Heparin-Binding Domains in Vascular Biology 来自 Semantic Scholar 喜欢 0 阅读量: 53 作者:EM Muñoz,RJ Linhardt 摘要: Heparin is a major anticoagulant with activity mediated primarily through its interaction with antithrombin (AT). Heparan sulfate (HS), structurally related to heparin, binds a ...
We thank Kristin Johnson (Vascular Biology Program, Boston Children's Hospital) for assistance in generating the figures. All authors reviewed the article and were involved in the final approval of the version to be published. Supplemental Data Download: Download XML file (305B) Data Profile. Ref...
Here, we show that multiple laminin isoforms promiscuously bind to growth factors (GFs) with high affinity, through their heparin-binding domains (HBDs) located in the α chain laminin-type G (LG) domains. These domains also bind to syndecan cell-surface receptors, promoting attachment of ...
Some of them are recovered in many bands which reflect either degradation, multimerization or aggregation, as already reported for other egg proteins including ovalbumin or avidin11,12. Protein binding to heparin (negatively charged glycosaminoglycan) does not depend on protein pI as attested in Tabl...
However, a common property of these heterogeneous N-terminal domains is the ability to bind fibrinogen. When skin sections were incubated with gold-labeled human fibrinogen, no colocalization was observed with bacterial surfaces (Figure 4d). The results suggest that the N-terminal portion of the ...
The transmembrane form of HB-EGF is synthesized by many cell types as a 208-amino acid transmembrane precursor (tm-HB-EGF) containing EGF, heparin-binding, transmembrane, and cytoplasmic domains. The extracellular domain can be released as a 12- to 22-kDa soluble form of HB-EGF (sol-HB-EG...
CXCL1/MGSA is a novel glycosaminoglycan (GAG)-binding chemokine: Structural evidence for two distinct non-overlapping binding domains. J. Biol. Chem. 2016, 291, 4247–4255. [CrossRef] [PubMed] 49. Sepuru, K.M.; Nagarajan, B.; Desai, U.R.; Rajarathnam, K. Molecular basis of ...
All members of the Rspo family contain an N-terminal signal peptide (SP), two furin-repeat domains that are rich in cysteine residues (FR1 and FR2; also called cysteine-rich domain, CRD), one thrombospondin type 1 domain (TSR1), and a C-terminal region enriched with positively charged ...