Distribution of a tumor cell surface protein common to several murine lung carcinomas

S. J. Kennel, P. K. Lankford, L. J. Foote, F. S. Tsakeres, L. M. Adams, R. L. Ullrich

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

In previous work with line 1, a spontaneous BALB/c alveolar carcinoma, the authors identified a surface protein with a molecular weight of 180,000 (TSP-180) on tumor cells but not on normal mouse cells. This protein was not identical to known cell surface proteins or any C-type virus protein. In this report, the authors continued to characterize TSP-180. It can be labeled metabolically with [ 3H]leucine or [ 3H]glucosamine, confirming that it is a glycoprotein synthesized by line 1 cells. In addition, a competition radioimmunoassay using radioiodinated TSP-180 from line 1 cells was used to measure the amount of TSP-180 in tissues of tumor-bearing animals as well as in other tissues and cells. It was found that during tumor growth, TSP-180 accumulates in the area of primary tumor to a plateau level. It is not detected in other organs except that small amounts are detected in serum when the primary tumor exceeds 1 cm in diameter. No evidence of cross-reactive material was found using BALB/c fibroblasts, mouse mammary tumor cells, BALB/c embryonic tissues, rat tracheal tumor cells, or human alveolar tumor cells. Complete competition was obtained using line 1 tissue culture cell or extracted tumor proteins. Carcinomas from two other mouse strains were also good competitors while adenomas of BALB/c lung competed weakly. Proteins from six other BALB/c lung carcinoma cell lines derived from radiation- or chemically-induced tumors as well as tumors of spontaneous origin were also found to compete efficiently in the radioimmunoassay. The presence of TSP-180 on the surfaces of these lung carcinoma cell lines was confirmed using radioiodination catalyzed by lactoperoxidase. Partial protease digests of TSP-180 isolated from four of these lines showed identical molecular weight patterns indicating a highly conserved sequence homology. These results strongly suggest that TSP-180 represents a cell surface protein common to several tumors of the lung carcinoma class. The feasibility of using TSP-180 antigenic determinants for early detection of radiation or chemically-induced tumors, for monitoring progression of metastases, or as targets for directed drug delivery is discussed.

Original languageEnglish (US)
Pages (from-to)2153-2159
Number of pages7
JournalCancer Research
Volume40
Issue number7
StatePublished - 1980
Externally publishedYes

Fingerprint

Integrin alpha6beta4
Membrane Proteins
Carcinoma
Lung
Neoplasms
Radioimmunoassay
Molecular Weight
Radiation
Bronchiolo-Alveolar Adenocarcinoma
Lactoperoxidase
Alveolar Epithelial Cells
Cell Line
Proteins
Conserved Sequence
Glucosamine
Sequence Homology
Protein C
Leucine
Adenoma
Epitopes

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

Kennel, S. J., Lankford, P. K., Foote, L. J., Tsakeres, F. S., Adams, L. M., & Ullrich, R. L. (1980). Distribution of a tumor cell surface protein common to several murine lung carcinomas. Cancer Research, 40(7), 2153-2159.

Distribution of a tumor cell surface protein common to several murine lung carcinomas. / Kennel, S. J.; Lankford, P. K.; Foote, L. J.; Tsakeres, F. S.; Adams, L. M.; Ullrich, R. L.

In: Cancer Research, Vol. 40, No. 7, 1980, p. 2153-2159.

Research output: Contribution to journalArticle

Kennel, SJ, Lankford, PK, Foote, LJ, Tsakeres, FS, Adams, LM & Ullrich, RL 1980, 'Distribution of a tumor cell surface protein common to several murine lung carcinomas', Cancer Research, vol. 40, no. 7, pp. 2153-2159.
Kennel SJ, Lankford PK, Foote LJ, Tsakeres FS, Adams LM, Ullrich RL. Distribution of a tumor cell surface protein common to several murine lung carcinomas. Cancer Research. 1980;40(7):2153-2159.
Kennel, S. J. ; Lankford, P. K. ; Foote, L. J. ; Tsakeres, F. S. ; Adams, L. M. ; Ullrich, R. L. / Distribution of a tumor cell surface protein common to several murine lung carcinomas. In: Cancer Research. 1980 ; Vol. 40, No. 7. pp. 2153-2159.
@article{cb79c93c45734f1c9ff8035312b3df27,
title = "Distribution of a tumor cell surface protein common to several murine lung carcinomas",
abstract = "In previous work with line 1, a spontaneous BALB/c alveolar carcinoma, the authors identified a surface protein with a molecular weight of 180,000 (TSP-180) on tumor cells but not on normal mouse cells. This protein was not identical to known cell surface proteins or any C-type virus protein. In this report, the authors continued to characterize TSP-180. It can be labeled metabolically with [ 3H]leucine or [ 3H]glucosamine, confirming that it is a glycoprotein synthesized by line 1 cells. In addition, a competition radioimmunoassay using radioiodinated TSP-180 from line 1 cells was used to measure the amount of TSP-180 in tissues of tumor-bearing animals as well as in other tissues and cells. It was found that during tumor growth, TSP-180 accumulates in the area of primary tumor to a plateau level. It is not detected in other organs except that small amounts are detected in serum when the primary tumor exceeds 1 cm in diameter. No evidence of cross-reactive material was found using BALB/c fibroblasts, mouse mammary tumor cells, BALB/c embryonic tissues, rat tracheal tumor cells, or human alveolar tumor cells. Complete competition was obtained using line 1 tissue culture cell or extracted tumor proteins. Carcinomas from two other mouse strains were also good competitors while adenomas of BALB/c lung competed weakly. Proteins from six other BALB/c lung carcinoma cell lines derived from radiation- or chemically-induced tumors as well as tumors of spontaneous origin were also found to compete efficiently in the radioimmunoassay. The presence of TSP-180 on the surfaces of these lung carcinoma cell lines was confirmed using radioiodination catalyzed by lactoperoxidase. Partial protease digests of TSP-180 isolated from four of these lines showed identical molecular weight patterns indicating a highly conserved sequence homology. These results strongly suggest that TSP-180 represents a cell surface protein common to several tumors of the lung carcinoma class. The feasibility of using TSP-180 antigenic determinants for early detection of radiation or chemically-induced tumors, for monitoring progression of metastases, or as targets for directed drug delivery is discussed.",
author = "Kennel, {S. J.} and Lankford, {P. K.} and Foote, {L. J.} and Tsakeres, {F. S.} and Adams, {L. M.} and Ullrich, {R. L.}",
year = "1980",
language = "English (US)",
volume = "40",
pages = "2153--2159",
journal = "Journal of Cancer Research",
issn = "0008-5472",
publisher = "American Association for Cancer Research Inc.",
number = "7",

