Abstract
Lymphocytes were assessed for the presence of surface actin and myosin by lactoperoxidase-catalyzed iodination and indirect immunofluorescence using antisera against purified pig skeletal muscle actin and pig smooth muscle myosin. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis of 125I-labeled pig, mouse, and human B lymphocytes revealed an intense radioactive band of 43,000 molecular weight, whereas pig and mouse T lymphocytes gave a much less intense band. This band comigrated with actin, was nonglycosylated as judged by lack of binding to lentil lectin-Sepharose, was bound specifically by myosin fibers, and could be distinguished from a polypeptide of similar mobility derived from the major histocompatibility antigens. These results suggest that actin is present on the surface of B lymphocytes and, to a lesser extent, on T lymphocytes. Pig, mouse, and human Ig-bearing cells were stained by antiactin and antimyosin antisera, as judged by indirect immunofluorescence, whereas non-Ig-bearing cells were not stained. Antibody binding, however, was depleted by adsorbing the antisera with Ig-Sepharose. It was concluded that the immunofluorescence results are misleading and reflect the presence of antibodies that crossreact with Ig.
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- Arce-Gomez B., Jones E. A., Barnstable C. J., Solomon E., Bodmer W. F. The genetic control of HLA-A and B antigens in somatic cell hybrids: requirement for beta2 microglobulin. Tissue Antigens. 1978 Feb;11(2):96–112. doi: 10.1111/j.1399-0039.1978.tb01233.x. [DOI] [PubMed] [Google Scholar]
- Barber B. H., Crumpton M. J. Actin associated with purified lymphocyte plasma membrane. FEBS Lett. 1976 Jul 15;66(2):215–220. doi: 10.1016/0014-5793(76)80507-8. [DOI] [PubMed] [Google Scholar]
- Bottomley R. C., Trayer I. P. Affinity chromatography of immobilized actin and myosin. Biochem J. 1975 Aug;149(2):365–379. doi: 10.1042/bj1490365. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cleveland D. W., Fischer S. G., Kirschner M. W., Laemmli U. K. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem. 1977 Feb 10;252(3):1102–1106. [PubMed] [Google Scholar]
- Edelman G. M. Surface modulation in cell recognition and cell growth. Science. 1976 Apr 16;192(4236):218–226. doi: 10.1126/science.769162. [DOI] [PubMed] [Google Scholar]
- Fagraeus A., Lidman K., Biberfeld G. Reaction of human smooth muscle antibodies with human blood lymphocytes and lymphoid cell lines. Nature. 1974 Nov 15;252(5480):246–247. doi: 10.1038/252246a0. [DOI] [PubMed] [Google Scholar]
- Gabbiani G., Chaponnier C., Zumbe A., Vassalli P. Actin and tubulin co-cap with surface immunoglobulins in mouse B lymphocytes. Nature. 1977 Oct 20;269(5630):697–698. doi: 10.1038/269697a0. [DOI] [PubMed] [Google Scholar]
- Gröschel-Stewart U. Comparative studies of human smooth and striated muscle myosins. Biochim Biophys Acta. 1971 Feb 16;229(2):322–334. doi: 10.1016/0005-2795(71)90191-7. [DOI] [PubMed] [Google Scholar]
- Handwerger B. S., Schwartz R. H. Separation of murine lymphoid cells using nylon wool columns. Recovery of the B cell-enriched population. Transplantation. 1974 Dec;18(6):544–548. doi: 10.1097/00007890-197412000-00013. [DOI] [PubMed] [Google Scholar]
- Hayman M. J., Crumpton M. J. Isolation of glycoproteins from pig lymphocyte plasma membrane using Lens culinaris phytohemagglutinin. Biochem Biophys Res Commun. 1972 May 26;47(4):923–930. doi: 10.1016/0006-291x(72)90581-5. [DOI] [PubMed] [Google Scholar]
