p24 and p26, structurally related cell surface molecules identified by monoclonal antibody BA-2

Tucker W. LeBlen; Samuel J. Pirruccello; Robert T. McCormack; J. Garrett Bradley

doi:10.1016/0161-5890(85)90007-0

p24 and p26, structurally related cell surface molecules identified by monoclonal antibody BA-2

Tucker W. LeBlen
, Samuel J. Pirruccello
, Robert T. McCormack
, J. Garrett Bradley

Health Sciences Administration

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

This paper describes additional structural analyses of the p24 cell surface molecule recognized by monoclonal antibody BA-2. Since BA-2 is broadly reactive with a variety of normal and malignant lymphohematopoietic and nonlymphohematopoietic cells, we examined the structure of p24 expressed on different cell types. Tryptic peptide mapping and 2-dimensional gel electrophoresis of p24 isolated from colon carcinoma cells, fresh leukemic cells, leukemic cell lines, and activated T-cells indicated that p24 exhibits no structural polymorphism within the cells examined. As has recently been demonstrated with several other cell surface molecules, p24 is shown 10 possess a covalently-attached fatty acid, based on the incorporation of [³H]palmitate. We have also identified an additional protein, designated p26, that is coprecipitated with p24. The p26 molecule is not disulfide-linked to p24, and can be immunoprecipitated from a variety of ¹²⁵I- or [³⁵S]methionine-labeled cells. V8 protease peptide mapping indicated that p24 and p26 are structurally homologous. Pulse-chase analysis using [³⁵S]methionine and digestion with endoglycosidase-F indicated that p24 and p26 are probably derived from a p23 precursor, but no precursor-product relationship exists between p24 and p26. Based on this data we propose that p24 and p26 are most likely differentially-processed protein products of the same gene.

Original language	English (US)
Pages (from-to)	1185-1194
Number of pages	10
Journal	Molecular Immunology
Volume	22
Issue number	10
DOIs	https://doi.org/10.1016/0161-5890(85)90007-0
State	Published - Oct 1985

Bibliographical note

Funding Information:
*Supported by CA-21737, CA-31685 and RR-05385 from the National Institutes of Health, grant IN-13-W-12 from the American Cancer Society, the Alison Eberlein Fund and the Leukemia Research Fund (formerly the Leukemia Task Force). T.W.L. is a Scholar of the Leukemia Society of America. tcorrespondence should be addressed LeBien, Box 609 Mayo, Department Medicine and Pathology, University Minneapolis, MN 55455, U.S.A. fAbbreviations: ALL, acute lymphoblastic leukemia; endo-F, endoglycosidase-F; FBS, fetal bovine serum; IEF, isoelectric focussing; kDa, kilodalton( NP-40, Non-idet P-40; RIP, radioimmunoprecipitation; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electro-phoresis; 2-D, 2-dimensional.

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@article{fb64bbbfde234e4e961c47f0c6464582,

title = "p24 and p26, structurally related cell surface molecules identified by monoclonal antibody BA-2",

abstract = "This paper describes additional structural analyses of the p24 cell surface molecule recognized by monoclonal antibody BA-2. Since BA-2 is broadly reactive with a variety of normal and malignant lymphohematopoietic and nonlymphohematopoietic cells, we examined the structure of p24 expressed on different cell types. Tryptic peptide mapping and 2-dimensional gel electrophoresis of p24 isolated from colon carcinoma cells, fresh leukemic cells, leukemic cell lines, and activated T-cells indicated that p24 exhibits no structural polymorphism within the cells examined. As has recently been demonstrated with several other cell surface molecules, p24 is shown 10 possess a covalently-attached fatty acid, based on the incorporation of [3H]palmitate. We have also identified an additional protein, designated p26, that is coprecipitated with p24. The p26 molecule is not disulfide-linked to p24, and can be immunoprecipitated from a variety of 125I- or [35S]methionine-labeled cells. V8 protease peptide mapping indicated that p24 and p26 are structurally homologous. Pulse-chase analysis using [35S]methionine and digestion with endoglycosidase-F indicated that p24 and p26 are probably derived from a p23 precursor, but no precursor-product relationship exists between p24 and p26. Based on this data we propose that p24 and p26 are most likely differentially-processed protein products of the same gene.",

author = "LeBlen, \{Tucker W.\} and Pirruccello, \{Samuel J.\} and McCormack, \{Robert T.\} and Bradley, \{J. Garrett\}",

