Skip to main content
PMC home page
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1979 Feb;63(2):318–325. doi: 10.1172/JCI109305

Tissue Distribution of Human α1-Microglobulin

Kimiteru Takagi 1,2, Kohjin Kin 1,2, Yoshihisa Itoh 1,2, Tadashi Kawai 1,2, Tadashi Kasahara 1,2, Toshihiko Shimoda 1,2, Toshio Shikata 1,2
PMCID: PMC371955  PMID: 85635

Abstract

Human α1-microglobulin was isolated from the urine of patients with tubular proteinuria, and its molecular weight was established by sodium dodecyl sulfate-polyacrylamide gel electrophoresis at 33,000 daltons. The carbohydrate content was 21.7%. Anti-α1-microglobulin serum was prepared and observed to react monospecifically in gel diffusion to purified α1-microglobulin, as well as to normal human serum and urine. Sera from the domestic chicken, mouse, rat, rabbit, dog, calf, cow, goat, sheep, and horse, however, did not react to anti-α1-microglobulin serum in immunodiffusion. The lymphocyte culture supernate was found to contain α1-microglobulin. Both thymus-derived(T)- and bone marrow-derived(B)-lymphocyte culture media clearly displayed a specific precipitin line against anti-α1-microglobulin serum when tested with the Ouchterlony immunodiffusion method. The tissue distribution of α1-microglobulin was studied under immunofluorescence, and a positive staining was recognized on the lymphocyte surface. Identical staining patterns were noted on both T and B lymphocytes, though B lymphocytes took a more intense stain. It would thus seem quite possible that lymphocytes are the primary source of α1-microglobulin and that this is filtered through the glomerular basement membrane and partly reabsorbed by the renal tubules. This, then, would suggest the possibility that α1-microglobulin shares some immunological role in vivo with lymphocytes and(or) is one of the membrane proteins of lymphocytes.

Full text

PDF
322

Images in this article

322Image
on p.322
322Image
on p.322
320Image
on p.320
321Image
on p.321
323Image
on p.323

