[Expression pattern of invasion-related molecules in brain tumors of different origin].
Tumor cell invasion into the surrounding brain tissue is mainly responsible for the failure of radical surgical resection and successful treatment, with tumor recurrence as microdisseminated disease. Epidermal growth factor receptors (EGFRs), integrins and their ligands in the extracellular matrix (ECM) predominantly participate in the invasion process, including the cell adhesion to the surrounding microenvironment and cell migration. The extent of infiltration of the surrounding brain tissue by malignant tumors strongly depends on the tumor cell type. Malignant gliomas show much more intensive peritumoral invasion than do metastatic tumors. In this study, the mRNA expression of 29 invasion-related molecules (18 cell membrane receptors or receptor subunits (EGFRs and integrins) and 11 ECM components: collagens, laminins and fibronectin) was investigated by quantitative reverse transcriptase-polymerase chain reaction. Fresh frozen human tissue samples from glioblastoma (GBM) and intracerebral bronchial adenocarcinoma metastases (five pieces from each) were evaluated. Significant differences were established in six of the 29 molecules (ErbB1, 2, 3, integrins alpha3, 7 and beta1). To confirm our results at the protein level, immunohistochemical analysis of nine molecules was performed. The staining intensity differed definitely in the case of ErbB1, 2 and integrins alpha3 and beta1. Determining the differences in invasion-related molecules in tumors of different origin can help identify the exact molecular mechanisms that facilitate peritumoral infiltration by glioblastoma cells. These results should allow the selection of target molecules for potential chemotherapeutic agents directed against highly invasive malignant gliomas.
Debreceni Egyetem Orvos- és Egészségtudományi Centrum Idegsebészeti Klinika, Debrecen.
Miklós
M
Petrás
Gábor
G
Hutóczki
Imre
I
Varga
György
G
Vereb
János
J
Szöllosi
László
L
Bognár
Péter
P
Ruszthi
Annamária
A
Kenyeres
Judit
J
Tóth
Zoltán
Z
Hanzély
Beáta
B
Scholtz
Almos
A
Klekner
D000199:Actins / Q000032:analysis; D000599:Amino Acids, Diamino / Q000032:analysis; D014408:Biomarkers, Tumor / Q000032:analysis* / Q000235:genetics / Q000276:immunology; D001932:Brain Neoplasms / Q000378:metabolism* / Q000473:pathology* / Q000601:surgery; D003094:Collagen / Q000032:analysis; D066246:ErbB Receptors / Q000032:analysis; D005353:Fibronectins / Q000032:analysis; D015972:Gene Expression Regulation, Neoplastic; D005909:Glioblastoma / Q000378:metabolism / Q000473:pathology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000032:analysis; D006801:Humans; D007150:Immunohistochemistry; D039001:Integrin alpha Chains / Q000032:analysis; D039641:Integrin beta Chains / Q000032:analysis; D019394:Ki-67 Antigen / Q000032:analysis; D009361:Neoplasm Invasiveness; D012333:RNA, Messenger / Q000032:analysis; D018719:Erb-b2 Receptor Tyrosine Kinases / Q000032:analysis; D020893:Receptor, ErbB-3 / Q000032:analysis; D066247:Receptor, ErbB-4
D000199:Actins; D000599:Amino Acids, Diamino; D014408:Biomarkers, Tumor; D003094:Collagen; D066246:ErbB Receptors; D005353:Fibronectins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D039001:Integrin alpha Chains; D039641:Integrin beta Chains; D019394:Ki-67 Antigen; D012333:RNA, Messenger; D018719:Erb-b2 Receptor Tyrosine Kinases; D020893:Receptor, ErbB-3; D066247:Receptor, ErbB-4; C045397:laminine; C587689:ERBB4 protein, human