Non-muscle myosin heavy chain as a possible target for protein encoded by metastasis-related mts-1 gene
The mts-1 gene is associated with the expression of the metastatic phenotype of tumor cells. The protein product of the mts-1 gene belongs to the S100 family of Ca(2+)-binding proteins with unknown biochemical function. In the present work, monoclonal anti-Mts-1 antibodies were used to isolate and c...
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Veröffentlicht in: | The Journal of biological chemistry 1994-08, Vol.269 (31), p.19679-19682 |
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container_end_page | 19682 |
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container_issue | 31 |
container_start_page | 19679 |
container_title | The Journal of biological chemistry |
container_volume | 269 |
creator | KRIAJEVSKA, M. V CARDENAS, M. N GRIGORIAN, M. S AMBARTSUMIAN, N. S GEORGIEV, G. P LUKANIDIN, E. M |
description | The mts-1 gene is associated with the expression of the metastatic phenotype of tumor cells. The protein product of the mts-1
gene belongs to the S100 family of Ca(2+)-binding proteins with unknown biochemical function. In the present work, monoclonal
anti-Mts-1 antibodies were used to isolate and characterize Mts-1 protein possible targets. Mts-1 protein can be immunoprecipitated
by both anti-Mts-1 and anti-myosin antibodies as a complex with myosin from lysates of different mouse and human cell lines.
Precipitation of myosin by anti-Mts-1 antibodies is specific and depends on the presence of Mts-1 protein. Ca(2+)-dependent
association between Mts-1 protein and the heavy chain of non-muscle myosin was demonstrated by blot overlay technique. Furthermore,
association between myosin and Mts-1 was confirmed by sucrose gradient analysis. Finally, immunofluorescent staining of the
mouse mammary adenocarcinoma cell line showed that Mts-1 protein is co-localized with the myosin complex. The data suggest
that the target for Mts-1 protein is a heavy chain of non-muscle myosin. |
doi_str_mv | 10.1016/s0021-9258(17)32072-0 |
format | Article |
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gene belongs to the S100 family of Ca(2+)-binding proteins with unknown biochemical function. In the present work, monoclonal
anti-Mts-1 antibodies were used to isolate and characterize Mts-1 protein possible targets. Mts-1 protein can be immunoprecipitated
by both anti-Mts-1 and anti-myosin antibodies as a complex with myosin from lysates of different mouse and human cell lines.
Precipitation of myosin by anti-Mts-1 antibodies is specific and depends on the presence of Mts-1 protein. Ca(2+)-dependent
association between Mts-1 protein and the heavy chain of non-muscle myosin was demonstrated by blot overlay technique. Furthermore,
association between myosin and Mts-1 was confirmed by sucrose gradient analysis. Finally, immunofluorescent staining of the
mouse mammary adenocarcinoma cell line showed that Mts-1 protein is co-localized with the myosin complex. The data suggest
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gene belongs to the S100 family of Ca(2+)-binding proteins with unknown biochemical function. In the present work, monoclonal
anti-Mts-1 antibodies were used to isolate and characterize Mts-1 protein possible targets. Mts-1 protein can be immunoprecipitated
by both anti-Mts-1 and anti-myosin antibodies as a complex with myosin from lysates of different mouse and human cell lines.
