A scanning electron microscope study of myoepithelial cells in exocrine glands

Nagato, Toshikazu; Yoshida, Hiroki; Yoshida, Aichi; Uehara, Yasuo

doi:10.1007/bf00219918

Cited by 95 publications

(66 citation statements)

References 21 publications

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“…We measured the numbers of fluorescence spots for CX43 in SMG and S E , and we found that the differences between the two glands were statistically significant at p = 0.05. These results may be related to the differences in the ... degree of development and volume of myoepithelial cells shown by SEM (Nagato et al, 1980) in both glands. Our results showing the Presence of many spots of cx43 between myoepithelial cells suggest that coupling to coordinate contraction of myoepithelial cells plays an important role in expelling the viscous materials from the acinar lumen in the SLG.…”

Section: Discussionmentioning

confidence: 86%

Differential expression of gap junction proteins connexin32 and 43 in rat submandibular and sublingual glands.

Muramatsu¹,

Hashimoto²,

Shimono³

1996

J Histochem Cytochem.

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We examined the expression and localization of the gap junction proteins connexin32 and 43 in rat submandibular and sublingual glands. Westem blot analysis with anti-conne~in32 and 43 antibodies showed bands of approximately 27 KD and 43 KD, respectively, in both glands. Immunofluorescence microscopy demonstrated the presence of reactive spots for connexin32 between acinar cells in both glands. The frequency of connexin32-positive spots in the submandibular glands was approximately equal to that in the sublingual glands. In contrast, reactive spots for connexin43 were observed at the periphery of the alveolar structures in both glands. The connexin43-positive spots in the sublingual glands were more frequent and larger than those in the sub-

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Section: Discussionmentioning

confidence: 86%

Differential expression of gap junction proteins connexin32 and 43 in rat submandibular and sublingual glands.

Muramatsu¹,

Hashimoto²,

Shimono³

1996

J Histochem Cytochem.

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“…After a graded alcohol dehydration and two xylene-clearing stages, the sections were stained with conventional hematoxylin-eosin reagents. For electron microscopy, the mammary glands were processed, embedded, sectioned, and examined using previously described methods (24,51).…”

Section: Generation and Analysis Of Mkl1mentioning

confidence: 99%

Acute Myeloid Leukemia-Associated Mkl1 (Mrtf-a) Is a Key Regulator of Mammary Gland Function

Sun¹,

Boyd

Xu³

et al. 2006

Molecular and Cellular Biology

154

147

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Transcription of immediate-early genes-as well as multiple genes affecting muscle function, cytoskeletal integrity, apoptosis control, and wound healing/angiogenesis-is regulated by serum response factor (Srf). Extracellular signals regulate Srf in part via a pathway involving megakaryoblastic leukemia 1 (Mkl1, also known as myocardin-related transcription factor A [Mrtf-a]), which coactivates Srf-responsive genes downstream of Rho GTPases. Here we investigate Mkl1 function using gene targeting and show the protein to be essential for the physiologic preparation of the mammary gland during pregnancy and the maintenance of lactation. Lack of Mkl1 causes premature involution and impairs expression of Srf-dependent genes in the mammary myoepithelial cells, which control milk ejection following oxytocin-induced contraction. Despite the importance of Srf in multiple transcriptional pathways and widespread Mkl1 expression, the spectrum of abnormalities associated with Mkl1 absence appears surprisingly restricted.Megakaryoblastic leukemia 1 (MKL1) was initially identified in acute megakaryoblastic leukemias (AMKLs) that occur in infants and young children due to its involvement in the RBM15-MKL1 fusion protein created by the t(1;22) chromosomal translocation found uniquely in these leukemias (41, 48). As a result of this translocation, the MKL1 gene (alternatively known as MAL [megakaryocytic acute leukemia], MRTF-A

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“…Comparing the results in this study with those in our previous study, the frequency of CX43 in PGs was definitely lower than that in both submandibular and sublingual glands. It is well established that myoepithelial cells invest only the intercalated ducts in the mature rat PG, although their processes often extend onto adjacent portions of acini and striated ducts [7,19]. Thus, the observed localization of CX43 around the intercalated V.…”

Section: Discussionmentioning

confidence: 93%