Adhesion of Human Neutrophils to Fibronectin Is Inhibited by Comaruman, Pectin of Marsh Cinquefoil Comarum palustre L., and by Its Fragments

---

S. V. Popov, R. G. Ovodova, G. Yu. Popova, I. R. Nikitina, and Yu. S. Ovodov^*

Institute of Physiology, Komi Science Center, The Urals Branch of the Russian Academy of Sciences, ul. Pervomaiskaya 50, 167982 Syktyvkar, Russia; fax: 7 (8212) 241-001; E-mail: ovoys@physiol.komisc.ru

^* To whom correspondence should be addressed.

Received July 22, 2004; Revision received August 30, 2004

---

Earlier, we detected antiinflammatory action of comaruman, pectin of the marsh cinquefoil Comarum palustre L. This effect can be explained by new data concerning inhibition of adhesion of human neutrophils to fibronectin by comaruman and its fragments. The galacturonan backbone fragment of molecular mass >10 kD appears to be the active region of the comaruman macromolecule. Comaruman CP (50-200 µg/ml) was found to decrease adhesion of neutrophils stimulated by phorbol 12-myristate 13-acetate (PMA, 1.625 µM) and by dithiothreitol (DTT, 0.5 mM). The fragments of comaruman CP-H (100 kD), CP-H1 (10-50 kD), and CP-H2 (100 kD) obtained by acidic hydrolysis and representing regions of linear polygalacturonan are shown to inhibit neutrophil adhesion more than the crude pectin. A fragment CP-E (<10 kD) obtained using pectinolysis and representing a branched region of the comaruman macromolecule failed to influence cell adhesion. The parent comaruman CP as well as fragments of its polygalacturonan backbone diminish PMA-initiated generation of oxygen radicals in neutrophils.

---

KEY WORDS: pectins, Comarum palustre, comaruman, linear polygalacturonan, neutrophil adhesion, fibronectin

---