Heparan sulfate domains

Thompson, S. M., M. G. Connell, D. G. Femig, G. B. Ten Dam, T. H. van Kuppevelt, J. E. Turnbull, E. C. Jesudason, and P. D. Losty. 2007. Novel phage display antibodies identify distinct heparan sulfate domains in developing mammalian lung. Pediatr. Surg. Int. 23 411-7. 

E. Feyzi, F. Lustig, G. Fager, D. Spillmann, U. Lindahl, M. Salmivirta, Characterization of heparin and heparan sulfate domains binding to the long splice variant of platelet-derived growth factor A chain. J. Biol Chem. 1997 272, 5518-24. 

Type I collagen can interact with various other molecules in the extracellular matrix and on the cell surface. Cell receptors of type I collagen have been identified and include the heterodimeric integrin family receptors, ctl, 0 2, olO, and ol 1, especially o2/3l, the receptor tyrosine kinase discoidin domain receptor (DDR), and the heparan sulfate membrane proteoglycan syndecan family... 

FIGURE 7-28 Four types of protein interactions with S domains of heparan sulfate. 

The high density of negative charges in heparan sulfate brings positively charged molecules of lipoprotein lipase into the vicinity and holds them by electrostatic interactions as well as by sequence-specific interactions with S domains. Such interactions are also central in the first step in the entry of certain viruses (such as herpes simplex viruses HSV-1 and HSV-2) into cells. 

Review of the chemistry and biology of high-sulfate domains in heparan sulfate. 

Fragment 3 (Mr 50K) possessed / structure, appeared globular in electron micrographs, and was found to bind to heparin. It was assumed to be the globular region at the end of the long arm of laminin. This site is one of the main heparin- and heparan sulfate-binding domains in laminin (Ott et al., 1982). 

Already in 1965, Ryser and Hancock provided evidence that histones and polyamino acids could greatly enhance albumin uptake by cultured tumor cells (6). More recently, several polybasic peptides (so-called protein transduction domains, PTDs or cell-penetrating peptides, CPPs) have been shown to efficiently mediate uptake of nucleic acids, bioactive peptides, phage particles, and liposomes into a wide variety of mammalian cells. The initially proposed ability of CPPs to penetrate plasma membranes via a temperature-independent, non-endocytotic pathway was later shown to be a fixation artifact, and it is currently widely accepted that CPP-mediated macromolecular delivery follows energy-dependent endocytotic pathways that in most cases depend on the expression of cell-surface heparan sulfate proteoglycans (HSPGs) (7). 

Cladera J, Martin I, O Shea P. The fusion domain of HIV gp41 interacts specifically with heparan sulfate on the T-lymphocyte cell surface. EMBO J. 2001 20 19-26. 

In the case of 0-fucose, there are two types of 0-fucosyltransferase (EC 2.4.1.221), specific for either EGF or TSR domains, whose action is followed by, respectively, the 1,3-iV-acetylglu-cosaminyltransferase known as Fringe or a /31,3-glucosyltransferase [143]. In mammals, there are two polypeptide-modifying xylosyltransferases (EC 2.4.2.26) which are the first of a series of glycosyltransferases required for the synthesis of the chondroitin and heparan sulfates [144]. The first residue of 0-mannosyl glycans is transferred by a heterodimeric peptide-O-mannosyltransferase in mammals [145], whereas in yeast there are a number of... 

Lortat-Jacob H, Grosdidier A, Imberty A. Structural diversity of heparan sulfate binding domains in... 

Spillmann, D., Witt, D., and Lindahl, U. (1998). Defining the interleukin-8-binding domain of heparan sulfate. J. Biol. Chem. 273, 15487-15493. 

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