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Regulation of lewis lung carcinoma invasion and metastasis by protein kinase A
Author(s) -
Young M. Rita I.,
Montpetit Michelle,
Lozano Yvonne,
Djordjevic Andelka,
Devata Sandeep,
Matthews John P.,
Yedavallli Sreedhar,
Chejfec Gregorio
Publication year - 1995
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910610118
Subject(s) - lewis lung carcinoma , transfection , in vivo , protein kinase a , in vitro , protein subunit , cancer research , metastasis , mutant , biology , kinase , cell culture , microbiology and biotechnology , cancer , gene , biochemistry , genetics
Metastatic Lewis lung carcinoma (LLC‐LN7) cells have increased protein kinase A (PKA) activity and are more invasive in vitro than are non‐metastatic (LLC‐C8) cells. To determine whether PKA mediates the in vitro invasiveness and in vivo metastatic capabilities of these tumor cells, the LLC variants were stably transfected to over‐express the C α subunit of PKA, and thus to have increased PKA activity, or to express a mutant cAMP‐resistant PKA R lα subunit which blocks PKA activation. Wild‐type LLC‐LN7 tumor cells were invasive in vitro and in vivo , recurred after tumor excision and metastasized to the lungs. However, they lost these properties after transfection to express the mutant R lα that blocks PKA activation. The non‐invasive, non‐recurring and non‐metastatic LLC‐C8 cells gained the capacity to invade, to recur following tumor excision and to metastasize when transfected to express the PKA C α subunit. © 1995 Wiley‐Liss, Inc .