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Growth factor regulation of a 69kDa phosphoprotein secreted by NRK- -49F cells

Our study shows that the secretion of a major glycosylated, phosphoprotein with a molecular weight of 69kDa (pp69) is a specific marker for non-transformed NRK-49F cells. Antibody raised against pp69 recognizes, in addition to pp69, another major phosphoprotein with a molecular weight of 62kDa (pp62) secreted by RR1022 and spontaneously transformed NRK-49F cells (spt-NRK-49F). Immunoprecipitation of total cell lysates from both NRK-49F and RR1022 cells with anti-pp69 antibody detected only pp69. Treatments with: epidermal growth factor (EGF), transforming growth factor-$ beta$ (TGF-$ beta$) retinoic acid (RA), and TPA modulate the levels of pp69 present in the conditioned media. Furthermore, TPA and EGF induce the synthesis of 3 internal peptides with molecular weights of 58, 54, and 44 kDa which appear to be pre-processed forms of pp69. / Treatment of NRK-49F cells with insulin, EGF, TGF-$ beta$, PPA, levamisole and spermine clearly demonstrate alterations in the phosphorylation of pp69, concomitant with changes in extracellular phosphatase activity.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.59535
Date January 1989
CreatorsLaverdure, Guy R. J.
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageMaster of Science (Department of Biology.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 001072247, proquestno: AAIMM63670, Theses scanned by UMI/ProQuest.

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