Abstract

The circadian clock is the central timing system that controls numerous physiologic processes. The current model of these oscillators is based on autoregulatory transcription and translation feedback loops of these circadian genes in which Period1 (Per1) gene occupies a central position. The laminin receptor 1 (Lamr1) and its precursor are expressed in most tissues and play important roles in several physiologic and pathologic processes, including cell differentiation, growth, migration and cancer invasion. The present study showed that Lamr1 was a novel protein that interacted with human circadian clock protein hPer1 by the yeast two-hybrid system and co-immunoprecipitation, which was expressed in many tissues and did not display circadian rhythm. The expression of hPer1 was knocked down to 84.9% by the hPer1 RNA interfering test, but the expression levels of Lamr1 was not depressed by the hPer1 RNA interfering test. The results suggest that Lamr1 is a novel protein that interacts with human circadian clock protein hPer1 and Lamr1 is not a direct efferent element of circadian clock.

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