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Becker W. Determination of antisera titres ing the single radial immunodiffusion method. Immunochemistry. 1969 Jul;6(4):539–546. doi: 10.1016/0019-2791(69)90193-1. [DOI] [PubMed] [Google Scholar]
  2. Berggård I., Bearn A. G. Isolation and properties of a low molecular weight beta-2-globulin occurring in human biological fluids. J Biol Chem. 1968 Aug 10;243(15):4095–4103. [PubMed] [Google Scholar]
  3. Bernier I., Dautigny A., Jollès J., Colombani J., Jollès P. Molecular data on urinary glycoproteins with human leucocyte antigen (HLA) activity. Biochim Biophys Acta. 1978 Apr 26;533(2):355–361. doi: 10.1016/0005-2795(78)90381-1. [DOI] [PubMed] [Google Scholar]
  4. Bismuth A., Neauport-Sautes C., Kourilsky F. M., Manuel Y., Greenland T., Silvestre D. Distribution and mobility of beta 2-microglobulin on the human lymphocyte membrane: immunofluorescence and immunoferritin studies. J Immunol. 1974 Jun;112(6):2036–2046. [PubMed] [Google Scholar]
  5. COONS A. H., KAPLAN M. H. Localization of antigen in tissue cells; improvements in a method for the detection of antigen by means of fluorescent antibody. J Exp Med. 1950 Jan 1;91(1):1–13. doi: 10.1084/jem.91.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ekström B., Berggård I. Human alpha1-microglobulin. Purification procedure, chemical and physiochemical properties. J Biol Chem. 1977 Nov 25;252(22):8048–8057. [PubMed] [Google Scholar]
  7. Ekström B., Peterson P. A., Berggård I. A urinary and plasma alpha1-glycoprotein of low molecular weight: isolation and some properties. Biochem Biophys Res Commun. 1975 Aug 18;65(4):1427–1433. doi: 10.1016/s0006-291x(75)80388-3. [DOI] [PubMed] [Google Scholar]
  8. Forsum U. Characterization of FITC-labelled F(ab')2 fragments of IgG and a rapid technique for the separation of optimally labelled fragments. J Immunol Methods. 1973 Jan;2(2):183–195. doi: 10.1016/0022-1759(73)90015-x. [DOI] [PubMed] [Google Scholar]
  9. Frangione B., Franklin E. C., Grubb A., Tejler L. The amino-terminal sequence of human protein HC. FEBS Lett. 1976 Nov;70(1):239–240. doi: 10.1016/0014-5793(76)80765-x. [DOI] [PubMed] [Google Scholar]
  10. GRABAR P., WILLIAMS C. A. Méthode permettant l'étude conjuguée des proprietés électrophorétiques et immunochimiques d'un mélange de protéines; application au sérum sanguin. Biochim Biophys Acta. 1953 Jan;10(1):193–194. doi: 10.1016/0006-3002(53)90233-9. [DOI] [PubMed] [Google Scholar]
  11. HAMASHIMA Y., HARTER J. G., COONS A. H. THE LOCALIZATION OF ALBUMIN AND FIBRINOGEN IN HUMAN LIVER CELLS. J Cell Biol. 1964 Feb;20:271–279. doi: 10.1083/jcb.20.2.271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hütteroth T. H., Cleve H., Litwin S. D., Poulik M. D. The relationship between 2 -microglobulin and immunoglobulin in cultured human lymphoid cell lines. J Exp Med. 1973 Mar 1;137(3):838–843. doi: 10.1084/jem.137.3.838. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Pearlstein E., Turesson I., Tejler L., Grubb A. O. Expression of protein HC on the plasma membrane of different human cell types. J Immunol. 1977 Sep;119(3):824–829. [PubMed] [Google Scholar]
  15. Poulik M. D., Bernoco M., Bernoco D., Ceppellinni R. Aggregation of HL-A Antigens at the Lymphocyte Surface Induced by Antiserum to beta2-Microglobulin. Science. 1973 Dec 28;182(4119):1352–1355. doi: 10.1126/science.182.4119.1352. [DOI] [PubMed] [Google Scholar]
  16. Poulik M. D., Bloom A. D. Beta 2 -microglobulin production and secretion by lymphocytes in culture. J Immunol. 1973 May;110(5):1430–1433. [PubMed] [Google Scholar]
  17. Schubert D. Immunoglobulin biosynthesis. IV. Carbohydrate attachment to immunoglobulin subunits. J Mol Biol. 1970 Jul 28;51(2):287–301. doi: 10.1016/0022-2836(70)90143-9. [DOI] [PubMed] [Google Scholar]
  18. Strober W., Waldmann T. A. The role of the kidney in the metabolism of plasma proteins. Nephron. 1974;13(1):35–66. doi: 10.1159/000180368. [DOI] [PubMed] [Google Scholar]
  19. Svensson L., Ravnskov U. alpha1-Microglobulin, a new low molecular weight plasma protein. Clin Chim Acta. 1976 Dec;73(3):415–422. doi: 10.1016/0009-8981(76)90142-x. [DOI] [PubMed] [Google Scholar]
  20. Tejler L., Grubb A. O. A complex-forming glycoprotein heterogeneous in charge and present in human plasma, urine, and cerebrospinal fluid. Biochim Biophys Acta. 1976 Jul 19;439(1):82–94. doi: 10.1016/0005-2795(76)90164-1. [DOI] [PubMed] [Google Scholar]
  21. Tejler L., Grubb A. O., Turesson I. Immunofluorescent demonstration of the presence of protein HC on the surface of human lymphocytes. Acta Med Scand. 1976;199(5):425–427. doi: 10.1111/j.0954-6820.1976.tb06759.x. [DOI] [PubMed] [Google Scholar]
  22. Tung J. S., Knight C. A. Relative importance of some factors affecting the electrophoretic migration of proteins in sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem. 1972 Jul;48(1):153–163. doi: 10.1016/0003-2697(72)90179-0. [DOI] [PubMed] [Google Scholar]
  23. WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [PubMed] [Google Scholar]
  24. Waldmann T. A., Strober W., Mogielnicki R. P. The renal handling of low molecular weight proteins. II. Disorders of serum protein catabolism in patients with tubular proteinuria, the nephrotic syndrome, or uremia. J Clin Invest. 1972 Aug;51(8):2162–2174. doi: 10.1172/JCI107023. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  26. Wilde C. E., 3rd, Koshland M. E. Molecular size and shape of the J chain from polymeric immunoglobulins. Biochemistry. 1973 Aug 14;12(17):3218–3224. doi: 10.1021/bi00741a012. [DOI] [PubMed] [Google Scholar]
  27. Wochner R. D., Strober W., Waldmann T. A. The role of the kidney in the catabolism of Bence Jones proteins and immunoglobulin fragments. J Exp Med. 1967 Aug 1;126(2):207–221. doi: 10.1084/jem.126.2.207. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES