Date of Award

1990

Embargo Period

8-1-2024

Document Type

Dissertation

Degree Name

Doctor of Philosophy (PhD)

Department

Molecular and Cellular Biology and Pathobiology

College

College of Graduate Studies

Abstract

Human umbilical vein endothelial (HUVE) cells have been previously reported to express the genes for the A and B chain peptides of the dimeric molecule Platelet-Derived Growth Factor (PDGF) and to secrete PDGF-related factors into culture media. Anti-human PDGF IgG affinity chromatography was used to purify PDGF-related activity from HUVE cell conditioned media. Immunoblot analysis of the affinity purified proteins with anti-PDGF IgG and antibodies specific for the A or B chain peptides of PDGF combined with chemotactic and mitogenic assays revealed that the major PDGF immunorelated molecule secreted by HUVE cells is a monomer of approximately 36-38 kd MW and that less than 15% of the purified biologically active molecules are PDGF A or B chain peptides. Screening of an HUVE cell cDNA library in the expression vector lambda gtll with the anti-PDGF antibody resulted in the cloning and sequencing of a cDNA with an open reading frame encoding a 38 kd cysteine-rich secreted protein which our data indicate is the major PDGF-related mitogen secreted by human vascular endothelial cells. The protein has a 45% overall homology to the translation product of the v-src-induced CEF-10 mRNA from chick embryo fibroblasts. We have termed this mitogen Connective Tissue Growth Factor (CTGF).

Rights

All rights reserved. Copyright is held by the author.

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