Fibronectin interacts with Clq, a subcomponent of the first component of complement.

Abstract:

:Human Clq, a subcomponent of the first component of complement interacts with human fibronectin. Using ELISA methodology fixation of Clq to solid phase fibronectin, as well as fibronectin to solid phase Clq has been demonstrated. Cl in its native macromolecular form displays little reactivity for fibronectin, nor does Cl reconstituted from Clq, Clr and Cls in the presence of Ca2+ ions. Heating of Clq above its thermal transition temperature (51 degrees C) induces an increased binding capacity for fibronectin. On the other hand, a mixture of the dissociated A, B and C chains of Clq is less active than native Clq. The binding of fibronectin appears to be mediated by the A chain. Studies with Clq deprived of its globular parts by peptic digestion indicate that the collagen-like regions of Clq are involved in fibronectin binding. In contrast, collagenase treatment of Clq abrogates its fibronectin binding capacity.

journal_name

Immunol Lett

journal_title

Immunology letters

authors

Isliker H,Bing DH,Lahan J,Hynes RO

doi

10.1016/0165-2478(82)90075-x

subject

Has Abstract

pub_date

1982-01-01 00:00:00

pages

39-43

issue

1

eissn

0165-2478

issn

1879-0542

pii

0165-2478(82)90075-X

journal_volume

4

pub_type

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