Key result
Confocal microscopy and immunoblot analysis demonstrated that TIARP co-localizes with caveolin-1 as patches at the plasma membrane of 3T3-L1 adipocytes.
No immediate clinical implications; leaves open TIARP's functional role in adipocyte caveolae.
We previously identified TIARP (TNF(alpha)-induced adipose-related protein, where TNF(alpha) stands for tumour necrosis factor alpha), a novel plasma-membrane protein that is induced during 3T3-L1 preadipocytes differentiation by TNF(alpha). Whereas the biological function of TIARP is currently unknown, its protein sequence is reminiscent of transporter protein and/or NAD(P)/NAD(P)H-dependent oxidoreductase activities. We hypothesized that TIARP could be associated with the 3T3-L1 adipocyte plasma-membrane caveolae domains that contain many proteins involved in cellular trafficking and signalling processes. Studies by confocal microscopy showed that TIARP and caveolin-1, a major protein of caveolae, co-localized as patches at the plasma membrane. Immunoblot analysis of cell extracts indicated that TIARP was completely detergent-extractible from membranes, whereas caveolin-1 was present as both detergent-extractible and -insoluble pools. Since TIARP is compartmentalized with caveolin-1 within caveolae domains, we suggest this protein to be part of a signalling complex in association with caveolin-1 and regulatory proteins.
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Chambaut‐Guérin et al. (2005) studied this question. TIARP was evaluated on Co-localization of TIARP and caveolin-1. Confocal microscopy and immunoblot analysis demonstrated that TIARP co-localizes with caveolin-1 as patches at the plasma membrane of 3T3-L1 adipocytes.
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