Identification of a cytoskeleton-associated glycoprotein from isolated microvilli of a mammary ascites tumor.

Abstract

Microvilli isolated from MAT-C1 13762 ascites tumor cells were extracted with Triton X-100 in phosphate-buffered saline (PBS) to yield cytoskeletal residues. Analysis of the residues by two-dimensional isoelectric focusing-dodecyl sulfate electrophoresis and silver staining suggested that one of the major components is a glycoprotein (CAG). Neuraminidase treatments and glucosamine labeling demonstrated that CAG is a glycoprotein, and lactoperoxidase iodination showed its presence at the microvillar surface. DNase treatments and myosin affinity analysis suggested an association between CAG and the microvillar microfilaments. Thus, CAG has the properties expected of a transmembrane-linking molecule connecting the cell surface to the cytoskeleton.

• Authors: C A Carraway, G Jung, J R Craik, R W Rubin, K L Carraway
• Journal: Experimental cell research (Exp Cell Res) Vol. 143 Issue 2 Pg. 303-8 (Feb 1983) ISSN: 0014-4827 [Print] United States
• PMID: 6682044 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Glycoproteins
• Lactoperoxidase
• Deoxyribonucleases
• Neuraminidase

Topics

• Animals
• Ascites
• Cell Line
• Cell Membrane (analysis)
• Cytoskeleton (analysis)
• Deoxyribonucleases (pharmacology)
• Electrophoresis, Polyacrylamide Gel
• Glycoproteins (analysis)
• Isoelectric Focusing
• Lactoperoxidase
• Mammary Neoplasms, Experimental (analysis)
• Microvilli (analysis)
• Neuraminidase (pharmacology)
• Rats