Blast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23.
Blast-1 is a human activation-associated glycoprotein expressed on the surface of leukocytes. Analysis of a translated sequence from a Blast-1 cDNA reveals a single hydrophobic sequence which could traverse the plasma membrane, but is devoid of charged residues that might represent a cytoplasmic tai...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1989
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| _version_ | 1826301087891587072 |
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| author | Staunton, D Fisher, R LeBeau, M Lawrence, J Barton, D Francke, U Dustin, M Thorley-Lawson, D |
| author_facet | Staunton, D Fisher, R LeBeau, M Lawrence, J Barton, D Francke, U Dustin, M Thorley-Lawson, D |
| author_sort | Staunton, D |
| collection | OXFORD |
| description | Blast-1 is a human activation-associated glycoprotein expressed on the surface of leukocytes. Analysis of a translated sequence from a Blast-1 cDNA reveals a single hydrophobic sequence which could traverse the plasma membrane, but is devoid of charged residues that might represent a cytoplasmic tail. Consistent with this characteristic, Blast-1 is demonstrated here to be anchored to the cell surface through a glycosyl-phosphatidylinositol (GPI)-containing lipid. Comparison of Blast-1 to other GPI-anchored membrane proteins revealed a striking primary and secondary structure similarity with MRC OX45 and the lymphocyte function antigen LFA-3. The degree of overall amino acid sequence homology reveals that OX45 is a rat homologue of Blast-1. The greatest homology to LFA-3 occurs between their NH2-terminal Ig-like domains. Evidence is presented that demonstrates that Blast-1 and LFA-3 possess a disulfide-bonded second domain. These common characteristics demonstrate a structural and evolutionary relationship between Blast-1, OX45, LFA-3, and CD2, which in turn suggests a functional role for Blast-1 in cell-cell interactions in the immune response. The gene for Blast-1 has been localized to chromosome 1 q21-q23, indistinguishable from the CD1 cluster of Ig superfamily genes, raising the possibility that they may be linked. |
| first_indexed | 2024-03-07T05:27:04Z |
| format | Journal article |
| id | oxford-uuid:e0ed4d0e-b9a7-4e6c-a7a5-436e4cadf14c |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:27:04Z |
| publishDate | 1989 |
| record_format | dspace |
| spelling | oxford-uuid:e0ed4d0e-b9a7-4e6c-a7a5-436e4cadf14c2022-03-27T09:50:47ZBlast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:e0ed4d0e-b9a7-4e6c-a7a5-436e4cadf14cEnglishSymplectic Elements at Oxford1989Staunton, DFisher, RLeBeau, MLawrence, JBarton, DFrancke, UDustin, MThorley-Lawson, DBlast-1 is a human activation-associated glycoprotein expressed on the surface of leukocytes. Analysis of a translated sequence from a Blast-1 cDNA reveals a single hydrophobic sequence which could traverse the plasma membrane, but is devoid of charged residues that might represent a cytoplasmic tail. Consistent with this characteristic, Blast-1 is demonstrated here to be anchored to the cell surface through a glycosyl-phosphatidylinositol (GPI)-containing lipid. Comparison of Blast-1 to other GPI-anchored membrane proteins revealed a striking primary and secondary structure similarity with MRC OX45 and the lymphocyte function antigen LFA-3. The degree of overall amino acid sequence homology reveals that OX45 is a rat homologue of Blast-1. The greatest homology to LFA-3 occurs between their NH2-terminal Ig-like domains. Evidence is presented that demonstrates that Blast-1 and LFA-3 possess a disulfide-bonded second domain. These common characteristics demonstrate a structural and evolutionary relationship between Blast-1, OX45, LFA-3, and CD2, which in turn suggests a functional role for Blast-1 in cell-cell interactions in the immune response. The gene for Blast-1 has been localized to chromosome 1 q21-q23, indistinguishable from the CD1 cluster of Ig superfamily genes, raising the possibility that they may be linked. |
| spellingShingle | Staunton, D Fisher, R LeBeau, M Lawrence, J Barton, D Francke, U Dustin, M Thorley-Lawson, D Blast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23. |
| title | Blast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23. |
| title_full | Blast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23. |
| title_fullStr | Blast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23. |
| title_full_unstemmed | Blast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23. |
| title_short | Blast-1 possesses a glycosyl-phosphatidylinositol (GPI) membrane anchor, is related to LFA-3 and OX-45, and maps to chromosome 1q21-23. |
| title_sort | blast 1 possesses a glycosyl phosphatidylinositol gpi membrane anchor is related to lfa 3 and ox 45 and maps to chromosome 1q21 23 |
| work_keys_str_mv | AT stauntond blast1possessesaglycosylphosphatidylinositolgpimembraneanchorisrelatedtolfa3andox45andmapstochromosome1q2123 AT fisherr blast1possessesaglycosylphosphatidylinositolgpimembraneanchorisrelatedtolfa3andox45andmapstochromosome1q2123 AT lebeaum blast1possessesaglycosylphosphatidylinositolgpimembraneanchorisrelatedtolfa3andox45andmapstochromosome1q2123 AT lawrencej blast1possessesaglycosylphosphatidylinositolgpimembraneanchorisrelatedtolfa3andox45andmapstochromosome1q2123 AT bartond blast1possessesaglycosylphosphatidylinositolgpimembraneanchorisrelatedtolfa3andox45andmapstochromosome1q2123 AT franckeu blast1possessesaglycosylphosphatidylinositolgpimembraneanchorisrelatedtolfa3andox45andmapstochromosome1q2123 AT dustinm blast1possessesaglycosylphosphatidylinositolgpimembraneanchorisrelatedtolfa3andox45andmapstochromosome1q2123 AT thorleylawsond blast1possessesaglycosylphosphatidylinositolgpimembraneanchorisrelatedtolfa3andox45andmapstochromosome1q2123 |