- Kekwick R. A. The serum proteins in multiple myelomatosis. Biochem J. 1940 Sep;34(8-9):1248–1257. doi: 10.1042/bj0341248. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Koch G. L., Smith M. J. An association between actin and the major histocompatibility antigen H-2. Nature. 1978 May 25;273(5660):274–278. doi: 10.1038/273274a0. [DOI] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Loken M. R., Herzenber L. A. Analysis of cell populations with a fluorescence-activated cell sorter. Ann N Y Acad Sci. 1975 Jun 30;254:163–171. doi: 10.1111/j.1749-6632.1975.tb29166.x. [DOI] [PubMed] [Google Scholar]
- Maino V. C., Hayman M. J., Crumpton M. J. Relationship between enhanced turnover of phosphatidylinositol and lymphocyte activation by mitogens. Biochem J. 1975 Jan;146(1):247–252. doi: 10.1042/bj1460247. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nicolson G. L. Trans-membrane control of the receptors on normal and tumor cells. II. Surface changes associated with transformation and malignancy. Biochim Biophys Acta. 1976 Apr 30;458(1):1–72. doi: 10.1016/0304-419x(76)90014-7. [DOI] [PubMed] [Google Scholar]
- Olden K., Willingham M., Pastan I. Cell surface myosin in cultured fibroblasts. Cell. 1976 Jul;8(3):383–390. doi: 10.1016/0092-8674(76)90150-1. [DOI] [PubMed] [Google Scholar]
- PORTER R. R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. doi: 10.1042/bj0730119. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Perlés B., Flanagan M. T., Auger J., Crumpton M. J. Mechanism of lymphocyte activation: the binding of phytohemagglutinin to the lymphocyte surface. Eur J Immunol. 1977 Sep;7(9):613–619. doi: 10.1002/eji.1830070907. [DOI] [PubMed] [Google Scholar]
- Pollard T. D., Weihing R. R. Actin and myosin and cell movement. CRC Crit Rev Biochem. 1974 Jan;2(1):1–65. doi: 10.3109/10409237409105443. [DOI] [PubMed] [Google Scholar]
- Puszkin E. G., Maldonado R., Spaet T. H., Zucker M. B. Platelet myosin. Localization of the rod myosin fragment and effect of its antibodies on platelet function. J Biol Chem. 1977 Jun 25;252(12):4371–4378. [PubMed] [Google Scholar]
- Schreiner G. F., Fujiwara K., Pollard T. D., Unanue E. R. Redistribution of myosin accompanying capping of surface Ig. J Exp Med. 1977 May 1;145(5):1393–1398. doi: 10.1084/jem.145.5.1393. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sparrow M. P., Maxwell L. C., Ruegg J. C., Bohr D. F. Preparation and properties of a calcium ion-sensitive actomyosin from arteries. Am J Physiol. 1970 Nov;219(5):1366–1372. doi: 10.1152/ajplegacy.1970.219.5.1366. [DOI] [PubMed] [Google Scholar]
- Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
- Sundqvist K. G., Ehrnst A. Cytoskeletal control of surface membrane mobility. Nature. 1976 Nov 18;264(5583):226–231. doi: 10.1038/264226a0. [DOI] [PubMed] [Google Scholar]
- Trowbridge I. S., Hyman R., Mazauskas C. Surface molecules of cultured human lymphoid cells. Eur J Immunol. 1976 Nov;6(11):777–782. doi: 10.1002/eji.1830061105. [DOI] [PubMed] [Google Scholar]
- Trowbridge I. S., Ralph P., Bevan M. J. Differences in the surface proteins of mouse B and T cells. Proc Natl Acad Sci U S A. 1975 Jan;72(1):157–161. doi: 10.1073/pnas.72.1.157. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Walsh F. S., Crumpton M. J. Orientation of cell-surface antigens in the lipid bilayer of lymphocyte plasma membrane. Nature. 1977 Sep 22;269(5626):307–311. doi: 10.1038/269307a0. [DOI] [PubMed] [Google Scholar]


