G
Guadalupe A. Limjuco
Researcher at Merck & Co.
Publications - 20
Citations - 4286
Guadalupe A. Limjuco is an academic researcher from Merck & Co.. The author has contributed to research in topics: Peptide sequence & Peptide. The author has an hindex of 14, co-authored 20 publications receiving 4131 citations.
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Journal ArticleDOI
A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes.
Nancy A. Thornberry,Herbert G. Bull,Jimmy R. Calaycay,Kevin T. Chapman,Andrew D. Howard,Matthew J. Kostura,Douglas K. Miller,Susan M. Molineaux,Jeffrey R. Weidner,John G. Aunins,Keith O. Elliston,Julia M. Ayala,Francesca J. Casano,Jayne Chin,Gloria J.-F. Ding,Linda A. Egger,Erin P. Gaffney,Guadalupe A. Limjuco,Oksana C. Palyha,S.M. Raju,Anna M. Rolando,J. Paul Salley,Ting-Ting Yamin,Terry D. Lee,John E. Shively,Malcolm MacCross,Richard A. Mumford,John A. Schmidt,Michael J. Tocci +28 more
TL;DR: Purification and cloning of the complementary DNA indicates that IL-lβ-converting enzyme is composed of two nonidentical subunits that are derived from a single proenzyme, possibly by autoproteolysis.
Journal ArticleDOI
Identification of a monocyte specific pre-interleukin 1 beta convertase activity
Matthew J. Kostura,Michael J. Tocci,Guadalupe A. Limjuco,Jayne Chin,Patricia M. Cameron,Andrew G. Hillman,Nicole A. Chartrain,John A. Schmidt +7 more
TL;DR: In this paper, the authors showed that only extracts derived from human monocytes and THP.1 cells were capable of cleaving precursor IL-1 beta to authentic mature IL 1 β.
Journal Article
IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1 beta precursor at two distinct sites and does not cleave 31-kDa IL-1 alpha.
Andrew D. Howard,Matthew J. Kostura,Nancy A. Thornberry,Gloria J.-F. Ding,Guadalupe A. Limjuco,Jeffrey R. Weidner,J P Salley,Kristin A. Hogquist,David D. Chaplin,David D. Chaplin,Richard A. Mumford +10 more
TL;DR: Results show that ICE is a highly specific IL-1 beta convertase with absolute requirements for Asp in P1 and a small hydrophobic amino acid in P2', and not like any other eukaryotic protease.
Journal ArticleDOI
The interleukin-1 beta-converting enzyme (ICE) is localized on the external cell surface membranes and in the cytoplasmic ground substance of human monocytes by immuno-electron microscopy.
Irwin I. Singer,S Scott,Jayne Chin,Ellen K. Bayne,Guadalupe A. Limjuco,Jeffrey R. Weidner,Douglas K. Miller,Kevin T. Chapman,Matthew J. Kostura +8 more
TL;DR: The data suggests that mature IL-1 beta is generated via cleavage of the 31-kD inactive cytoplasmic IL- 1 beta precursor by ICE after association with the plasma membrane during secretion.
Journal ArticleDOI
Interleukin 1 beta is localized in the cytoplasmic ground substance but is largely absent from the Golgi apparatus and plasma membranes of stimulated human monocytes.
TL;DR: The results suggest that IL-1 beta is not anchored on the plasma membrane, and that its secretion occurs by a novel mechanism that does not use a secretory leader sequence, nor the classical secretory pathway involving the ER and Golgi apparatus.