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Blood, Vol. 92 No. 6 (September 15), 1998:
pp. 1870-1877
RAPID COMMUNICATION
Increased Susceptibility in Hp Knockout Mice During Acute
Hemolysis
Sai-Kiang Lim,
Hongkyun Kim,
Shen Kiat Lim,
Azhar bin Ali,
Yew
Koon Lim,
Yanping Wang,
Siew Meng Chong,
Frank Costantini, and
Heinz Baumman
From the Cardiovascular Research Institute, National University
Medical Institutes, and the Honors Program in Biochemistry, The
National University of Singapore, Singapore; the Department of
Molecular and Cellular Biology, Roswell Park Cancer Institute, Buffalo,
NY; the Department of Pathology, National University Hospital,
Singapore; and the Department of Genetics and Development, Columbia
University, New York, NY.
Haptoglobin, a conserved plasma glycoprotein, forms very stable
soluble complexes with free plasma hemoglobin. Hemoglobin binding by
haptoglobin is thought to be important in the rapid hepatic clearance
of hemoglobin from the plasma and in the inhibition of glomerular
filtration of hemoglobin. To evaluate these functions, Haptoglobin knockout ( /) mice were created. These mice
were viable but had a small, significant reduction in postnatal
viability. Contrary to popular belief, the lack of haptoglobin did not
impair clearance of free plasma hemoglobin in / mice. Induction
of severe hemolysis by phenylhydrazine caused extensive hemoglobin precipitation in the renal tubular cells of both / and +/+
mice, with death occurring in 55% of / mice and in 18% of
+/+ mice. In general, phenylhydrazine-treated / mice suffered
greater tissue damage, as evidenced by the induction of hepatic acute phase response resulting in increased plasma alpha 1-acid glycoprotein (AGP) levels. Among / and +/+ mice that survived, /
mice tend to suffer greater oxidative damage and failed to repair or
regenerate damaged renal tissues, as indicated by their higher plasma
malonaldehyde (MDA) and 4-hydroxy-2(E)-nonenal (HNE) levels and lower
mitotic indices in their kidneys, respectively. This study suggested
that a physiologically important role of hemoglobin-haptoglobin complex formation is the amelioration of tissue damages by hemoglobin-driven lipid peroxidation.
© 1998 by The American Society of Hematology.
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