FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2026355265> ?p ?o ?g. }

• W2026355265 endingPage "15433" @default.
• W2026355265 startingPage "15425" @default.
• W2026355265 abstract "Cranin was described in 1987 as a membrane glycoprotein expressed in brain and many other tissues, which binds laminin with high affinity in a calcium-dependent manner. Dystrophin-associated glycoprotein (“dystroglycan”) is a laminin-binding protein cloned in 1992 whose relation to cranin has remained uncertain. Here we describe the purification of cranin to homogeneity from sheep brain, show cranin to be a form of dystroglycan, and localize the N terminus of β-dystroglycan to amino acid residue 654. We find that brain α-dystroglycan is tightly associated with membranes, and localizes to regions of synaptic contact as assessed by immunocytochemistry of rat cerebellum. Brain α-dystroglycan expresses high mannose/hybrid N-linked saccharides, terminal GalNAc residues, and the HNK-1 epitope. Although dystroglycan has previously been presumed to be a proteoglycan, the amino acid sequence, pI, O-sialoglycoprotease susceptibility, lectin-binding profile, and laminin-binding properties of brain dystroglycan are more typical of mucin-like proteins. Furthermore, using CHO mutant cell lines deficient in xylosyltransferase and galactosyltransferase I, which are required for glycosaminoglycan biosynthesis, it is shown that chondroitin sulfate and heparan sulfate are not critical for laminin binding, and indeed are apparently not expressed at all in dystroglycan from CHO cells. Cranin was described in 1987 as a membrane glycoprotein expressed in brain and many other tissues, which binds laminin with high affinity in a calcium-dependent manner. Dystrophin-associated glycoprotein (“dystroglycan”) is a laminin-binding protein cloned in 1992 whose relation to cranin has remained uncertain. Here we describe the purification of cranin to homogeneity from sheep brain, show cranin to be a form of dystroglycan, and localize the N terminus of β-dystroglycan to amino acid residue 654. We find that brain α-dystroglycan is tightly associated with membranes, and localizes to regions of synaptic contact as assessed by immunocytochemistry of rat cerebellum. Brain α-dystroglycan expresses high mannose/hybrid N-linked saccharides, terminal GalNAc residues, and the HNK-1 epitope. Although dystroglycan has previously been presumed to be a proteoglycan, the amino acid sequence, pI, O-sialoglycoprotease susceptibility, lectin-binding profile, and laminin-binding properties of brain dystroglycan are more typical of mucin-like proteins. Furthermore, using CHO mutant cell lines deficient in xylosyltransferase and galactosyltransferase I, which are required for glycosaminoglycan biosynthesis, it is shown that chondroitin sulfate and heparan sulfate are not critical for laminin binding, and indeed are apparently not expressed at all in dystroglycan from CHO cells." @default.
• W2026355265 created "2016-06-24" @default.
• W2026355265 creator A5033859037 @default.
• W2026355265 creator A5062980852 @default.
• W2026355265 date "1995-06-01" @default.
• W2026355265 modified "2023-10-18" @default.
• W2026355265 title "Purification of Cranin, a Laminin Binding Membrane Protein" @default.
• W2026355265 cites W1502661652 @default.
• W2026355265 cites W1527810981 @default.
• W2026355265 cites W1531251890 @default.
• W2026355265 cites W1559138834 @default.
• W2026355265 cites W1560897882 @default.
• W2026355265 cites W1564301159 @default.
• W2026355265 cites W1578270753 @default.
• W2026355265 cites W1585957774 @default.
• W2026355265 cites W1624352116 @default.
• W2026355265 cites W1641373107 @default.
• W2026355265 cites W1682371299 @default.
• W2026355265 cites W1968666078 @default.
• W2026355265 cites W1968957805 @default.
• W2026355265 cites W1969570221 @default.
• W2026355265 cites W1969584458 @default.
• W2026355265 cites W1980726194 @default.
• W2026355265 cites W1981850472 @default.
• W2026355265 cites W1990585109 @default.
