Extracellular Matrix Elements, Cell Adhesion Molecules, and Signal Transduction in the Control of Sertoli Cell Function

Author(s):  
M. Dym
1998 ◽  
Vol 57 (9) ◽  
pp. 858-865
Author(s):  
Yasuhiro Nakamura ◽  
Munehiko Yamamoto ◽  
Sonoe Itoh ◽  
Akiko Haratake ◽  
Yuko Nakano ◽  
...  

1995 ◽  
Vol 7 (35) ◽  
pp. 205-221
Author(s):  
Maria L. Jaramillo ◽  
J. C. Bell

2020 ◽  
Vol 295 (8) ◽  
pp. 2495-2505 ◽  
Author(s):  
Michalina Janiszewska ◽  
Marina Candido Primi ◽  
Tina Izard

Homeostasis in healthy tissues strongly relies on cell-to-cell adhesion and cell-to-extracellular matrix interactions. For instance, normal epithelial cells maintain tissue structure by adhering to each other and to the extracellular matrix. The proteins that mediate these distinct interactions are collectively called cell adhesion molecules and are divided into four major groups: cadherins, integrins, selectins, and immunoglobulins. They not only physically anchor cells, but also critically integrate signaling between the extracellular microenvironment and cells. These signals include biochemical cues, as adhesion proteins can both act as ligand-activated receptors and activate mechanotransduction triggered by changes in the physical environment. Molecular mechanisms related to cell adhesion signaling have been extensively studied, especially because mutations and changes in expression of these proteins, particularly cadherins and integrins, are frequently associated with diseases ranging from developmental intellectual disability to cancer. In fact, two major hallmarks of cancer, loss of cell-to-cell adhesion and anchorage-independent growth, are both dependent on cell adhesion molecules. Despite many studies elucidating the relationships between malignant transformation and metastasis and cellular adhesion processes, several areas still await exploration. Here, we highlight recently discovered roles of adhesion molecules in collective cancer cell migration and discuss the utility of three-dimensional models in studying cell-cell adhesion. We also describe recent therapeutic approaches targeting adhesion molecules.


1998 ◽  
Vol 4 (S2) ◽  
pp. 1068-1069
Author(s):  
Ann-Marie Broome ◽  
Clarke F. Millette

Cell adhesion and cell adhesion molecules (CAMs) play a crucial role in testicular development and function. The seminiferous epithelium, the functional unit of the testis, represents a three dimensional architecture of supporting Sertoli cells (SC), and developing germ cells (GC). The seminiferous epithelium, therefore, must be receptive not only to individual cell growth and differentiation, but also to cell-cell interactions. Morphologically distinct cell-cell interactions occur between SC and GC and also between SC.[1] In general, these junctions can be categorized into three types: adhesive, occluding, and gap junctions. The orientation and function of these junctions are interaction dependent. For example, desmosome-like junctions (spot desmosomes) are found between SC and GC. These junctions are present in the basal and intermediate compartments of the testis and serve to translocate developing GC. SC-SC interactions, like the zonula occludens (tight junction), function as vectorial mediators, maintaining the blood-testis barrier and SC polarity.


2008 ◽  
Vol 4 (3) ◽  
pp. 223-234 ◽  
Author(s):  
Tet Woo Lee ◽  
Vicky W.K. Tsang ◽  
Nigel P. Birch

Research on the molecular and cellular basis of learning and memory has focused on the mechanisms that underlie the induction and expression of synaptic plasticity. There is increasing evidence that structural changes at the synapse are associated with synaptic plasticity and that extracellular matrix (ECM) components and cell adhesion molecules are associated with these changes. The functions of both groups of molecules can be regulated by proteolysis. In this article we review the roles of selected proteases and protease inhibitors in perisynaptic proteolysis of the ECM and synaptic adhesion proteins and the impact of proteolysis on synaptic modification and cognitive function.


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