Detail of "119978-18-6"

Reference

Entactin promotes adhesion and long-term maintenance of cultured regenerated skeletal myotubes

Entactin promotes adhesion and long-term maintenance of cultured regenerated skeletal myotubes. Funanage, Vicky L.; Smith, Susan M.; Minnich, Michelle A. (Res. Dep., Alfred I. DuPont Inst., Wilmington, DE 19899, USA). J. Cell. Physiol., 150(2), 251-7 (English) 1992. CODEN: JCLLAX. ISSN: 0021-9541. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) The basal laminal protein, laminin, has been shown to promote migration and proliferation of cultured skeletal myoblasts, resulting in increased myotube formation. However, skeletal myotubes adhere poorly to a laminin substrate, and long-term cultures of skeletal myotubes on laminin have not been achieved. Cultured satellite cells from bupivacine-damaged rat skeletal muscle actively proliferate and differentiate on a dild. Matrigel substrate composed of laminin, type IV collagen, heparan sulfate proteoglycan, and entacin. Myotubes cultured on dild. Matrigel are contractile and have never been obsd. to detach from the culture dish; rather, myotubes generally atrophy after 2-3 wk in culture. Antibodies directed against the various protein components of Matrigel were used to det. the role of each component in enhancing muscle differentiation. Anti-laminin impaired satellite cell adhesion, whereas antibodies against either type IV collagen or heparan sulfate proteoglycan had no effect. Anti-entactin did not inhibit attachment, proliferation, or fusion of cultured satellite cells; however, myotubes exposed to anti-enactin failed to adhere to the culture dish after spontaneous myotube contractions began. 119978-18-6 is just another one chemical used in this study. Apparently, entactin is responsible for long-term maintenance and maturation of contractile skeletal myotubes on a dild. Matrigel substrate. .

Protein kinase C regulates endothelial cell tube formation on basement membrane matrix, Matrigel

Protein kinase C regulates endothelial cell tube formation on basement membrane matrix, Matrigel. Kinsella, J. L.; Grant, D. S.; Weeks, B. S.; Kleinman, H. K. (Gerontol. Res. Cent., Natl. Inst. Aging, Baltimore, MD 21224, USA). Exp. Cell Res., 199(1), 56-62 (English) 1992. CODEN: ECREAL. ISSN: 0014-4827. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Human umbilical vein endothelial cells differentiate within 12 h to form capillary-like networks of tube structures when the cells are plated on Matrigel, a mixt. of basement membrane proteins. Nothing is known about the intracellular signaling events involved in this differentiation. As a first step to define the process, the authors investigated the possible role of protein kinase C activation by b-phorbol 12-myristate 13-acetate (PMA) in regulating the formation of the tube structures.There are some commonly used reagents with their cas registry numbers 9026-43-1 and 119978-18-6 in this article. In this model, PMA increased tube formation several-fold in a dose-dependent manner with half-max. stimulation of tube formation at approx. 5 nM PMA. In the absence of serum, essentially little or no tubes were formed on Matrigel unless PMA was added to the medium. Only active phorbol analogs increased tube formation, whereas the protein kinase C inhibitor, H-7, blocked tube formation. The protein kinase C activators and inhibitors were effective only when added at or just after plating of the cells and did not affect already formed tubes. This study suggests that protein kinase C is involved in the early events of in vitro endothelial cell tube formation on Matrigel. .