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논문 기본 정보

자료유형
학술저널
저자정보
Joong-Kook Choi (Chungbuk National University) Eun-Ju Lee (Chungbuk National University) Kwan-Sik Park (Chungbuk National University) 전인숙 (Chungbuk National University) Jae-Woon Choi (Chungbuk National University) Sang Jeon Lee (Chungbuk National University Hospita) Hyun E. Choy (Chonnam National University) Ki-Duk Song (Chonbuk National University Korea) Hak-Kyo Lee (Chonbuk National University Korea)
저널정보
한국분자세포생물학회 Molecules and Cells Molecules and Cells 제39권 제7호
발행연도
2016.7
수록면
566 - 572 (7page)
DOI
http://dx.doi.org/10.14348/molcells.2016.0112

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Lysosomes are cellular organelles containing diverse classes of catabolic enzymes that are implicated in diverse cellular processes including phagocytosis, autophagy, lipid transport, and aging. Lysosome-associated membrane proteins (LAMP-1 and LAMP-2) are major glycoproteins important for maintaining lysosomal integrity, pH, and catabolism. LAMP-1 and LAMP-2 are constitutively expressed in Salmonella-infected cells and are recruited to Salmonella-containing vacuoles (SCVs) as well as Salmonella-induced filaments (Sifs) that promote the survival and proliferation of the Salmonella. LAMP-3, also known as DC-LAMP/CD208, is a member of the LAMP family of proteins, but its role during Salmonella infection remains unclear. DNA microarray analysis identified LAMP-3 as one of the genes responding to LPS stimulation in THP-1 macrophage cells. Subsequent analyses reveal that LPS and Salmonella induced the expression of LAMP-3 at both the transcriptional and translational levels. Confocal Super resolution N-SIM imaging revealed that LAMP-3, like LAMP-2, shifts its localization from the cell surface to alongside Salmonella. Knock-down of LAMP-3 by specific siRNAs decreased the number of Salmonella recovered from the infected cells. Therefore, we conclude that LAMP-3 is induced by Salmonella infection and recruited to the Salmonella pathogen for intracellular proliferation.

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