Título del libro: Proteases In Physiology And Pathology
Título del capítulo: Metalloproteases in adaptative cell responses
PAVEL MONTES DE OCA BALDERAS;
Autores externos:
Idioma:
Año de publicación:
2017
Palabras clave:
"Ectodomain shedding"; ADAM; I-CLiPs; Metalloproteases; MMP; RIP; Signaling; Transmembrane molecules
Resumen:
Throughout evolution, cells have acquired molecular mechanisms that enable them to interact with and adapt to the extracellular milieu. In the last decade, ectodomain shedding (ES) has emerged as a critical sensing mechanism of the environment that may remodel cell membrane molecular repertoire, eliciting dynamic intracellular responses. ES is the proteolytic release of the extracellular domain (ectodomain) from cell membrane molecules (CMM). This proteolysis is mediated mainly by matrix metalloproteases (MMPs) or disintegrin and metal- loproteases (ADAMs). Virtually, all functional categories of CMM are subject of this proteolysis; therefore, ES is involved in most cellular processes including proliferation, apoptosis, migration, and differentiation or pathologies such as inflammation or cancer. ES releases membrane molecule's ectodomain to the extracellular space where it can play biological functions. ES of transmembrane molecules also generates membrane-attached terminal fragments comprising transmembrane and intracellular domains. These fragments may be further processed by intramembrane-cleaving proteases (i-CLiPs), a mechanism known as regulated intramembrane proteolysis (RIP), which releases molecule's intracellular domain (ICD). Contrary to the initial hypothesis, fragments that result from ES and/or RIP are not necessarily in the pathway of degradation. Instead, they may carry out specific functions that cannot be performed by full-length native molecules. Thus, ES has emerged as a switch that unmasks multifunctional activities of CMM. In this chapter, the general mechanism of ES is reviewed, and some considerations are formulated in an effort to disentangle the complexity that this proteolytic mechanism and the processing of CMM clusters represent for the understanding of cell signaling. © Springer Nature Singapore Pte Ltd. 2017. All rights reserved.
Entidades citadas de la UNAM:
ISBN:
9789811025136
Editorial:
Springer Singapore Nombre de la publicación:
Metalloproteases in adaptative cell responses
Página inicial:
121
Página final:
142
