Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin.

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin. / Wewer, U M; Liotta, L A; Jaye, M; Ricca, G A; Drohan, W N; Claysmith, A P; Rao, C N; Wirth, P; Coligan, J E; Albrechtsen, R.

In: Proceedings of the National Academy of Science of the United States of America, Vol. 83, No. 19, 1986, p. 7137-41.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Wewer, UM, Liotta, LA, Jaye, M, Ricca, GA, Drohan, WN, Claysmith, AP, Rao, CN, Wirth, P, Coligan, JE & Albrechtsen, R 1986, 'Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin.', Proceedings of the National Academy of Science of the United States of America, vol. 83, no. 19, pp. 7137-41.

APA

Wewer, U. M., Liotta, L. A., Jaye, M., Ricca, G. A., Drohan, W. N., Claysmith, A. P., Rao, C. N., Wirth, P., Coligan, J. E., & Albrechtsen, R. (1986). Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin. Proceedings of the National Academy of Science of the United States of America, 83(19), 7137-41.

Vancouver

Wewer UM, Liotta LA, Jaye M, Ricca GA, Drohan WN, Claysmith AP et al. Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin. Proceedings of the National Academy of Science of the United States of America. 1986;83(19):7137-41.

Author

Wewer, U M ; Liotta, L A ; Jaye, M ; Ricca, G A ; Drohan, W N ; Claysmith, A P ; Rao, C N ; Wirth, P ; Coligan, J E ; Albrechtsen, R. / Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin. In: Proceedings of the National Academy of Science of the United States of America. 1986 ; Vol. 83, No. 19. pp. 7137-41.

Bibtex

@article{f8f942b05c7f11dd8d9f000ea68e967b,
title = "Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin.",
abstract = "The human laminin receptor was purified and molecularly cloned to investigate its biosynthetic regulation. Laminin receptor from normal and neoplastic tissue was preparatively affinity purified to homogeneity based on the high affinity of the receptor for laminin. The apparent molecular weight of the receptor from different carcinoma sources and from normal placental tissue is in the range of 68-72 kDa. Isoelectric focusing and two-dimensional gel electrophoresis indicated that the receptor protein consists of one major polypeptide chain with a pI value of 6.4 +/- 0.2. Laminin receptor cDNA clones were isolated after screening a human endothelial lambda gt11 cDNA library with a monoclonal antibody directed against a domain of the laminin receptor involved in ligand binding. Definitive identification of the cDNA clones was based on comparison of cDNA sequence with the amino acid sequence of a cyanogen bromide-generated octapeptide of purified placental laminin receptor. The laminin receptor mRNA is approximately 1700 bases long. The level of laminin receptor mRNA in a variety of human carcinoma-derived cell lines correlated with the number of laminin receptors on the cell surfaces of those cells. This suggests that the amount of laminin receptor mRNA may be a rate-limiting control step in the biosynthesis of the laminin receptor, and hence in the regulation of cellular attachment to basement membranes via laminin.",
author = "Wewer, {U M} and Liotta, {L A} and M Jaye and Ricca, {G A} and Drohan, {W N} and Claysmith, {A P} and Rao, {C N} and P Wirth and Coligan, {J E} and R Albrechtsen",
note = "Keywords: Amino Acid Sequence; Base Sequence; Breast Neoplasms; Carcinoma; Cell Line; Cloning, Molecular; DNA; Epitopes; Gene Expression Regulation; Humans; Laminin; RNA, Messenger; Receptors, Immunologic; Receptors, Laminin",
year = "1986",
language = "English",
volume = "83",
pages = "7137--41",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "19",

}

RIS

TY - JOUR

T1 - Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin.

AU - Wewer, U M

AU - Liotta, L A

AU - Jaye, M

AU - Ricca, G A

AU - Drohan, W N

AU - Claysmith, A P

AU - Rao, C N

AU - Wirth, P

AU - Coligan, J E

AU - Albrechtsen, R

N1 - Keywords: Amino Acid Sequence; Base Sequence; Breast Neoplasms; Carcinoma; Cell Line; Cloning, Molecular; DNA; Epitopes; Gene Expression Regulation; Humans; Laminin; RNA, Messenger; Receptors, Immunologic; Receptors, Laminin

PY - 1986

Y1 - 1986

N2 - The human laminin receptor was purified and molecularly cloned to investigate its biosynthetic regulation. Laminin receptor from normal and neoplastic tissue was preparatively affinity purified to homogeneity based on the high affinity of the receptor for laminin. The apparent molecular weight of the receptor from different carcinoma sources and from normal placental tissue is in the range of 68-72 kDa. Isoelectric focusing and two-dimensional gel electrophoresis indicated that the receptor protein consists of one major polypeptide chain with a pI value of 6.4 +/- 0.2. Laminin receptor cDNA clones were isolated after screening a human endothelial lambda gt11 cDNA library with a monoclonal antibody directed against a domain of the laminin receptor involved in ligand binding. Definitive identification of the cDNA clones was based on comparison of cDNA sequence with the amino acid sequence of a cyanogen bromide-generated octapeptide of purified placental laminin receptor. The laminin receptor mRNA is approximately 1700 bases long. The level of laminin receptor mRNA in a variety of human carcinoma-derived cell lines correlated with the number of laminin receptors on the cell surfaces of those cells. This suggests that the amount of laminin receptor mRNA may be a rate-limiting control step in the biosynthesis of the laminin receptor, and hence in the regulation of cellular attachment to basement membranes via laminin.

AB - The human laminin receptor was purified and molecularly cloned to investigate its biosynthetic regulation. Laminin receptor from normal and neoplastic tissue was preparatively affinity purified to homogeneity based on the high affinity of the receptor for laminin. The apparent molecular weight of the receptor from different carcinoma sources and from normal placental tissue is in the range of 68-72 kDa. Isoelectric focusing and two-dimensional gel electrophoresis indicated that the receptor protein consists of one major polypeptide chain with a pI value of 6.4 +/- 0.2. Laminin receptor cDNA clones were isolated after screening a human endothelial lambda gt11 cDNA library with a monoclonal antibody directed against a domain of the laminin receptor involved in ligand binding. Definitive identification of the cDNA clones was based on comparison of cDNA sequence with the amino acid sequence of a cyanogen bromide-generated octapeptide of purified placental laminin receptor. The laminin receptor mRNA is approximately 1700 bases long. The level of laminin receptor mRNA in a variety of human carcinoma-derived cell lines correlated with the number of laminin receptors on the cell surfaces of those cells. This suggests that the amount of laminin receptor mRNA may be a rate-limiting control step in the biosynthesis of the laminin receptor, and hence in the regulation of cellular attachment to basement membranes via laminin.

M3 - Journal article

C2 - 2429301

VL - 83

SP - 7137

EP - 7141

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 19

ER -

ID: 5236992