PMA induces shift from chondroitin to heparan sulphate on proteoglycans correlating with fibronectin adhesion of MDS human leukemia cells

J. Tímár, C. Diczhazi, I. Bartha, A. Ladányi, A. Tarcsafalvi, K. Lapis

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

We have analysed the mechanism of PMA-induced adhesion of the MDS human leukemia cell line. Affinity to various matrix ligands indicated that PMA induced fibronectin adhesion of MDS cells. This interaction could not be inhibited by RGDS-peptide, therefore it was most probably not mediated by integrins. Rather, both the basal and PMA-induced fibronectin adhesion of MDS cells could be inhibited by heparin and much less efficiently by chondroitin sulphate, suggesting that glycosaminoglycans of proteoglycans may be responsible for the change in adhesive phenotype. PMA stimulation of MDS cells induced a significant increase in proteoglycan biosynthesis. Studies on the glycosaminoglycan pattern of the proteoglycans showed that PMA treatment initiated a shift in glycanation of the MDS-proteoglycans from the predominant chondroitin sulphate-proteoglycans in control cells to a predominant heparan sulphate-proteoglycans in adherent cells. These data indicate that protein kinase C, the main target of PMA, may have a profound role in the regulation of glycanation pattern of proteoglycans. Furthermore, such alterations in the cellular proteoglycans may significantly affect the matrix adhesion potential of hematopoietic cells.

Original languageEnglish
Pages (from-to)1227-1231
Number of pages5
JournalAnticancer Research
Volume14
Issue number3 A
Publication statusPublished - 1994

Fingerprint

Chondroitin
Heparan Sulfate Proteoglycans
Proteoglycans
Fibronectins
Leukemia
Cell Adhesion
arginyl-glycyl-aspartyl-serine
Chondroitin Sulfate Proteoglycans
Glycosaminoglycans
Integrins
Adhesives
Protein Kinase C
Heparin
Ligands
Phenotype
Cell Line

Keywords

  • Adhesion
  • Leukemia cells
  • PMA
  • Proteoglycans

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

PMA induces shift from chondroitin to heparan sulphate on proteoglycans correlating with fibronectin adhesion of MDS human leukemia cells. / Tímár, J.; Diczhazi, C.; Bartha, I.; Ladányi, A.; Tarcsafalvi, A.; Lapis, K.

In: Anticancer Research, Vol. 14, No. 3 A, 1994, p. 1227-1231.

Research output: Contribution to journalArticle

@article{7d7d629cd92748ad9d822584acbcae8b,
title = "PMA induces shift from chondroitin to heparan sulphate on proteoglycans correlating with fibronectin adhesion of MDS human leukemia cells",
abstract = "We have analysed the mechanism of PMA-induced adhesion of the MDS human leukemia cell line. Affinity to various matrix ligands indicated that PMA induced fibronectin adhesion of MDS cells. This interaction could not be inhibited by RGDS-peptide, therefore it was most probably not mediated by integrins. Rather, both the basal and PMA-induced fibronectin adhesion of MDS cells could be inhibited by heparin and much less efficiently by chondroitin sulphate, suggesting that glycosaminoglycans of proteoglycans may be responsible for the change in adhesive phenotype. PMA stimulation of MDS cells induced a significant increase in proteoglycan biosynthesis. Studies on the glycosaminoglycan pattern of the proteoglycans showed that PMA treatment initiated a shift in glycanation of the MDS-proteoglycans from the predominant chondroitin sulphate-proteoglycans in control cells to a predominant heparan sulphate-proteoglycans in adherent cells. These data indicate that protein kinase C, the main target of PMA, may have a profound role in the regulation of glycanation pattern of proteoglycans. Furthermore, such alterations in the cellular proteoglycans may significantly affect the matrix adhesion potential of hematopoietic cells.",
keywords = "Adhesion, Leukemia cells, PMA, Proteoglycans",
author = "J. T{\'i}m{\'a}r and C. Diczhazi and I. Bartha and A. Lad{\'a}nyi and A. Tarcsafalvi and K. Lapis",
year = "1994",
language = "English",
volume = "14",
pages = "1227--1231",
journal = "Anticancer Research",
issn = "0250-7005",
publisher = "International Institute of Anticancer Research",
number = "3 A",

}

TY - JOUR

T1 - PMA induces shift from chondroitin to heparan sulphate on proteoglycans correlating with fibronectin adhesion of MDS human leukemia cells

AU - Tímár, J.

AU - Diczhazi, C.

AU - Bartha, I.

AU - Ladányi, A.

AU - Tarcsafalvi, A.

AU - Lapis, K.

PY - 1994

Y1 - 1994

N2 - We have analysed the mechanism of PMA-induced adhesion of the MDS human leukemia cell line. Affinity to various matrix ligands indicated that PMA induced fibronectin adhesion of MDS cells. This interaction could not be inhibited by RGDS-peptide, therefore it was most probably not mediated by integrins. Rather, both the basal and PMA-induced fibronectin adhesion of MDS cells could be inhibited by heparin and much less efficiently by chondroitin sulphate, suggesting that glycosaminoglycans of proteoglycans may be responsible for the change in adhesive phenotype. PMA stimulation of MDS cells induced a significant increase in proteoglycan biosynthesis. Studies on the glycosaminoglycan pattern of the proteoglycans showed that PMA treatment initiated a shift in glycanation of the MDS-proteoglycans from the predominant chondroitin sulphate-proteoglycans in control cells to a predominant heparan sulphate-proteoglycans in adherent cells. These data indicate that protein kinase C, the main target of PMA, may have a profound role in the regulation of glycanation pattern of proteoglycans. Furthermore, such alterations in the cellular proteoglycans may significantly affect the matrix adhesion potential of hematopoietic cells.

AB - We have analysed the mechanism of PMA-induced adhesion of the MDS human leukemia cell line. Affinity to various matrix ligands indicated that PMA induced fibronectin adhesion of MDS cells. This interaction could not be inhibited by RGDS-peptide, therefore it was most probably not mediated by integrins. Rather, both the basal and PMA-induced fibronectin adhesion of MDS cells could be inhibited by heparin and much less efficiently by chondroitin sulphate, suggesting that glycosaminoglycans of proteoglycans may be responsible for the change in adhesive phenotype. PMA stimulation of MDS cells induced a significant increase in proteoglycan biosynthesis. Studies on the glycosaminoglycan pattern of the proteoglycans showed that PMA treatment initiated a shift in glycanation of the MDS-proteoglycans from the predominant chondroitin sulphate-proteoglycans in control cells to a predominant heparan sulphate-proteoglycans in adherent cells. These data indicate that protein kinase C, the main target of PMA, may have a profound role in the regulation of glycanation pattern of proteoglycans. Furthermore, such alterations in the cellular proteoglycans may significantly affect the matrix adhesion potential of hematopoietic cells.

KW - Adhesion

KW - Leukemia cells

KW - PMA

KW - Proteoglycans

UR - http://www.scopus.com/inward/record.url?scp=0028168219&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028168219&partnerID=8YFLogxK

M3 - Article

VL - 14

SP - 1227

EP - 1231

JO - Anticancer Research

JF - Anticancer Research

SN - 0250-7005

IS - 3 A

ER -