Extracellular matrix proteins and myofibroblasts in granulomas of sarcoidosis, atypical mycobacteriosis, and tuberculosis of the lung.
Sarcoidosis, atypical mycobacteriosis, and tuberculosis are common diseases of human lung with a typical feature of formation of granulomas. The structure of granulomas has not been elucidated completely. We studied the expression of tenascin-C, precursor proteins of collagens I and III, and the presence of myofibroblasts in granulomas of sarcoidosis, atypical mycobacteriosis, and tuberculosis of human lung. Twenty-five histologic samples of lung were analyzed by immunohistochemistry using antibodies to tenascin-C and aminoterminal propeptides of collagens I and III. To identify the myofibroblast-type cells in granulomas, the sections were also stained with antibodies against alpha-smooth muscle actin, vimentin, and desmin. In every case, tenascin-C and precursor proteins of collagens I and III were expressed around granulomas. Precursor protein of collagen I was expressed also within them. In tuberculosis and atypical mycobacteriosis, expression of tenascin-C and precursor protein of collagen I was stronger than in sarcoidosis. The cells demarcating granulomas and, thus, colocalizing with tenascin-C and both collagen precursors were positive for alpha-smooth muscle actin and vimentin, which suggests that these cells are myofibroblasts. They were also more abundantly present in tuberculosis and atypical mycobacteriosis, as suggested by alpha-smooth muscle actin staining. We concluded that tenascin-C and precursor proteins of collagens I and III are expressed around granulomas in sarcoidosis, atypical mycobacteriosis, and tuberculosis of the lung; and furthermore, their expression colocalize with the expression of myofibroblasts. Our results further point to the fact that fibrogenesis and matrix turnover is stronger in tuberculosis and atypical mycobacteriosis than in sarcoidosis.
Kaarteenaho-Wiik
Riitta
R
Department of Internal Medicine, University of Oulu and Oulu University Hospital, PO Box 5000, FIN-90014 Oulu, Finland. riitta.kaarteenaho-wiik@oulu.fi
Sademies
Outi
O
Pääkkö
Paavo
P
Risteli
Juha
J
Soini
Ylermi
Y
D000199:Actins / Q000032:analysis; D015415:Biomarkers / Q000032:analysis; D016326:Extracellular Matrix Proteins / Q000032:analysis*; D005260:Female; D005347:Fibroblasts / Q000737:chemistry / Q000473:pathology*; D006099:Granuloma / Q000378:metabolism / Q000473:pathology*; D006801:Humans; D007150:Immunohistochemistry; D008168:Lung / Q000737:chemistry / Q000473:pathology; D008297:Male; D009130:Muscle, Smooth / Q000737:chemistry / Q000473:pathology; D009165:Mycobacterium Infections, Nontuberculous / Q000378:metabolism / Q000473:pathology*; D010446:Peptide Fragments / Q000032:analysis; D011347:Procollagen / Q000032:analysis; D017565:Sarcoidosis, Pulmonary / Q000378:metabolism / Q000473:pathology*; D019063:Tenascin / Q000032:analysis; D014397:Tuberculosis, Pulmonary / Q000378:metabolism / Q000473:pathology*
D000199:Actins; D015415:Biomarkers; D016326:Extracellular Matrix Proteins; D010446:Peptide Fragments; D011347:Procollagen; D019063:Tenascin; C047202:procollagen Type I N-terminal peptide; C041876:procollagen Type III-N-terminal peptide