Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems.
Serpins compose the largest superfamily of peptidase inhibitors and are well known as regulators of hemostasis and thrombolysis. Studies using model organisms, from plants to vertebrates, now show that serpins and their unique inhibitory mechanism and conformational flexibility are exploited to control proteolysis in molecular pathways associated with cell survival, development, and host defense. In addition, an increasing number of non-inhibitory serpins are emerging as important elements within a diversity of biological systems by serving as chaperones, hormone transporters, or anti-angiogenic factors.
Silverman
Gary A
GA
Department of Pediatrics and Cell Biology and Physiology, Children's Hospital of Pittsburgh and Magee-Womens Hospital, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15201, USA. gsilverman@upmc.edu
Whisstock
James C
JC
Bottomley
Stephen P
SP
Huntington
James A
JA
Kaiserman
Dion
D
Luke
Cliff J
CJ
Pak
Stephen C
SC
Reichhart
Jean-Marc
JM
Bird
Phillip I
PI
D000818:Animals; D017173:Caenorhabditis elegans; D016923:Cell Death; D002454:Cell Differentiation; D002470:Cell Survival; D004331:Drosophila melanogaster; D006706:Homeostasis; D006801:Humans; D007113:Immunity, Innate; D051379:Mice; D008822:Mice, Transgenic; D008954:Models, Biological; D010641:Phenotype; D015843:Serpins / Q000737:chemistry / Q000502:physiology*; D019076:Transgenes
D015843:Serpins