scholarly journals Subcellular Distribution and Cell Cycle-Associated Expression of New Member of S100 Protein Family (S100C)

1993 ◽  
Vol 61 ◽  
pp. 138
Author(s):  
Takuya Komada ◽  
Toshimichi Yoshida ◽  
Kaname Nakatani ◽  
Toshio Tanaka
1989 ◽  
Vol 108 (2) ◽  
pp. 569-578 ◽  
Author(s):  
J R Glenney ◽  
M S Kindy ◽  
L Zokas

A low molecular mass protein which we term S100L was isolated from bovine lung. S100L possesses many of the properties of brain S100 such as self association, Ca++-binding (2 sites per subunit) with moderate affinity, and exposure of a hydrophobic site upon Ca++-saturation. Antibodies to brain S100 proteins, however, do not cross react with S100L. Tryptic peptides derived from S100L were sequenced revealing similarity to other members of the S100 family. Oligonucleotide probes based on these sequences were used to screen a cDNA library derived from a bovine kidney cell line (MDBK). A 562-nucleotide cDNA was sequenced and found to contain the complete coding region of S100L. The predicted amino acid sequence displays striking similarity, yet is clearly distinct from other members of the S100 protein family. Polyclonal and monoclonal antibodies were raised against S100L and used to determine the tissue and subcellular distribution of this molecule. The S100L protein is expressed at high levels in bovine kidney and lung tissue, low levels in brain and intestine, with intermediate levels in muscle. The MDBK cell line was found to contain both S100L and the calpactin light chain, another member of this protein family. S100L was not found associated with a higher molecular mass subunit in MDBK cells while the calpactin light chain was tightly bound to the calpactin heavy chain. Double label immunofluorescence microscopy confirmed the observation that the calpactin light chain and S100L have a different distribution in these cells.


Oncotarget ◽  
2018 ◽  
Vol 9 (49) ◽  
pp. 29064-29081 ◽  
Author(s):  
Patrizia Cancemi ◽  
Miriam Buttacavoli ◽  
Gianluca Di Cara ◽  
Nadia Ninfa Albanese ◽  
Serena Bivona ◽  
...  

2021 ◽  
Vol 48 (3) ◽  
Author(s):  
Shun Yao ◽  
Xingyue Yang ◽  
Jiaxing An ◽  
Hai Jin ◽  
Guorong Wen ◽  
...  

1992 ◽  
Vol 58 ◽  
pp. 240
Author(s):  
Toshio Tanaka ◽  
Hisataka Ohta ◽  
Toshiva Sasaki ◽  
Michiko Haka ◽  
Osamu Hiranka ◽  
...  

2016 ◽  
Vol 310 (8) ◽  
pp. E587-E596 ◽  
Author(s):  
Soni Shaikh ◽  
Rodrigo Troncoso ◽  
Alfredo Criollo ◽  
Roberto Bravo-Sagua ◽  
Lorena García ◽  
...  

Calcium signaling plays a crucial role in a multitude of events within the cardiomyocyte, including cell cycle control, growth, apoptosis, and autophagy. With respect to calcium-dependent regulation of autophagy, ion channels and exchangers, receptors, and intracellular mediators play fundamental roles. In this review, we discuss calcium-dependent regulation of cardiomyocyte autophagy, a lysosomal mechanism that is often cytoprotective, serving to defend against disease-related stress and nutrient insufficiency. We also highlight the importance of the subcellular distribution of calcium and related proteins, interorganelle communication, and other key signaling events that govern cardiomyocyte autophagy.


PLoS ONE ◽  
2016 ◽  
Vol 11 (10) ◽  
pp. e0164740 ◽  
Author(s):  
Lucas C. Wheeler ◽  
Micah T. Donor ◽  
James S. Prell ◽  
Michael J. Harms

2018 ◽  
Vol 69 (4) ◽  
pp. 622-635.e6 ◽  
Author(s):  
Cindy Meyer ◽  
Aitor Garzia ◽  
Michael Mazzola ◽  
Stefanie Gerstberger ◽  
Henrik Molina ◽  
...  

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