Disease relevance of Cald1

• We have found a lymphoma 140-kDa polypeptide that is structurally similar to muscle caldesmon, suggesting that this polypeptide may be a lymphoma caldesmon [1].

High impact information on Cald1

• We postulate that zyxin cooperates with Ena/VASP proteins and caldesmon to influence integrin-dependent cell motility and actin stress fiber remodeling [2].
• Tandem array mass spectrometry identified both modified proteins as isoforms of the actomyosin regulator caldesmon, a protein known to influence contractility, stress fiber formation, and motility [2].
• The distribution of high molecular weight caldesmon (h-caldesmon, Mr 120,000-150,000) was restricted to smooth muscles where it was found in large quantity [3].
• Together, these data strongly suggest that K-cyclin expression modulates the activity of caldesmon and through this the microfilament functions in cells [4].
• Regulation of microfilament organization by Kaposi sarcoma-associated herpes virus-cyclin.CDK6 phosphorylation of caldesmon [4].

Biological context of Cald1

• The role of caldesmon in the regulation of receptor capping in mouse T-lymphoma cell [1].
• CALD1 plays a central role in the regulation of microfilament organization, consequently controlling cell shape, adhesion, cytokinesis and motility [4].

Anatomical context of Cald1

• Several complementary techniques, including immunocytochemical and immunobiochemical analyses, two-dimensional gel electrophoresis, and peptide mapping, were used in this study to examine the involvement of caldesmon in lymphocyte receptor capping [1].
• Adding the 140-kDa protein or gizzard caldesmon back to the extracted cells restores their ability to cap [1].
• MK increased muscularization of small pulmonary arteries, increasing alpha-smooth muscle actin and caldesmon staining and the expression of myocardin [5].
• Specific disruption of smooth muscle caldesmon expression in mice [6].
• The localizations of calponin and caldesmon, and the correlation of their localizations with that of the actin cytoskeleton were analyzed by immunofluorescence microscopy using appropriate antibodies and rhodamine-phalloidin [7].

Other interactions of Cald1

• Calponin and activated mitogen-activated protein kinase expression is increased and caldesmon expression is decreased in aorta, as well as in bladder [8].
• However, ACLP overexpression promotes transdifferentiation of preadipocytes into smooth muscle-like cells, which express specific markers such as SM22alpha, SM alpha-actin, SM-MHC, and caldesmon [9].
• Secondary cultures from the SL were positive for caldesmon and S-100 and negative for Na-K-ATPase, suggesting that these cells were type I fibrocytes [10].
• Sequential expression of glutathione-S-transferase isoenzymes during hair growth phases in mice and their relationship to caldesmon, phosphotyrosinase and VIP receptor protein [11].

Analytical, diagnostic and therapeutic context of Cald1

• We therefore investigated the relationship of VIP receptor expression to intracellular phosphotyrosinase and caldesmon involved in the control of growth and differentiation and metabolizing isoenzymes of the glutathione-S-transferase (GST) family alpha, mu, and pi during induced anagen of C57 BI-6 mice by immunohistochemistry [11].

References