Identification of centrosomal proteins in a human lymphoblastic cell line

• Published in: The EMBO journal Vol. 5; no. 10; pp. 2545 - 2550
• Main Authors: Gosti‐Testu, F., Marty, M.C., Berges, J., Maunoury, R., Bornens, M.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group 01.10.1986; EMBO Press
• Subjects: Antibodies; Biological and medical sciences; Cell Fractionation - methods; Cell Line; Cell structures and functions; Cytoskeleton, cytoplasm. Intracellular movements; Fluorescent Antibody Technique; Fundamental and applied biological sciences. Psychology; HeLa Cells - ultrastructure; Humans; Immunoenzyme Techniques; Life Sciences; lymphocytes T; Microtubule Proteins - isolation & purification; Microtubules - ultrastructure; Molecular and cellular biology; Organoids - ultrastructure; proteins; T-Lymphocytes; Vegetal Biology; Human; Proteins; Nucleation; Established cell line; Identification; Lymphoblast; Microtubule; Centrosome
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1002/j.1460-2075.1986.tb04533.x

Highly enriched preparations of centrosomes from human T‐lymphoblasts KE 37 were analyzed for their protein content. The specific pattern of polypeptides was characterized by an abundant subset of high mol. wt proteins and a major group of proteins with mol. wt ranging from 50 to 65 kd. Several immunoreactive proteins were identified, using a rabbit serum spontaneously reacting with human centrosomes. They include a family of high mol. wt ranging from 180 to 250 kd, a 130‐kd protein and a 60‐65 kd doublet. These antigens have the following properties: they are localized within the pericentriolar material; their abundance, as judged by centrosome labelling, changes significantly during the cell cycle, the maximum being observed at the pole of the metaphasic spindle; in Taxol‐treated cells where the centrosome is no longer acting as a nucleating center, they redistribute at one end of the microtubule arrays in both mitotic and interphasic cells, as expected for nucleating, or capping, proteins. All these properties are compatible with their involvement in microtubule nucleation.