Extracellular matrix proteins and their receptors in the normal, hyperplastic and neoplastic breast.
We studied by immunohistochemistry, the distribution of tenascin (Ten), cellular fibronectin (cFn), laminin and certain pertinent extracellular matrix protein receptors in normal human female breast, variants of fibrocystic disease (FCD), benign tumors, and ductal and lobular carcinomas. Monoclonal antibodies (mAb) to Ten, extradomain A containing cFn (EDAcFn), A and B chains of laminin, and beta-1 (beta-1) and different alpha subunits of intergrins were used. In in-situ ductal and lobular carcinomas, laminin staining had focal gaps, Ten-immunoreactivity displayed periductal or periacinar bands, and cFn showed broad and intense periductal staining; strong reactions for beta-1 and alpha-6 were noted in the basal cytoplasm of non-neoplastic myoepithelial cells while few tumor cells stained weakly. In infiltrating ductal and lobular carcinomas (IDC, ILC), laminin reactivity was weak, uneven or absent around neoplastic clusters whereas stromal staining for Ten and cFn was extensive and strong. In most IDC, moderate beta-1 and alpha-6 staining involved variable subpopulations; one mucinous carcinoma stained strongly and diffusely. In 20-40% of cells in ILC, beta-1 and alpha-6 were localized in delicate, ramified cytoplasmic processes. Indirect immunofluorescence studies with mAbs to other alpha-integrin subunits suggest that in various breast carcinomas only alpha-3 is expressed in tumor cells and that the vessels contained alpha-1 integrin. As compared with the normal breast, FCD and benign tumors, reactivity for Ten and cFn is increased in breast carcinomas while laminin is attenuated and decreased or absent; yet, Ten cannot be regarded as a carcinoma marker since it can be detected in benign tumors, FCD, and even in the normal breast.(ABSTRACT TRUNCATED AT 250 WORDS)
Gould
V E
VE
Department of Pathology, Rush Medical College, Chicago, IL 60612-3684.
Koukoulis
G K
GK
Virtanen
I
I
D000232:Adenofibroma / Q000737:chemistry; D015415:Biomarkers; D001940:Breast / Q000737:chemistry* / Q000196:embryology / Q000473:pathology; D001943:Breast Neoplasms / Q000737:chemistry*; D002277:Carcinoma / Q000737:chemistry; D002285:Carcinoma, Intraductal, Noninfiltrating / Q000737:chemistry; D015816:Cell Adhesion Molecules, Neuronal / Q000032:analysis; D016326:Extracellular Matrix Proteins / Q000032:analysis*; D005260:Female; D005348:Fibrocystic Breast Disease / Q000378:metabolism*; D005353:Fibronectins / Q000032:analysis; D006801:Humans; D006965:Hyperplasia; D016023:Integrins / Q000032:analysis*; D007797:Laminin / Q000032:analysis; D010641:Phenotype; D003557:Phyllodes Tumor / Q000737:chemistry; D019063:Tenascin
D015415:Biomarkers; D015816:Cell Adhesion Molecules, Neuronal; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D016023:Integrins; D007797:Laminin; D019063:Tenascin