the H–L heterodimers. The elementary unit was found and purified from the endoplasmic reticulum (ER) extract of PSG cells. A substantial amount of fhx/P25 unassembled into the elementary unit was also present in ER. In normal‐level fibroin‐producing breeds (J‐139 and C108), the elementary unit contained fhx/P25 of either 30 kDa (major) or 27 kDa (minor). The 27‐kDa fhx/P25 was produced from the 30‐kDa form by digestion with the bacterial α1,2‐mannosidase in vitro. The elementary unit in the ER extract contained only the 30‐kDa fhx/P25, whereas both 30‐ and 27‐kDa forms of fhx/P25 were present in the ER plus Golgi mixed extracts. In naked‐pupa mutants [Nd(2), Nd‐s and Nd‐s (D)], extremely small amounts of fibroin were produced and they consisted of one molecule of 27‐kDa fhx/P25 and six molecules of H‐chain but no L‐chain. When the Nd‐s (D) mutant was subjected to transgenesis with the normal L‐chain gene, the (H‐L)(6)fhx(1)‐type elementary unit containing the 30‐kDa fhx/P25, was produced. These results suggest that fhx/P25 in the elementary unit is largely protected from digestion with Golgi α1,2‐mannosidases when L‐chains are present in the unit. Models suggesting a role of L‐chain for the protection of α1,2‐mannose residues of fhx/P25 are presented.
has issue date	2003-12-19(xsd:dateTime)
bibo:doi	10.1046/j.1432-1033.2003.03934.x
bibo:pmid	14717703
has license	no-cc
sha1sum (hex)	c1f92b2880a7d4216be9f68ffa537e391626c5bc
schema:url	https://doi.org/10.1046/j.1432-1033.2003.03934.x
resource representing a document's title	Assembly of the silk fibroin elementary unit in endoplasmic reticulum and a role of L‐chain for protection of α1,2‐mannose residues in N‐linked oligosaccharide chains of fibrohexamerin/P25
has PubMed Central identifier	PMC7232747
has PubMed identifier	14717703
schema:publication	Eur J Biochem
resource representing a document's body	covid:c1f92b2880a7d4216be9f68ffa537e391626c5bc#body_text
is schema:about of	named entity 'endoplasmic reticulum' named entity 'N-linked oligosaccharide' named entity 'sericin' named entity 'filtration' named entity 'molecular forms' »more»

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