}

TY - JOUR

T1 - Distribution of a tumor cell surface protein common to several murine lung carcinomas

AU - Kennel, S. J.

AU - Lankford, P. K.

AU - Foote, L. J.

AU - Tsakeres, F. S.

AU - Adams, L. M.

AU - Ullrich, R. L.

PY - 1980

Y1 - 1980

N2 - In previous work with line 1, a spontaneous BALB/c alveolar carcinoma, the authors identified a surface protein with a molecular weight of 180,000 (TSP-180) on tumor cells but not on normal mouse cells. This protein was not identical to known cell surface proteins or any C-type virus protein. In this report, the authors continued to characterize TSP-180. It can be labeled metabolically with [ 3H]leucine or [ 3H]glucosamine, confirming that it is a glycoprotein synthesized by line 1 cells. In addition, a competition radioimmunoassay using radioiodinated TSP-180 from line 1 cells was used to measure the amount of TSP-180 in tissues of tumor-bearing animals as well as in other tissues and cells. It was found that during tumor growth, TSP-180 accumulates in the area of primary tumor to a plateau level. It is not detected in other organs except that small amounts are detected in serum when the primary tumor exceeds 1 cm in diameter. No evidence of cross-reactive material was found using BALB/c fibroblasts, mouse mammary tumor cells, BALB/c embryonic tissues, rat tracheal tumor cells, or human alveolar tumor cells. Complete competition was obtained using line 1 tissue culture cell or extracted tumor proteins. Carcinomas from two other mouse strains were also good competitors while adenomas of BALB/c lung competed weakly. Proteins from six other BALB/c lung carcinoma cell lines derived from radiation- or chemically-induced tumors as well as tumors of spontaneous origin were also found to compete efficiently in the radioimmunoassay. The presence of TSP-180 on the surfaces of these lung carcinoma cell lines was confirmed using radioiodination catalyzed by lactoperoxidase. Partial protease digests of TSP-180 isolated from four of these lines showed identical molecular weight patterns indicating a highly conserved sequence homology. These results strongly suggest that TSP-180 represents a cell surface protein common to several tumors of the lung carcinoma class. The feasibility of using TSP-180 antigenic determinants for early detection of radiation or chemically-induced tumors, for monitoring progression of metastases, or as targets for directed drug delivery is discussed.

AB - In previous work with line 1, a spontaneous BALB/c alveolar carcinoma, the authors identified a surface protein with a molecular weight of 180,000 (TSP-180) on tumor cells but not on normal mouse cells. This protein was not identical to known cell surface proteins or any C-type virus protein. In this report, the authors continued to characterize TSP-180. It can be labeled metabolically with [ 3H]leucine or [ 3H]glucosamine, confirming that it is a glycoprotein synthesized by line 1 cells. In addition, a competition radioimmunoassay using radioiodinated TSP-180 from line 1 cells was used to measure the amount of TSP-180 in tissues of tumor-bearing animals as well as in other tissues and cells. It was found that during tumor growth, TSP-180 accumulates in the area of primary tumor to a plateau level. It is not detected in other organs except that small amounts are detected in serum when the primary tumor exceeds 1 cm in diameter. No evidence of cross-reactive material was found using BALB/c fibroblasts, mouse mammary tumor cells, BALB/c embryonic tissues, rat tracheal tumor cells, or human alveolar tumor cells. Complete competition was obtained using line 1 tissue culture cell or extracted tumor proteins. Carcinomas from two other mouse strains were also good competitors while adenomas of BALB/c lung competed weakly. Proteins from six other BALB/c lung carcinoma cell lines derived from radiation- or chemically-induced tumors as well as tumors of spontaneous origin were also found to compete efficiently in the radioimmunoassay. The presence of TSP-180 on the surfaces of these lung carcinoma cell lines was confirmed using radioiodination catalyzed by lactoperoxidase. Partial protease digests of TSP-180 isolated from four of these lines showed identical molecular weight patterns indicating a highly conserved sequence homology. These results strongly suggest that TSP-180 represents a cell surface protein common to several tumors of the lung carcinoma class. The feasibility of using TSP-180 antigenic determinants for early detection of radiation or chemically-induced tumors, for monitoring progression of metastases, or as targets for directed drug delivery is discussed.

UR - http://www.scopus.com/inward/record.url?scp=0018852431&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018852431&partnerID=8YFLogxK

M3 - Article

C2 - 6155990

AN - SCOPUS:0018852431

VL - 40

SP - 2153

EP - 2159

JO - Journal of Cancer Research

JF - Journal of Cancer Research

SN - 0008-5472

IS - 7

ER -