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. 1988 Apr 1;251(1):171–174. doi: 10.1042/bj2510171

67 k calcimedin (67 kDa) is distinct from p67 calelectrin and lymphocyte 68 kDa Ca2+-binding protein.

S S Morse 1, P B Moore 1
PMCID: PMC1148979  PMID: 2968790

Abstract

The 67 k calcimedin is a Ca2+-binding protein present in both muscle cells and peritoneal macrophages. Many tissues, including lymphoid tissues, liver and lymphocytes, have been shown to contain Ca2+-binding proteins of similar molecular size, such as the p67(67 kDa) calelectrin or the 68 kDa lymphocyte protein. We have tested affinity-purified antibodies raised to the smooth-muscle 67 k calcimedin in these several tissues and here report that the 67 k calcimedin is not detectable in liver, thymus, spleen or thymic lymphocytes. These findings support recent biochemical evidence, discussed here, suggesting that the 67 k calcimedin is a protein different from calelectrin and the 68 kDa lymphocyte protein. The more limited tissue distribution of the 67 k calcimedin, which includes muscle and macrophages, suggests that the 67 k calcimedin may function in Ca2+-mediated events special to these cell types. The affinity-purified antibodies to the 67 k calcimedin will be useful in obtaining information concerning the special roles of this Ca2+-binding protein in these cells.

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Selected References

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  1. Davies A. A., Crumpton M. J. Identification of calcium-binding proteins associated with the lymphocyte plasma membrane. Biochem Biophys Res Commun. 1985 Apr 30;128(2):571–577. doi: 10.1016/0006-291x(85)90084-1. [DOI] [PubMed] [Google Scholar]
  2. Fauvel J., Vicendo P., Roques V., Ragab-Thomas J., Granier C., Vilgrain I., Chambaz E., Rochat H., Chap H., Douste-Blazy L. Isolation of two 67 kDa calcium-binding proteins from pig lung differing in affinity for phospholipids and in anti-phospholipase A2 activity. FEBS Lett. 1987 Sep 14;221(2):397–402. doi: 10.1016/0014-5793(87)80963-8. [DOI] [PubMed] [Google Scholar]
  3. Geisow M., Childs J., Dash B., Harris A., Panayotou G., Südhof T., Walker J. H. Cellular distribution of three mammalian Ca2+-binding proteins related to Torpedo calelectrin. EMBO J. 1984 Dec 1;3(12):2969–2974. doi: 10.1002/j.1460-2075.1984.tb02242.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Mathew J. K., Krolak J. M., Dedman J. R. Calcimedins: purification and characterization from chicken gizzard and rat and bovine livers. J Cell Biochem. 1986;32(3):223–234. doi: 10.1002/jcb.240320309. [DOI] [PubMed] [Google Scholar]
  5. Moore P. B. 67 kDa calcimedin, a new Ca2+-binding protein. Biochem J. 1986 Aug 15;238(1):49–54. doi: 10.1042/bj2380049. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Moore P. B., Dedman J. R. Calcium-dependent protein binding to phenothiazine columns. J Biol Chem. 1982 Aug 25;257(16):9663–9667. [PubMed] [Google Scholar]
  7. Moore P. B. Isolation and purification of an antibody to 67-KD calcimedin. J Histochem Cytochem. 1988 Feb;36(2):185–192. doi: 10.1177/36.2.2961799. [DOI] [PubMed] [Google Scholar]
  8. Moore P. B., Kraus-Friedmann N., Dedman J. R. Unique calcium-dependent hydrophobic binding proteins: possible independent mediators of intracellular calcium distinct from calmodulin. J Cell Sci. 1984 Dec;72:121–133. doi: 10.1242/jcs.72.1.121. [DOI] [PubMed] [Google Scholar]
  9. Morse S. S., Moore P. B. Effect of nifedipine on 67k calcimedin in cultured macrophages and smooth muscle cells. Biochem Biophys Res Commun. 1987 Jun 15;145(2):726–732. doi: 10.1016/0006-291x(87)91025-4. [DOI] [PubMed] [Google Scholar]
  10. Owens R. J., Crumpton M. J. Isolation and characterization of a novel 68,000-Mr Ca2+-binding protein of lymphocyte plasma membrane. Biochem J. 1984 Apr 1;219(1):309–316. doi: 10.1042/bj2190309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Rhoads A. R., Lulla M., Moore P. B., Jackson C. E. Characterization of calcium-dependent membrane binding proteins of brain cortex. Biochem J. 1985 Aug 1;229(3):587–593. doi: 10.1042/bj2290587. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Smith V. L., Dedman J. R. An immunological comparison of several novel calcium-binding proteins. J Biol Chem. 1986 Dec 5;261(34):15815–15818. [PubMed] [Google Scholar]
  13. Sohar I., Bird J. W., Moore P. B. Calcium-dependent proteolysis of calcium-binding proteins. Biochem Biophys Res Commun. 1986 Feb 13;134(3):1269–1275. doi: 10.1016/0006-291x(86)90387-6. [DOI] [PubMed] [Google Scholar]
  14. Südhof T. C. Calelectrins are a ubiquitous family of Ca2+-binding proteins purified by Ca2+-dependent hydrophobic affinity chromatography by a mechanism distinct from that of calmodulin. Biochem Biophys Res Commun. 1984 Aug 30;123(1):100–107. doi: 10.1016/0006-291x(84)90385-1. [DOI] [PubMed] [Google Scholar]
  15. Südhof T. C., Ebbecke M., Walker J. H., Fritsche U., Boustead C. Isolation of mammalian calelectrins: a new class of ubiquitous Ca2+-regulated proteins. Biochemistry. 1984 Mar 13;23(6):1103–1109. doi: 10.1021/bi00301a010. [DOI] [PubMed] [Google Scholar]
  16. Südhof T. C., Zimmermann C. W., Walker J. H. Calelectrin in human blood cells. Eur J Cell Biol. 1983 May;30(2):214–218. [PubMed] [Google Scholar]

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