• W2026355265 cites W2000720508 @default.
• W2026355265 cites W2006147388 @default.
• W2026355265 cites W2008115339 @default.
• W2026355265 cites W2015114304 @default.
• W2026355265 cites W2024666935 @default.
• W2026355265 cites W2029418672 @default.
• W2026355265 cites W2032616796 @default.
• W2026355265 cites W2038140607 @default.
• W2026355265 cites W2040418570 @default.
• W2026355265 cites W2044110769 @default.
• W2026355265 cites W2050087745 @default.
• W2026355265 cites W2057200625 @default.
• W2026355265 cites W2059367496 @default.
• W2026355265 cites W2062049077 @default.
• W2026355265 cites W2063622594 @default.
• W2026355265 cites W2066011643 @default.
• W2026355265 cites W2067456678 @default.
• W2026355265 cites W2071870745 @default.
• W2026355265 cites W2075939418 @default.
• W2026355265 cites W2080780289 @default.
• W2026355265 cites W2087362044 @default.
• W2026355265 cites W2091285643 @default.
• W2026355265 cites W2091677322 @default.
• W2026355265 cites W2092117657 @default.
• W2026355265 cites W2094107328 @default.
• W2026355265 cites W2105232838 @default.
• W2026355265 cites W2106473403 @default.
• W2026355265 cites W2109073906 @default.
• W2026355265 cites W2136726626 @default.
• W2026355265 cites W2138894342 @default.
• W2026355265 cites W2181486330 @default.
• W2026355265 cites W2433861420 @default.
• W2026355265 cites W2576742884 @default.
• W2026355265 doi "https://doi.org/10.1074/jbc.270.25.15425" @default.
• W2026355265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7797531" @default.
• W2026355265 hasPublicationYear "1995" @default.
• W2026355265 type Work @default.
• W2026355265 sameAs 2026355265 @default.
• W2026355265 citedByCount "137" @default.
• W2026355265 countsByYear W20263552652012 @default.
• W2026355265 countsByYear W20263552652013 @default.
• W2026355265 countsByYear W20263552652014 @default.
• W2026355265 countsByYear W20263552652015 @default.
• W2026355265 countsByYear W20263552652018 @default.
• W2026355265 countsByYear W20263552652019 @default.
• W2026355265 countsByYear W20263552652020 @default.
• W2026355265 crossrefType "journal-article" @default.
• W2026355265 hasAuthorship W2026355265A5033859037 @default.
• W2026355265 hasAuthorship W2026355265A5062980852 @default.
• W2026355265 hasBestOaLocation W20263552651 @default.
• W2026355265 hasConcept C108625454 @default.
• W2026355265 hasConcept C153911025 @default.
• W2026355265 hasConcept C189165786 @default.
• W2026355265 hasConcept C2778384963 @default.
• W2026355265 hasConcept C2779814568 @default.
• W2026355265 hasConcept C55493867 @default.
• W2026355265 hasConcept C86803240 @default.
• W2026355265 hasConcept C95444343 @default.
• W2026355265 hasConceptScore W2026355265C108625454 @default.
• W2026355265 hasConceptScore W2026355265C153911025 @default.
• W2026355265 hasConceptScore W2026355265C189165786 @default.
• W2026355265 hasConceptScore W2026355265C2778384963 @default.
• W2026355265 hasConceptScore W2026355265C2779814568 @default.
• W2026355265 hasConceptScore W2026355265C55493867 @default.
• W2026355265 hasConceptScore W2026355265C86803240 @default.
• W2026355265 hasConceptScore W2026355265C95444343 @default.
• W2026355265 hasIssue "25" @default.
• W2026355265 hasLocation W20263552651 @default.
• W2026355265 hasOpenAccess W2026355265 @default.
• W2026355265 hasPrimaryLocation W20263552651 @default.
• W2026355265 hasRelatedWork W1979452378 @default.
• W2026355265 hasRelatedWork W1983833766 @default.
• W2026355265 hasRelatedWork W2001236385 @default.

• next