The Glycocode: Translating Heparan Sulfate Fine Structure into Developmental Function

Author(s):  
Adam B. Cadwallader ◽  
H. Joseph Yost
1994 ◽  
Vol 269 (18) ◽  
pp. 13100-13106
Author(s):  
R.D. Sanderson ◽  
J.E. Turnbull ◽  
J.T. Gallagher ◽  
A.D. Lander

2006 ◽  
Vol 174 (3) ◽  
pp. 323-327 ◽  
Author(s):  
Johan Kreuger ◽  
Dorothe Spillmann ◽  
Jin-ping Li ◽  
Ulf Lindahl

Proteoglycan (PG) coreceptors carry heparan sulfate (HS) chains that mediate interactions with growth factors, morphogens, and receptors. Thus, PGs modulate fundamental processes such as cell survival, division, adhesion, migration, and differentiation. This review summarizes recent biochemical and genetic information that sheds new light on the nature of HS–protein binding. Unexpectedly, many interactions appear to depend more on the overall organization of HS domains than on their fine structure.


2014 ◽  
Vol 192 (5) ◽  
pp. 2133-2142 ◽  
Author(s):  
Xin Yin ◽  
Scott C. Johns ◽  
Daniel Kim ◽  
Zbigniew Mikulski ◽  
Catherina L. Salanga ◽  
...  

2003 ◽  
Vol 279 (7) ◽  
pp. 5053-5054 ◽  
Author(s):  
Balagurunathan Kuberan ◽  
Miroslaw Lech ◽  
Jimo Borjigin ◽  
Robert D. Rosenberg

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Brent Ferguson ◽  
Michael Schlicht ◽  
Alexandra Migdal ◽  
Payal Shaw ◽  
Milton W. Datta ◽  
...  

1994 ◽  
Vol 269 (29) ◽  
pp. 18881-18890 ◽  
Author(s):  
M. Kato ◽  
H. Wang ◽  
M. Bernfield ◽  
J.T. Gallagher ◽  
J.E. Turnbull

Author(s):  
W. H. Zucker ◽  
R. G. Mason

Platelet adhesion initiates platelet aggregation and is an important component of the hemostatic process. Since the development of a new form of collagen as a topical hemostatic agent is of both basic and clinical interest, an ultrastructural and hematologic study of the interaction of platelets with the microcrystalline collagen preparation was undertaken.In this study, whole blood anticoagulated with EDTA was used in order to inhibit aggregation and permit study of platelet adhesion to collagen as an isolated event. The microcrystalline collagen was prepared from bovine dermal corium; milling was with sharp blades. The preparation consists of partial hydrochloric acid amine collagen salts and retains much of the fibrillar morphology of native collagen.


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