Biglycan is overexpressed in pancreatic cancer and induces G1-arrest in pancreatic cancer cell lines

Gastroenterology. 2001 Sep;121(3):657-67. doi: 10.1053/gast.2001.27222.

Abstract

Background & aims: Biglycan (PG-I), a component of the extracellular matrix (ECM), is overexpressed in pancreatic cancer. To determine possible matrix-tumor interactions, we investigated the effects of PG-I on pancreatic cancer.

Methods: PG-I expression in cell lines and tissue samples was examined by Northern blot and immunofluorescence. The effect of PG-I on proliferation was determined by measuring activity of Ras, ERK, Rb, [(3)H]-thymidine incorporation, and cell cycle analysis. Expression of cyclin A, B1, D1, E1, G1, PCNA, p21, and p27 was analyzed by Northern and Western blots.

Results: PG-I was overexpressed in the ECM of pancreatic cancer samples compared with normal pancreas or chronic pancreatitis tissues. Addition of transforming growth factor (TGF)-beta induced PG-I expression in HFL and HFFF2 fibroblasts as well as in the pancreatic cancer cell line PANC-1. PG-I inhibited growth of both TGF-beta-responsive and TGF-beta-unresponsive pancreatic cancer cells by inducing G1-arrest, which is accompanied by an increase of p27 and reduction of cyclin A and proliferating cell nuclear antigen. Furthermore, endogenous Ras and ERK activation was partly reduced by PG-I in vitro.

Conclusions: The ECM protein PG-I inhibits growth by arresting pancreatic cancer cells in G1 and may be part of a host defense mechanism aimed at slowing down pancreatic tumor progression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aged
  • Animals
  • Biglycan
  • Cell Cycle Proteins / analysis
  • Cell Cycle Proteins / metabolism
  • Cyclin A / metabolism
  • Cyclin-Dependent Kinase Inhibitor p27
  • Extracellular Matrix Proteins
  • Female
  • G1 Phase / physiology*
  • G2 Phase / physiology
  • Gene Expression Regulation, Neoplastic / drug effects
  • Gene Expression Regulation, Neoplastic / physiology*
  • Humans
  • Male
  • Mice
  • Mice, Nude
  • Middle Aged
  • Neoplasm Transplantation
  • Pancreatic Neoplasms*
  • Phosphorylation
  • Proliferating Cell Nuclear Antigen / metabolism
  • Proteoglycans / analysis
  • Proteoglycans / genetics*
  • Proto-Oncogene Proteins p21(ras) / analysis
  • Proto-Oncogene Proteins p21(ras) / metabolism
  • RNA, Messenger / analysis
  • Retinoblastoma Protein / analysis
  • Retinoblastoma Protein / metabolism
  • S Phase / physiology
  • Stromal Cells / chemistry
  • Stromal Cells / physiology
  • Transforming Growth Factor beta / pharmacology
  • Transplantation, Heterologous
  • Tumor Cells, Cultured / chemistry
  • Tumor Cells, Cultured / cytology
  • Tumor Cells, Cultured / metabolism
  • Tumor Suppressor Proteins*

Substances

  • BGN protein, human
  • Bgn protein, mouse
  • Biglycan
  • Cdkn1b protein, mouse
  • Cell Cycle Proteins
  • Cyclin A
  • Extracellular Matrix Proteins
  • Proliferating Cell Nuclear Antigen
  • Proteoglycans
  • RNA, Messenger
  • Retinoblastoma Protein
  • Transforming Growth Factor beta
  • Tumor Suppressor Proteins
  • Cyclin-Dependent Kinase Inhibitor p27
  • HRAS protein, human
  • Proto-Oncogene Proteins p21(ras)