Evidence for Heme Oxygenase‐1 Association with Caveolin‐1 and ‐2 in Mouse Mesangial Cells

• Published in: IUBMB life 2003-09, Vol.55 (9), p.525-532
• Main Authors: Jung, Nam‐Hee, Kim, Hong Pyo, Kim, Bum‐Rae, Cha, Seok Ho, Kim, Gyeong A., Ha, Hunjoo, Na, Young Eun, Cha, Young‐Nam
• Format: Article
• Language: English
• Subjects: Animals; Cadmium; Cadmium - pharmacology; Caveolin; Caveolin 1; Caveolin 2; Caveolins - drug effects; Caveolins - metabolism; Chemical Precipitation; Glomerular Mesangium - drug effects; Glomerular Mesangium - enzymology; Glomerular Mesangium - metabolism; Heme Oxygenase (Decyclizing) - drug effects; Heme Oxygenase (Decyclizing) - metabolism; Heme Oxygenase-1; Membrane Proteins; Mice; Microscopy, Confocal; Mouse mesangial cell; Nitric Oxide; Nitric Oxide Donors - pharmacology; Nitrogen Oxides; Spermine - analogs & derivatives; Spermine - pharmacology
• ISSN: 1521-6543; 1521-6551
• DOI: 10.1080/15216540310001620968

The interaction of heme oxygenase‐1 (HO‐1) and caveolin in the cultured mouse mesangial cells (MMC) was investigated. In normal MMCs, high levels of caveolin‐2 and low level of caveolin‐1 at mRNA and protein level were observed without any detectable expression of caveolin‐3. Upon treating the MMCs either with cadmium (Cd) or spermine NONOate (SPER/NO), expression of HO‐1 mRNA and protein was increased. Caveolae rich membranous fractions from the MMCs treated with Cd or SPER/NO contained both HO‐1 and caveolin‐1 or caveolin‐2. The experiments of immuno‐precipitation showed complex formation between the HO‐1 and caveolin‐1 or caveolin‐2 in the Cd treated MMCs. Confocal microscopic results also support co‐localization of HO‐1 and caveolin‐1 or caveolin‐2 at the plasma membrane. Co‐localization of caveolins with HO‐1 in caveolae suggested that caveolin could also play an important role in regulating the function of HO‐1. IUBMB Life, 55: 525‐532, 2003