Precipitation of myosin by anti-Mts-1 antibodies is specific and depends on the presence of Mts-1 protein. Ca(2+)-dependent
association between Mts-1 protein and the heavy chain of non-muscle myosin was demonstrated by blot overlay technique. Furthermore,
association between myosin and Mts-1 was confirmed by sucrose gradient analysis. Finally, immunofluorescent staining of the
mouse mammary adenocarcinoma cell line showed that Mts-1 protein is co-localized with the myosin complex. The data suggest
that the target for Mts-1 protein is a heavy chain of non-muscle myosin.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cell physiology</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>Fluorescent Antibody Technique</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Muscles - metabolism</subject><subject>Myosins - metabolism</subject><subject>Neoplasm Metastasis - genetics</subject><subject>S100 Calcium-Binding Protein A4</subject><subject>S100 Proteins</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFDEQx4Mo6-zqR1jIQUQPrak8O0dZVldY9KCCt5Ckq6cj_RiTHmW-vRl3GI-GUBVSv3rwL0Kugb0BBvptYYxDY7lqX4F5LTgzvGGPyAZYKxqh4PtjsjkjT8llKT9YPdLCBblomQImxYZsPy1zM-1LHJFOh6WkmQ7ofx1oHHx9-0I93S2lpFCB1ectrrRfMt3lZcUK4ByXDjsaDnTC1Zd6U2kyjn6tv9NaGqBbnPEZedL7seDzk78i397ffr25a-4_f_h48-6-iZIDq5ZZG3WoFkIIwkTtJUZmO6mNNL3B3iiQUYQYvBAKdee1hNApHtouRHFFXj7UrQP-3GNZ3ZRKxHH0My774ozWXKlW_RcEbazlklVQPYAxVx0y9m6X0-TzwQFzx024L0eZ3VFmB8b93YQ75l2fGuzDhN056yR9jb84xX2Jfuyzn2MqZ0xyqaUx_7AhbYffKaMLaYkDTo5r6wQ4sHVS8QeOPJ01</recordid><startdate>19940805</startdate><enddate>19940805</enddate><creator>KRIAJEVSKA, M. 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Psychology</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Muscles - metabolism</topic><topic>Myosins - metabolism</topic><topic>Neoplasm Metastasis - genetics</topic><topic>S100 Calcium-Binding Protein A4</topic><topic>S100 Proteins</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KRIAJEVSKA, M. V</creatorcontrib><creatorcontrib>CARDENAS, M. N</creatorcontrib><creatorcontrib>GRIGORIAN, M. S</creatorcontrib><creatorcontrib>AMBARTSUMIAN, N. S</creatorcontrib><creatorcontrib>GEORGIEV, G. P</creatorcontrib><creatorcontrib>LUKANIDIN, E. 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M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Non-muscle myosin heavy chain as a possible target for protein encoded by metastasis-related mts-1 gene</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-08-05</date><risdate>1994</risdate><volume>269</volume><issue>31</issue><spage>19679</spage><epage>19682</epage><pages>19679-19682</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The mts-1 gene is associated with the expression of the metastatic phenotype of tumor cells. The protein product of the mts-1
gene belongs to the S100 family of Ca(2+)-binding proteins with unknown biochemical function. In the present work, monoclonal
anti-Mts-1 antibodies were used to isolate and characterize Mts-1 protein possible targets. Mts-1 protein can be immunoprecipitated
by both anti-Mts-1 and anti-myosin antibodies as a complex with myosin from lysates of different mouse and human cell lines.
Precipitation of myosin by anti-Mts-1 antibodies is specific and depends on the presence of Mts-1 protein. Ca(2+)-dependent
association between Mts-1 protein and the heavy chain of non-muscle myosin was demonstrated by blot overlay technique. Furthermore,
association between myosin and Mts-1 was confirmed by sucrose gradient analysis. Finally, immunofluorescent staining of the
mouse mammary adenocarcinoma cell line showed that Mts-1 protein is co-localized with the myosin complex. The data suggest
that the target for Mts-1 protein is a heavy chain of non-muscle myosin.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8051043</pmid><doi>10.1016/s0021-9258(17)32072-0</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Binding Sites Biological and medical sciences Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology Humans Mice Molecular and cellular biology Molecular Sequence Data Muscles - metabolism Myosins - metabolism Neoplasm Metastasis - genetics S100 Calcium-Binding Protein A4 S100 Proteins Tumor Cells, Cultured |
title | Non-muscle myosin heavy chain as a possible target for protein encoded by metastasis-related mts-1 gene |
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