Affinity and kinetics of different heparins binding to P- and L-selectin.

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Simonis D, Christ K, Alban S, Bendas G

Affinity and kinetics of different heparins binding to P- and L-selectin.

Semin Thromb Hemost. 2007 Jul;33(5):534-9.

PubMed ID

17629851 [ View in PubMed

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Abstract

Selectins are adhesion receptors that participate in inflammation and tumor cell metastasis. The anti-inflammatory and antimetastatic activities of heparins have been related partly to their ability to interact with P- and L-selectin. The recent findings that various heparins differ in antimetastatic activity were explained by differences in their P- and L-selectin binding ability. To obtain data to illustrate the binding characteristics, we detected for the first time the binding kinetics and affinity of the two low molecular weight heparins (LMWHs) enoxaparin and nadroparin, and of the unfractionated heparin Liquemin N to P- and L-selectin using a quartz crystal microbalance biosensor. Enoxaparin and nadroparin behave nearly identical in their binding affinity to both P-selectin ( KD 4.60 x 10 (- 6) M versus 7.61 x 10 (- 6) M) and L-selectin ( KD 2.01 x 10 (- 6) M versus 2.84 x 10 (- 6) M). Liquemin N displayed slightly higher affinities to both selectins ( KD 6.07 x 10 (- 7) M versus 1.07 x 10 (- 7) M). The differences are caused by a higher association rate compared with that of the LMWHs. These data support recent findings of antimetastatic activities, but illustrate that the intrinsic selectin binding does not entirely reflect the antimetastatic activities in vivo.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Heparin	P-selectin	Protein	Humans	Unknown	Inhibitor	Details
Nadroparin	P-selectin	Protein	Humans	Unknown	Inhibitor	Details