Caldesmon and Its Phosphorylation in Regulating Contraction and Relaxation of Intestinal Smooth Muscle

The contraction and relaxation of intestinal smooth muscle are closely related to the regulation of thick and thin muscle filaments. As an actin-binding protein, Caldesmon is one of the important contractile proteins involved in the regulation of the thick and thin filaments of intestinal smooth muscle. It can cross-link with actin, myosin and tropomyosin to prevent the binding of actin and myosin, thus inhibiting the contraction of the intestinal smooth muscle. However, phosphorylation modifications of Caldesmon can reverse this inhibition. Caldesmon plays a key role in intestinal motility disorders, and can be stimulated by protein kinase activated through different signaling pathways to cause its own phosphorylation, thereby enhancing the binding of actin and myosin, and further causing the contraction of intestinal smooth muscle. In CKNI, Baidu Academic and PubMed databases, Caldesmon, smooth muscle, phosphorylation, actin, myosin and contraction and relaxation were used as keywords to find relevant literature. To provide a theoretic basis for clinical diseases targeting the regulation of intestinal smooth muscle contraction and relaxation based on Caldesmon and its phosphorylation, this article reviews the function and related upstream signaling pathways involved in the regulation of intestinal smooth muscle contraction and relaxation by Caldesmon and its phosphorylation.

CSTR: 32200.14.cjcb.2023.10.0010