Differential Expression of Myoepithelial Markers in Salivary, Sweat and Mammary Glands
Open Access
- 1 January 2000
- journal article
- research article
- Published by SAGE Publications in International Journal of Surgical Pathology
- Vol. 8 (1) , 29-37
- https://doi.org/10.1177/106689690000800108
Abstract
Myoepithelial cells (MECs) are contractile elements showing a combined epithelial and smooth muscle phenotype. Among the numerous immunohistochemical markers employed to detect MECs, smooth muscle actin (SMA) is the most widely used. Recently, other markers of smooth muscle differentiation have been demonstrated in MECs, such as calponin, heavy caldesmon (h-caldesmon), and smooth muscle myosin heavy chain (SMM-HC). In the present study normal salivary, mammary, and sweat glands have been studied with four markers of smooth muscle differentiation (SMA, calponin, h-caldesmon, and SMM-HC). The four markers were differentially expressed in the various types of glands. In parotid glands MECs mainly expressed calponin and caldesmon; in submandibular and in cutaneous apocrine and eccrine glands, MECs strongly expressed SMA, calponin, and caldesmon; in minor salivary glands all four markers were equally strongly expressed; and in mammary glands SMA, calponin, and SMM-HC were present both in periductal and periacinar MECs while caldesmon was present in periductal MECs only. In addition to MECs, SMA stained stromal myofibroblasts, sometimes hampering the identification of MECs. Among the other markers, calponin stained only rare stromal myofibroblasts, while caldesmon and SMM-HC were confined to MECs. In conclusion, these latter markers are very useful for identifying MECs. It is suggested that the differential expression of smooth muscle contractile proteins might reflect different functions of MECs in the various sites.Keywords
This publication has 20 references indexed in Scilit:
- Interaction of caldesmon with actin subdomain‐2European Journal of Biochemistry, 1998
- Does Calponin Interact with Caldesmon?Published by Elsevier ,1997
- Antibodies to Novel Myoepithelium-Associated Proteins Distinguish Benign Lesions and Carcinoma in Situ From Invasive Carcinoma of the BreastApplied Immunohistochemistry & Molecular Morphology, 1997
- Myoepithelioma: Definitions and Diagnostic CriteriaUltrastructural Pathology, 1995
- Calponin and SM22 as differentiation markers of smooth muscle: spatiotemporal distribution during avian embryonic developmentDifferentiation, 1993
- Identification of a novel smooth muscle myosin heavy chain cDNA: isoform diversity in the S1 head regionAmerican Journal of Physiology-Cell Physiology, 1993
- Tissue-specific and developmentally regulated alternative splicing of a visceral isoform of smooth muscle myosin heavy chainNucleic Acids Research, 1993
- Cloning of cDNAs encoding human caldesmonsGene, 1992
- Developmental changes in actin and myosin heavy chain isoform expression in smooth muscleArchives of Biochemistry and Biophysics, 1991
- Specific demonstration of myoepithelial cells by anti-alpha smooth muscle actin antibody.Journal of Histochemistry & Cytochemistry, 1988