Jeltraxin, a frog egg jelly glycoprotein, has calcium-dependent lectin properties and is related to human serum pentraxins CRP and SAP.

Abstract:

:The egg jelly that encapsulates amphibian eggs is essential for fertilization, but its molecular composition and roles remain largely unknown. We identified a calcium-dependent lectin from the pentraxin superfamily in the egg jelly coat from the South American burrowing frog, Lepidobatrachus laevis. This lectin, jeltraxin, was related to the host-response acute phase serum proteins C-reactive P component (CRP) and serum amyloid P component (SAP). The amino acid sequence of jeltraxin is 44% identical to that of Xenopus laevis CRP, 31-35% identical to those of mammalian CRP and SAP, and 21-27% identical to those of the large fusion pentraxins. Expression of jeltraxin mRNA was restricted to the oviduct, which distinguishes it as the first serum-related pentraxin not expressed in the liver. Purified jeltraxin was previously shown to exist in an oligomeric complex of approximately 250 kDa comprised of self-associating subunits. We have demonstrated by MALDI-TOF that this configuration is due to a decameric complex of 27.7 kDa subunits. Biotinylated jeltraxin bound to the high-molecular mass components of the egg jelly in a calcium-dependent manner with specificity for beta-galactose residues. On the basis of homology modeling, we predict that jeltraxin will coordinate two calcium ions. The function of jeltraxin will likely be related to its calcium-dependent lectin properties.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Peavy TR,Hernandez C,Carroll EJ Jr

doi

10.1021/bi035314o

subject

Has Abstract

pub_date

2003-11-11 00:00:00

pages

12761-9

issue

44

eissn

0006-2960

issn

1520-4995

journal_volume

42

pub_type

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