Similar and Divergent Patterns in the Regulation of Matrix Metalloproteinase-1 (MMP-1) and Tissue Inhibitor of MMP-1 Gene Expression in Benign and Malignant Human Thyroid Cells1
Autor: | M. B. Resnick, Zaki Kraiem, Sigal Korem |
---|---|
Rok vydání: | 1999 |
Předmět: |
medicine.medical_specialty
Endocrinology Diabetes and Metabolism Biochemistry (medical) Clinical Biochemistry Proteolytic enzymes Matrix metalloproteinase Biology Biochemistry Extracellular matrix chemistry.chemical_compound Endocrinology chemistry Epidermal growth factor Internal medicine Gene expression medicine Phorbol Cancer research Tyrosine kinase Protein kinase C |
Zdroj: | The Journal of Clinical Endocrinology & Metabolism. 84:3322-3327 |
ISSN: | 1945-7197 0021-972X |
DOI: | 10.1210/jcem.84.9.5984 |
Popis: | An imbalance between the activity of matrix metalloproteinases (MMPs) (proteolytic enzymes that degrade protein components of the extracellular matrix) and their inhibitors, the tissue inhibitors of metalloproteinases (TIMPs), may be one of the mechanisms responsible for tumor cell invasion. We have investigated the regulation of MMP-1 and TIMP-1 gene expression in benign and malignant (follicular, anaplastic, and papillary) human thyroid cells. As expected of cells with invasive potential, detectable MMP-1 messenger RNA (mRNA) levels were observed in malignant cells under basal conditions, in contrast to undetectable levels in benign cells. Exposure of these cells, for 1 h, to the active phorbol ester, phorbol 12-myristate 13-acetate (TPA, 100 nmol/L), acting via protein kinase C (PKC), elicited an increase in MMP-1 mRNA, with a peak stimulation after a 3- to 4-h culture period. Epidermal growth factor (EGF, 25 ng/mL), however, acting via protein tyrosine kinase (PTK), stimulated such gene expression in ... |
Databáze: | OpenAIRE |
Externí odkaz: |