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Hemopexin, the heme-binding serum β-glycoprotein

  • Editorials
  • Published:
Ricerca in clinica e in laboratorio

Summary

Current information on physicochemical and biological properties of the hemopexin molecule is presented. The protein consists of a single polypeptide chain of 57,000 daltons, is about 20 % carbohydrate, and binds equimolar amounts of porphyrins and metalloporphyrins. Genetic polymorphism has only been found for rabbits and pigs. Serum hemopexin levels in man, after 1 year of age, range from 500 to 1,000 µg/ml, and in rabbits from 300 to 600 µg/ml. Hemopexin, unlike haptoglobin, in humans is not an acute phase reactant. Hemopexin levels are reduced as those of heme rise. The concentration of this protein is, therefore, a good monitor for assessment of severity of intravascular hemolysis. The levels are somewhat lowered in patients with certain porphyrias and are elevated in diabetes mellitus and various forms of cancer. Metabolic studies with125I-hemopexin in humans show a turnover rate of about 7 mg/kg/day, a T/2 of 8 days, and a fractional catabolic rate of 24 % of the plasma pool/day somewhat increased in erythropoietic protoporphyria and sickle cell disease. This accelerated catabolism is not fully compensated for by an increased synthesis which may explain the decreased hemopexin levels. In rabbits, the T/2 of125I-hemopexin is about 35 hrs. The T/2 in man and rabbits is drastically reduced upon i.v. heme injection. The heme is delivered by hemopexin to the parenchymal liver cells. This function is abolished when the hemopexin molecules are photo-inactivatedin vitro. In experimental animals, carcinogens such as 3-methylcholanthrene and 3,4-benzpyrene as well as porphyrinogenic agents cause hemopexin levels to rise. Protein synthesis inhibitors prevent this rise in hemopexin concentration, therefore attributable tode novo synthesis, which takes place exclusively in the liver. Presently under investigation is whether heme entering the hepatocyte is entirely predestined for degradation, and what the interrelationship of this plasma heme scavenger is to the heme-proteins of the liver which are involved in the detoxification of environmental poisons or carcinogens.

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  1. Department of Biochemistry, Scripps Clinic and Research Foundation, 476 Prospect Street, 92037, La Jolla, Calif., USA

    Ursula Muller-Eberhard & Ham Heng Liem

  2. Department of Pediatrics — Division of Pediatric Hematology, University of California at San Diego, 92037, La Jolla, Calif.

    Ursula Muller-Eberhard & Ham Heng Liem

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  1. Ursula Muller-Eberhard
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  2. Ham Heng Liem
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Supported by a Career Development Award (5-K3-AM-16,923) from the National Institute of Arthritis and Metabolic Diseases, and by research grants from the National Heart Institute (HE-08660) and the Institute of Child Health and Human Development (HD-04445), as well as from the San Diego County Heart Association (No. 83).

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Muller-Eberhard, U., Liem, H.H. Hemopexin, the heme-binding serum β-glycoprotein. La Ricerca in Clin. Lab. 5, 275–291 (1975). https://doi.org/10.1007/BF02910154

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