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

1996 ◽  
Vol 44 (1) ◽  
pp. 49-56 ◽  
Author(s):  
T Muramatsu ◽  
S Hashimoto ◽  
M Shimono
Keyword(s):  
Western Blot ◽  
Gap Junction ◽  
Immunofluorescence Microscopy ◽  
Acinar Cells ◽  
Myoepithelial Cells ◽  
Secretory Function ◽  
Submandibular Glands ◽  
Gap Junction Proteins ◽  
Gap Junctional ◽  
Junction Proteins

We examined the expression and localization of the gap junction proteins connexin32 and 43 in rat submandibular and sublingual glands. Western blot analysis with anti-connexin32 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 submandibular glands. No positive spots for both connexins were detected between duct cells in either gland. Immunoelectron microscopy revealed that connexin32 was localized to the gap junctional membranes between acinar cells. Immunolabeling for connexin43 was located on the gap junctions between thin processes of myoepithelial cells. These results suggest that connexin32 of the gap junction is associated with regulation of the secretory function of acinar cells and that connexin43 is associated with that of contraction of the myoepithelial cells in rat salivary glands.

scholarly journals The tumor promoter 12-O-tetradecanoylphorbol-13-acetate and the ras oncogene modulate expression and phosphorylation of gap junction proteins.

1991 ◽  
Vol 11 (10) ◽  
pp. 5364-5371 ◽  
Author(s):  
J L Brissette ◽  
N M Kumar ◽  
N B Gilula ◽  
G P Dotto
Keyword(s):  
Gap Junction ◽  
Intercellular Communication ◽  
Molecular Mechanisms ◽  
Serine Phosphorylation ◽  
Tumor Promoter ◽  
Gap Junctional Intercellular Communication ◽  
Beta 2 ◽  
Gap Junction Proteins ◽  
Gap Junctional ◽  
Junction Proteins

Gap junctional intercellular communication is inhibited in response to tumor promoters and oncogene transformation, suggesting that loss of this function is an important step in tumor formation. To elucidate the molecular mechanisms responsible for this inhibition, we examined the expression of gap junction proteins and mRNA in mouse primary keratinocytes after treatment with the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) and/or ras transformation. During normal cell growth, keratinocytes expression the alpha 1 (connexin 43) and beta 2 (connexin 26) proteins. Within 5 min of TPA treatment, the alpha 1 protein became rapidly phosphorylated on serine residues and its expression was dramatically reduced by 24 h. The beta 2 protein, after an initial increase in expression, was also significantly reduced 24 h after treatment with TPA. ras transformation caused changes similar to those induced by TPA. The alpha 1 protein underwent an increase in serine phosphorylation, although its expression declined only slightly, while beta 2 expression was greatly reduced. The effects of TPA and ras on alpha 1 expression were additive; treatment of ras-transformed cells with TPA resulted in increased alpha 1 phosphorylation, with greatly decreased protein levels, much lower than those generated by either agent alone. These data provide a likely explanation for the similar and synergistic inhibition of gap junctional intercellular communication by phorbol esters and ras.

The tumor promoter 12-O-tetradecanoylphorbol-13-acetate and the ras oncogene modulate expression and phosphorylation of gap junction proteins

1991 ◽  
Vol 11 (10) ◽  
pp. 5364-5371
Author(s):  
J L Brissette ◽  
N M Kumar ◽  
N B Gilula ◽  
G P Dotto
Keyword(s):  
Gap Junction ◽  
Intercellular Communication ◽  
Molecular Mechanisms ◽  
Serine Phosphorylation ◽  
Tumor Promoter ◽  
Gap Junctional Intercellular Communication ◽  
Beta 2 ◽  
Gap Junction Proteins ◽  
Gap Junctional ◽  
Junction Proteins

Gap junctional intercellular communication is inhibited in response to tumor promoters and oncogene transformation, suggesting that loss of this function is an important step in tumor formation. To elucidate the molecular mechanisms responsible for this inhibition, we examined the expression of gap junction proteins and mRNA in mouse primary keratinocytes after treatment with the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) and/or ras transformation. During normal cell growth, keratinocytes expression the alpha 1 (connexin 43) and beta 2 (connexin 26) proteins. Within 5 min of TPA treatment, the alpha 1 protein became rapidly phosphorylated on serine residues and its expression was dramatically reduced by 24 h. The beta 2 protein, after an initial increase in expression, was also significantly reduced 24 h after treatment with TPA. ras transformation caused changes similar to those induced by TPA. The alpha 1 protein underwent an increase in serine phosphorylation, although its expression declined only slightly, while beta 2 expression was greatly reduced. The effects of TPA and ras on alpha 1 expression were additive; treatment of ras-transformed cells with TPA resulted in increased alpha 1 phosphorylation, with greatly decreased protein levels, much lower than those generated by either agent alone. These data provide a likely explanation for the similar and synergistic inhibition of gap junctional intercellular communication by phorbol esters and ras.

Innexin genes and gap junction proteins in the locust frontal ganglion

2009 ◽  
Vol 39 (3) ◽  
pp. 224-233 ◽  
Author(s):  
Sarit Anava ◽  
David Rand ◽  
Yael Zilberstein ◽  
Amir Ayali
Keyword(s):  
Gap Junction ◽  
Frontal Ganglion ◽  
Gap Junction Proteins ◽  
Junction Proteins

Gap-junction proteins and communication in human epidermis

Gap Junctions ◽  
1993 ◽  
pp. 225-231 ◽  
Author(s):  
D. SALOMON ◽  
E. MASGRAU ◽  
S. VISCHER ◽  
J.-H. SAURAT ◽  
M. CHANSON ◽  
...  
Keyword(s):  
Gap Junction ◽  
Human Epidermis ◽  
Gap Junction Proteins ◽  
Junction Proteins
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