Laminin, a noncollagenous component of epithelial basement membranes synthesized by a rat yolk sac tumor.

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Laminin, a noncollagenous component of epithelial basement membranes synthesized by a rat yolk sac tumor. / Wewer, U; Albrechtsen, R; Ruoslahti, E.

In: Cancer Research, Vol. 41, No. 4, 1981, p. 1518-24.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Wewer, U, Albrechtsen, R & Ruoslahti, E 1981, 'Laminin, a noncollagenous component of epithelial basement membranes synthesized by a rat yolk sac tumor.', Cancer Research, vol. 41, no. 4, pp. 1518-24.

APA

Wewer, U., Albrechtsen, R., & Ruoslahti, E. (1981). Laminin, a noncollagenous component of epithelial basement membranes synthesized by a rat yolk sac tumor. Cancer Research, 41(4), 1518-24.

Vancouver

Wewer U, Albrechtsen R, Ruoslahti E. Laminin, a noncollagenous component of epithelial basement membranes synthesized by a rat yolk sac tumor. Cancer Research. 1981;41(4):1518-24.

Author

Wewer, U ; Albrechtsen, R ; Ruoslahti, E. / Laminin, a noncollagenous component of epithelial basement membranes synthesized by a rat yolk sac tumor. In: Cancer Research. 1981 ; Vol. 41, No. 4. pp. 1518-24.

Bibtex

@article{f7e485105c8411dd8d9f000ea68e967b,
title = "Laminin, a noncollagenous component of epithelial basement membranes synthesized by a rat yolk sac tumor.",
abstract = "Laminin, a glycoprotein antigenically similar or identical to a component of epithelial basement membranes, was identified as a major component of the abundant extracellular matrix synthesized by an experimentally induced rat yolk sac tumor. Immunocytochemical staining revealed laminin in cultured tumor cells as well as in their extracellular matrix. The presence of soluble laminin in the culture media of the tumor cells was demonstrated using metabolic labeling followed by identification by immunoprecipitation and sodium dodecyl sulfate:polyacrylamide gel electrophoresis. This revealed two polypeptides with molecular weights of approximately 200,000 and 400,000. These comigrated with the polypeptides of mouse laminin isolated previously. The yolk sac tumor tissue grown in vivo contained laminin in the tumor cells and in the extracellular material as evidenced by immunofluorescence and immunoperoxidase staining. Immunization with the tumor matrix resulted in an antiserum that contained antilaminin and natifibronectin and was made specific for laminin by absorption with fibronectin. This antiserum precipitated laminin polypeptides from culture medium of yolk sac tumour cells and stained basement membranes in rat tissues in a manner indistinguishable from antilaminin. The presence of laminin in rat yolk sac cells, the presumed origin of our yolk sac tumor, was studied in some detail. Laminin was found to be present in normal cells of the visceral as well as the parietal yolk sac layer and in their basement membranes suggesting, but not proving, that both types of cells have ability to synthesize laminin. Production of laminin and the presence of laminin-containing basement membrane material may be important for the biological behavior of the yolk sac tumor. This tumor will also be a useful source of laminin for chemical and biological characterization of this basement membrane protein.",
author = "U Wewer and R Albrechtsen and E Ruoslahti",
note = "Keywords: Animals; Basement Membrane; Cell Line; Electrophoresis, Polyacrylamide Gel; Epithelium; Fibronectins; Fluorescent Antibody Technique; Glycoproteins; Laminin; Mesonephroma; Neoplasm Proteins; Neoplasms, Experimental; Rats",
year = "1981",
language = "English",
volume = "41",
pages = "1518--24",
journal = "Cancer Research",
issn = "0008-5472",
publisher = "American Association for Cancer Research",
number = "4",

}

RIS

TY - JOUR

T1 - Laminin, a noncollagenous component of epithelial basement membranes synthesized by a rat yolk sac tumor.

AU - Wewer, U

AU - Albrechtsen, R

AU - Ruoslahti, E

N1 - Keywords: Animals; Basement Membrane; Cell Line; Electrophoresis, Polyacrylamide Gel; Epithelium; Fibronectins; Fluorescent Antibody Technique; Glycoproteins; Laminin; Mesonephroma; Neoplasm Proteins; Neoplasms, Experimental; Rats

PY - 1981

Y1 - 1981

N2 - Laminin, a glycoprotein antigenically similar or identical to a component of epithelial basement membranes, was identified as a major component of the abundant extracellular matrix synthesized by an experimentally induced rat yolk sac tumor. Immunocytochemical staining revealed laminin in cultured tumor cells as well as in their extracellular matrix. The presence of soluble laminin in the culture media of the tumor cells was demonstrated using metabolic labeling followed by identification by immunoprecipitation and sodium dodecyl sulfate:polyacrylamide gel electrophoresis. This revealed two polypeptides with molecular weights of approximately 200,000 and 400,000. These comigrated with the polypeptides of mouse laminin isolated previously. The yolk sac tumor tissue grown in vivo contained laminin in the tumor cells and in the extracellular material as evidenced by immunofluorescence and immunoperoxidase staining. Immunization with the tumor matrix resulted in an antiserum that contained antilaminin and natifibronectin and was made specific for laminin by absorption with fibronectin. This antiserum precipitated laminin polypeptides from culture medium of yolk sac tumour cells and stained basement membranes in rat tissues in a manner indistinguishable from antilaminin. The presence of laminin in rat yolk sac cells, the presumed origin of our yolk sac tumor, was studied in some detail. Laminin was found to be present in normal cells of the visceral as well as the parietal yolk sac layer and in their basement membranes suggesting, but not proving, that both types of cells have ability to synthesize laminin. Production of laminin and the presence of laminin-containing basement membrane material may be important for the biological behavior of the yolk sac tumor. This tumor will also be a useful source of laminin for chemical and biological characterization of this basement membrane protein.

AB - Laminin, a glycoprotein antigenically similar or identical to a component of epithelial basement membranes, was identified as a major component of the abundant extracellular matrix synthesized by an experimentally induced rat yolk sac tumor. Immunocytochemical staining revealed laminin in cultured tumor cells as well as in their extracellular matrix. The presence of soluble laminin in the culture media of the tumor cells was demonstrated using metabolic labeling followed by identification by immunoprecipitation and sodium dodecyl sulfate:polyacrylamide gel electrophoresis. This revealed two polypeptides with molecular weights of approximately 200,000 and 400,000. These comigrated with the polypeptides of mouse laminin isolated previously. The yolk sac tumor tissue grown in vivo contained laminin in the tumor cells and in the extracellular material as evidenced by immunofluorescence and immunoperoxidase staining. Immunization with the tumor matrix resulted in an antiserum that contained antilaminin and natifibronectin and was made specific for laminin by absorption with fibronectin. This antiserum precipitated laminin polypeptides from culture medium of yolk sac tumour cells and stained basement membranes in rat tissues in a manner indistinguishable from antilaminin. The presence of laminin in rat yolk sac cells, the presumed origin of our yolk sac tumor, was studied in some detail. Laminin was found to be present in normal cells of the visceral as well as the parietal yolk sac layer and in their basement membranes suggesting, but not proving, that both types of cells have ability to synthesize laminin. Production of laminin and the presence of laminin-containing basement membrane material may be important for the biological behavior of the yolk sac tumor. This tumor will also be a useful source of laminin for chemical and biological characterization of this basement membrane protein.

M3 - Journal article

C2 - 7011537

VL - 41

SP - 1518

EP - 1524

JO - Cancer Research

JF - Cancer Research

SN - 0008-5472

IS - 4

ER -

ID: 5237282