title: Interleukin-15 signals T84 colonic epithelial cells in the absence of the interleukin-2 receptor beta-chain.
abstract: Interleukin-15 (IL-15) shares many biological functions with interleukin-2 (IL-2) due to common receptor components. IL-15 binds to the IL-2 receptor (IL-2R) beta-chain and the common gamma-chain receptor in addition to one other IL-15 binding receptor protein (IL-15R alpha). Both IL-2R beta- and gamma-chains are required to promote cell growth in hematopoietic cells. The colonic cryptlike epithelial cell line T84 contains the common gamma-chain but lacks the IL-2R beta-chain. We report IL-15R alpha-chain mRNA in T84 cells with the use of reverse transcriptase-polymerase chain reaction. T84 and normal colonic epithelial cells bind a FLAG-IL-15 fusion protein in immunoperoxidase and flow cytometric experiments. In addition, IL-15, but not IL-2, accelerates and enhances the development of transepithelial resistance across T84 monolayers in a dose-dependent fashion. We conclude that normal and T84 colonic epithelial cells express IL-15R alpha and are able to bind IL-15. IL-15 can deliver a nonproliferative functional signal in the absence of IL-2R beta-chain in T84 cells.
authors.affiliation: Department of Medicine, Beth Israel Hospital, Harvard Medical School, Boston, Massachusetts 02215, USA.
authors.forename: A C
authors.initials: AC
authors.lastname: Stevens
authors.forename: J
authors.initials: J
authors.lastname: Matthews
authors.forename: P
authors.initials: P
authors.lastname: Andres
authors.forename: V
authors.initials: V
authors.lastname: Baffis
authors.forename: X X
authors.initials: XX
authors.lastname: Zheng
authors.forename: D W
authors.initials: DW
authors.lastname: Chae
authors.forename: J
authors.initials: J
authors.lastname: Smith
authors.forename: T B
authors.initials: TB
authors.lastname: Strom
authors.forename: W
authors.initials: W
authors.lastname: Maslinski
mesh_terms: D002455:Cell Division / Q000187:drug effects; D003106:Colon / Q000473:pathology / Q000503:physiopathology*; D004305:Dose-Response Relationship, Drug; D017097:Electric Impedance; D005656:Fungal Proteins; D006801:Humans; D019409:Interleukin-15 / Q000235:genetics / Q000494:pharmacology / Q000502:physiology*; D007413:Intestinal Mucosa / Q000473:pathology / Q000503:physiopathology*; D009183:Mycotoxins / Q000378:metabolism; D009842:Oligopeptides; D010455:Peptides / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D015375:Receptors, Interleukin-2 / Q000172:deficiency* / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D011994:Recombinant Proteins; D015398:Signal Transduction; D014407:Tumor Cells, Cultured
chemical_list: D005656:Fungal Proteins; C085669:HMK protein, Hansenula; D019409:Interleukin-15; D009183:Mycotoxins; D009842:Oligopeptides; D010455:Peptides; D012333:RNA, Messenger; D015375:Receptors, Interleukin-2; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; C085706:FLAG peptide