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Low spring constant regulates P-selectin-PSGL-1 bond rupture.


ABSTRACT: Forced dissociation of selectin-ligand bonds is crucial to such biological processes as leukocyte recruitment, thrombosis formation, and tumor metastasis. Although the bond rupture has been well known at high loading rate r(f) (>or=10(2) pN/s), defined as the product of spring constant k and retract velocity v, how the low r(f) (<10(2) pN/s) or the low k regulates the bond dissociation remains unclear. Here an optical trap assay was used to quantify the bond rupture at r(f)

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC2586549 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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Low spring constant regulates P-selectin-PSGL-1 bond rupture.

Zhang Yan Y   Sun Ganyun G   Lü Shouqin S   Li Ning N   Long Mian M  

Biophysical journal 20080829 11


Forced dissociation of selectin-ligand bonds is crucial to such biological processes as leukocyte recruitment, thrombosis formation, and tumor metastasis. Although the bond rupture has been well known at high loading rate r(f) (>or=10(2) pN/s), defined as the product of spring constant k and retract velocity v, how the low r(f) (<10(2) pN/s) or the low k regulates the bond dissociation remains unclear. Here an optical trap assay was used to quantify the bond rupture at r(f) <or= 20 pN/s with low  ...[more]

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