(±)-Palmitoylcarnitine chloride - CAS 6865-14-1
Category: Inhibitor
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Molecular Formula:
Molecular Weight:
(±)-Palmitoylcarnitine chloride, a long-chain acylcarnitine with both intracellular and extracellular roles, has a wide range of biological actions including the inhibition of protein kinase C and cell membrane disruption.
3-carboxy-N,N,N-trimethyl-2-[(1-oxohexadecyl)oxy]-1-propanaminium, chloride; NSC 628323; Palmitoyl-DL-carnitine chloride
Store in a cool and dry place (or refer to the Certificate of Analysis).
Canonical SMILES:
1.Acyclovir permeation enhancement across intestinal and nasal mucosae by bile salt-acylcarnitine mixed micelles.
Park GB;Shao Z;Mitra AK Pharm Res. 1992 Oct;9(10):1262-7.
The purpose of this study was to investigate the absorption enhancement of acyclovir, an antiviral agent, by means of bile salt-acylcarnitine mixed micelles. The specificity, site dependence, palmitoyl-DL-carnitine chloride (PCC) concentration dependence, and effects of absorption promoters on acyclovir absorption via the nasal cavity (N) and four different intestinal segments of the rat, i.e., duodenum (D), upper jejunum (UJ), combined lower jejunum and ileum (LJ), and colon (C) were evaluated. The present study employed the rat in situ nasal and intestinal perfusion techniques and utilized sodium glycocholate (NaGC), three acylcarnitines, and their mixed micelles as potential nasal and intestinal absorption promoters. Acylcarnitines used were DL-octanoylcarnitine chloride (OCC), palmitoyl-DL-carnitine chloride (PCC), and DL-stearoylcarnitine chloride (SCC). All acylcarnitines and NaGC by themselves produced negligible enhancement of acyclovir absorption in the rat intestine, while OCC and SCC were totally ineffective in the nasal cavity. However, the mixed micellar solutions of NaGC with PCC or SCC could significantly increase the mucosal membrane permeability of acyclovir in the colon and nasal cavity.
2.Protein kinase A-regulated membrane trafficking of a green fluorescent protein-aquaporin 5 chimera in MDCK cells.
Kosugi-Tanaka C;Li X;Yao C;Akamatsu T;Kanamori N;Hosoi K Biochim Biophys Acta. 2006 Apr;1763(4):337-44. Epub 2006 Mar 10.
The green fluorescent protein (GFP) of the jellyfish, Aeqorea victoria, was used as an autofluorescent tag to track the trafficking of aquaporin 5 (AQP5), an exocrine gland-type water channel. Two groups of chimeric proteins were constructed; one in which GFP was fused to the amino-terminus of AQP5 (GFP-AQP5) and the other, in which it was fused to the carboxyl terminus of it (AQP5-GFP). In each group, 2 chimeras were produced, a wild-type AQP5 with its normal sequence and a mutant AQP5 having a mutated amino acid at 259, i.e., GFP-AQP5-T259A and AQP5-GFP-T259A. They were used to transfect Madin-Darby canine kidney (MDCK) cells. The GFP-AQP5 chimera was localized in the intracellular vesicles, which trafficked to the plasma membrane in response to N(6), 2'-O-dibutyryladenosine 3', 5'-cyclic monophosphate (dbcAMP). Membrane trafficking was inhibited by N-[2-(p-bromocinnamylamino)ethyl]-5-isoquimolinesulfonamide (H-89) but not by palmitoyl-dl-carnitine chloride (PCC). In contrast, the AQP5-GFP chimera expressed in MDCK cells was localized constitutively on the plasma membrane. The cellular localization of the latter chimera was not affected by stimulation with dbcAMP in the presence or absence of H-89 or PCC.
3.[Changes of phosphorylation states of Cx43 protein in Chinese hamster lung cells induced by SiO2].
Wu W;Mao G;Yu C Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi. 2002 Dec;20(6):455-7.
OBJECTIVE: ;To investigate whether cellular gap-junctional communication(GJIC) down-regulation and the internalization of connexin 43(Cx43) in Chinese hamster lung fibroblasts (CHL) induced by silica-stimulated pulmonary alveolar macrophages (PAM) supermatant is related with the phosphorylation states of Cx43 protein.;METHODS: ;Western-blot analysis was used to identify phosphorylated Cx43 species.;RESULTS: ;Samples from membrane protein, total protein and nucleoprotein in CHL cells with 50-500 micrograms/ml doses of silica-stimulated PAM supernatants showed NP, P1, P2, P3 four immunoreactive bands of Cx43 protein by contrast with the control group and 0 microgram/ml SiO2 group. And with the dose of SiO2 increased, the increment of the levels of P2 and P3 was observed. Moreover, the groups treated with SiO2 and protein kinase C inhibitor, Palmitoyl-DL-Camitine chloride (PMC), simutaneously showed reduced level of P2 and P3, as compared with the groups treated with SiO2 only.;CONCLUSION: ;The inhibition of GJIC and the internalization of Cx43 by SiO2 in CHL cells may relate to the changes of phosphorylation states of Cx43, and its mechanism may be similar to that of phorbol 12-myristate 13-acetate (TPA), i.
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CAS 6865-14-1 (±)-Palmitoylcarnitine chloride

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