Interaction of smooth muscle calponin with phospholipids.

Abstract:

:Analyzing the primary structure we predicted that calponin may interact with phospholipids. In order to check this suggestion we investigated the interaction of calponin with phospholipids by ultracentrifugation, light scattering, vesicles leakage and differential scanning calorimetry. In agreement with our prediction calponin interacts with acidic phospholipids and the phospholipid-binding site was located in the short (13 kDa) N-terminal chymotryptic peptide of calponin. The apparent dissociation constant of calponin-phospholipids complex was less than 0.2 microM and calmodulin competes with phospholipids for calponin binding. Although the interaction of calponin with phospholipids decreases at high ionic strength, calponin binds phospholipids even in the presence of 100-150 mM of the salt. Under certain conditions calponin induced leakage of phospholipid vesicles and affected the cooperativity of lipid phase transition. It is concluded that both electrostatic and hydrophobic interactions provide for calponin-phospholipid complex formation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Bogatcheva NV,Gusev NB

doi

10.1016/0014-5793(95)00868-a

subject

Has Abstract

pub_date

1995-09-04 00:00:00

pages

123-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)00868-A

journal_volume

371

pub_type

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