note = "Funding Information: *Supported by CA-21737, CA-31685 and RR-05385 from the National Institutes of Health, grant IN-13-W-12 from the American Cancer Society, the Alison Eberlein Fund and the Leukemia Research Fund (formerly the Leukemia Task Force). T.W.L. is a Scholar of the Leukemia Society of America. tcorrespondence should be addressed LeBien, Box 609 Mayo, Department Medicine and Pathology, University Minneapolis, MN 55455, U.S.A. fAbbreviations: ALL, acute lymphoblastic leukemia; endo-F, endoglycosidase-F; FBS, fetal bovine serum; IEF, isoelectric focussing; kDa, kilodalton( NP-40, Non-idet P-40; RIP, radioimmunoprecipitation; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electro-phoresis; 2-D, 2-dimensional.",

year = "1985",

month = oct,

doi = "10.1016/0161-5890(85)90007-0",

language = "English (US)",

volume = "22",

pages = "1185--1194",

journal = "Molecular Immunology",

issn = "0161-5890",

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TY - JOUR

T1 - p24 and p26, structurally related cell surface molecules identified by monoclonal antibody BA-2

AU - LeBlen, Tucker W.

AU - Pirruccello, Samuel J.

AU - McCormack, Robert T.

AU - Bradley, J. Garrett

N1 - Funding Information: *Supported by CA-21737, CA-31685 and RR-05385 from the National Institutes of Health, grant IN-13-W-12 from the American Cancer Society, the Alison Eberlein Fund and the Leukemia Research Fund (formerly the Leukemia Task Force). T.W.L. is a Scholar of the Leukemia Society of America. tcorrespondence should be addressed LeBien, Box 609 Mayo, Department Medicine and Pathology, University Minneapolis, MN 55455, U.S.A. fAbbreviations: ALL, acute lymphoblastic leukemia; endo-F, endoglycosidase-F; FBS, fetal bovine serum; IEF, isoelectric focussing; kDa, kilodalton( NP-40, Non-idet P-40; RIP, radioimmunoprecipitation; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electro-phoresis; 2-D, 2-dimensional.

PY - 1985/10

Y1 - 1985/10

N2 - This paper describes additional structural analyses of the p24 cell surface molecule recognized by monoclonal antibody BA-2. Since BA-2 is broadly reactive with a variety of normal and malignant lymphohematopoietic and nonlymphohematopoietic cells, we examined the structure of p24 expressed on different cell types. Tryptic peptide mapping and 2-dimensional gel electrophoresis of p24 isolated from colon carcinoma cells, fresh leukemic cells, leukemic cell lines, and activated T-cells indicated that p24 exhibits no structural polymorphism within the cells examined. As has recently been demonstrated with several other cell surface molecules, p24 is shown 10 possess a covalently-attached fatty acid, based on the incorporation of [3H]palmitate. We have also identified an additional protein, designated p26, that is coprecipitated with p24. The p26 molecule is not disulfide-linked to p24, and can be immunoprecipitated from a variety of 125I- or [35S]methionine-labeled cells. V8 protease peptide mapping indicated that p24 and p26 are structurally homologous. Pulse-chase analysis using [35S]methionine and digestion with endoglycosidase-F indicated that p24 and p26 are probably derived from a p23 precursor, but no precursor-product relationship exists between p24 and p26. Based on this data we propose that p24 and p26 are most likely differentially-processed protein products of the same gene.

AB - This paper describes additional structural analyses of the p24 cell surface molecule recognized by monoclonal antibody BA-2. Since BA-2 is broadly reactive with a variety of normal and malignant lymphohematopoietic and nonlymphohematopoietic cells, we examined the structure of p24 expressed on different cell types. Tryptic peptide mapping and 2-dimensional gel electrophoresis of p24 isolated from colon carcinoma cells, fresh leukemic cells, leukemic cell lines, and activated T-cells indicated that p24 exhibits no structural polymorphism within the cells examined. As has recently been demonstrated with several other cell surface molecules, p24 is shown 10 possess a covalently-attached fatty acid, based on the incorporation of [3H]palmitate. We have also identified an additional protein, designated p26, that is coprecipitated with p24. The p26 molecule is not disulfide-linked to p24, and can be immunoprecipitated from a variety of 125I- or [35S]methionine-labeled cells. V8 protease peptide mapping indicated that p24 and p26 are structurally homologous. Pulse-chase analysis using [35S]methionine and digestion with endoglycosidase-F indicated that p24 and p26 are probably derived from a p23 precursor, but no precursor-product relationship exists between p24 and p26. Based on this data we propose that p24 and p26 are most likely differentially-processed protein products of the same gene.

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UR - https://www.scopus.com/pages/publications/0021881281#tab=citedBy

U2 - 10.1016/0161-5890(85)90007-0

DO - 10.1016/0161-5890(85)90007-0

M3 - Article

C2 - 4079940

AN - SCOPUS:0021881281

SN - 0161-5890

VL - 22

SP - 1185

EP - 1194

JO - Molecular Immunology

JF - Molecular Immunology

IS - 10

ER -

p24 and p26, structurally related cell surface molecules identified by monoclonal antibody BA-2

Abstract

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