Proteoglycans: structures and interactions.
- L. Kjellén, U. Lindahl
- Biology, ChemistryAnnual Review of Biochemistry
n, sulfation, L-iduronic acid, glycosam inoglycan-protei n in teractions, extracellular matrix.
Molecular diversity of heparan sulfate.
- J. Esko, U. Lindahl
- BiologyJournal of Clinical Investigation
- 15 July 2001
This Perspective aims to provide an overview of HS structure, function, and biosynthesis to set the stage for discussing the relationship between structure and function of these fascinating molecules and how altered HS biosynthesis and catabolism can lead to human disorders.
QSulf1 remodels the 6-O sulfation states of cell surface heparan sulfate proteoglycans to promote Wnt signaling
- Xingbin Ai, Anh-Tri Do, O. Lozynska, M. Kusche‐Gullberg, U. Lindahl, C. Emerson
- Biology, ChemistryJournal of Cell Biology
- 21 July 2003
A two-state “catch or present” model for QSulf1 regulation of Wnt signaling in which QSolf1 removes 6-O sulfates from HS chains to promote the formation of low affinity HS–Wnt complexes that can functionally interact with Frizzled receptors to initiate Wnt signal transduction is suggested.
Proteoglycans and Sulfated Glycosaminoglycans
- U. Lindahl, J. Couchman, K. Kimata, J. Esko
Regulated Diversity of Heparan Sulfate*
- U. Lindahl, M. Kusche‐Gullberg, L. Kjellén
- BiologyJournal of Biological Chemistry
- 25 September 1998
The evidence for regulated expression of specific domains in HS chains and its relation to selective protein binding is outlined and the current information on HS biosynthesis is considered, with the aim of understanding the mechanisms in control of generating specific saccharide sequences.
Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4.
- S. Guimond, M. Maccarana, B. Olwin, U. Lindahl, A. Rapraeger
- Biology, ChemistryJournal of Biological Chemistry
- 15 November 1993
It is concluded that specific saccharide sequences within heparan sulfate glycosaminoglycan chains favor the signaling by distinct members of the FGF family.
A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis.
- K. Lidholt, J. L. Weinke, J. Esko
- BiologyProceedings of the National Academy of Sciences…
- 15 March 1992
Findings indicate that the pgsD locus may represent a gene involved in the coordinate control of glycosaminoglycan formation in Chinese hamster ovary cells, and is associated with heparan sulfate synthesis.
Interactions between heparan sulfate and proteins: the concept of specificity
- J. Kreuger, D. Spillmann, Jin-ping Li, U. Lindahl
- BiologyJournal of Cell Biology
- 31 July 2006
This review summarizes recent biochemical and genetic information that sheds new light on the nature of HS–protein binding that appears to depend more on the overall organization of HS domains than on their fine structure.
Defining the Interleukin-8-binding Domain of Heparan Sulfate*
- D. Spillmann, D. Witt, U. Lindahl
- Chemistry, BiologyJournal of Biological Chemistry
- 19 June 1998
The affinity of a monomeric interleukin-8 molecule for heparin/heparin sulfate is too weak to allow binding at physiological ionic strength, whereas the dimeric form of the protein mediates binding to two sulfated domains of heparan sulfate.
Heparan sulfate: a piece of information
- M. Salmivirta, K. Lidholt, U. Lindahl
- Biology, ChemistryThe FASEB Journal
- 1 September 1996
The sulfated glycosaminoglycans, heparan sulfate and heparin, are increasingly implicated in cell‐biological processes such as cytokine action, cell adhesion, and regulation of enzymic catalysis.…