Bryostatin 2
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| Category | Enzyme inhibitors |
| Catalog number | BBF-04100 |
| CAS | 87745-28-6 |
| Molecular Weight | 862.99 |
| Molecular Formula | C45H66O16 |
| Purity | ≥95% by HPLC |
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Description
Bryostatin 2, an analog of Bryostatin 1, is an activator of PKC (protein kinase C) with anti-tumor properties. Bryostatin 2 inhibits DNA synthesis at 100 nM in SH-SY5Y human neuroblastoma cells.
Specification
| Synonyms | Bryostatin-2; Bryostatin2; Deacetyl Bryostatin 1; Deacetyl Bryostatin-1; NSC 339554; NSC339554; NSC-339554 |
| Storage | Store at -20°C |
| IUPAC Name | [(1S,3S,5Z,7R,8E,11S,12S,13E,15S,17R,21R,23R,25S)-1,11,21,25-tetrahydroxy-17-[(1R)-1-hydroxyethyl]-5,13-bis(2-methoxy-2-oxoethylidene)-10,10,26,26-tetramethyl-19-oxo-18,27,28,29-tetraoxatetracyclo[21.3.1.13,7.111,15]nonacos-8-en-12-yl] (2E,4E)-octa-2,4-dienoate |
| Canonical SMILES | CCCC=CC=CC(=O)OC1C(=CC(=O)OC)CC2CC(OC(=O)CC(CC3CC(C(C(O3)(CC4CC(=CC(=O)OC)CC(O4)C=CC(C1(O2)O)(C)C)O)(C)C)O)O)C(C)O |
| InChI | InChI=1S/C45H66O16/c1-9-10-11-12-13-14-37(49)59-41-29(21-39(51)56-8)20-32-24-35(27(2)46)58-40(52)23-30(47)22-33-25-36(48)43(5,6)44(53,60-33)26-34-18-28(19-38(50)55-7)17-31(57-34)15-16-42(3,4)45(41,54)61-32/h11-16,19,21,27,30-36,41,46-48,53-54H,9-10,17-18,20,22-26H2,1-8H3/b12-11+,14-13+,16-15+,28-19+,29-21+/t27-,30-,31+,32+,33-,34+,35-,36+,41+,44+,45-/m1/s1 |
| InChI Key | LIPGUSBNMQRYNL-IZBIBDMISA-N |
Properties
| Appearance | White Lyophilised Solid |
| Antibiotic Activity Spectrum | neoplastics (Tumor) |
| Boiling Point | 957.2±65.0°C at 760 mmHg |
| Density | 1.28±0.1 g/cm3 |
| Solubility | Soluble in ethanol |
Reference Reading
1.Bryostatins selectively regulate protein kinase C-mediated effects on GH4 cell proliferation.
Mackanos EA1, Pettit GR, Ramsdell JS. J Biol Chem. 1991 Jun 15;266(17):11205-12.
The phorbol ester tumor promoter, 12-O-tetradecanoylphorbol-13-acetate [TPA) or phorbol 12-myristate 13-acetate), directly activates the calcium- and phospholipid-dependent protein kinase C (protein kinase C), which, in turn, generates a number of cellular responses. The bryostatins, a family of macrocyclic lactones isolated from marine bryozoans, also bind to and active protein kinase C. However, they differ from TPA in the selectivity of their responses in that they behave either as agonists or antagonists of protein kinase C actions. We used several bryostatins and TPA to examine the role of protein kinase C in the regulation of GH4C1 rat pituitary tumor cell proliferation. TPA inhibited [3H]thymidine incorporation in GH4 cells in a stereoselective and concentration-dependent manner. Examination of cell cycle distribution by flow cytometry revealed that TPA decreased the percentage of cells in S-phase and proportionally increased the percentage of G1-phase cells.
2.Effects of bryostatins 1 and 2 on morphological and functional differentiation of SH-SY5Y human neuroblastoma cells.
Jalava AM1, Heikkilä J, Akerlind G, Pettit GR, Akerman KE. Cancer Res. 1990 Jun 1;50(11):3422-8.
SH-SY5Y human neuroblastoma cells can be induced to differentiate to mature ganglion cells when treated with the phorbol ester tetradecanoylphorbol acetate (TPA). Bryostatins are a new class of protein kinase C activators that are structurally unrelated to phorbol esters. This paper describes the effects of bryostatins 1 and 2 on morphological and functional differentiation of SH-SY5Y cells. Both bryostatins induced a rapid translocation of protein kinase C from the cytosol to the membrane fraction. Within 24 h, the bryostatins had caused a nearly complete down-regulation of the enzyme. Bryostatin 1 competed for [3H]phorbol-12,13-dibutyrate binding in intact cells with potency equal to that of TPA, in contrast to bryostatin 2, which exhibited a Ki value 1 order of magnitude higher than those of the two other agents. Bryostatins induced morphological changes similar to those induced by TPA. These changes were, however, only transient, occurring during the first 6 h of incubation in the presence of these compounds.
3.Lipopolysaccharide reduces electrical coupling in microvascular endothelial cells by targeting connexin40 in a tyrosine-, ERK1/2-, PKA-, and PKC-dependent manner.
Bolon ML1, Kidder GM, Simon AM, Tyml K. J Cell Physiol. 2007 Apr;211(1):159-66.
Electrical coupling along the endothelium is central in the arteriolar conducted response and in control of vascular resistance. It has been shown that exposure of endothelium to lipopolysaccharide (LPS, an initiating factor in sepsis) reduces intercellular communication in vitro and in vivo. The molecular basis for this reduction is not known. We examined the effect of LPS on electrical coupling in monolayers of cultured mouse microvascular endothelial cells (MMEC) derived from the mouse hindlimb skeletal muscle. To assess coupling, we measured the spread of electrical current injected into the monolayer and computed the monolayer intercellular resistance (inverse measure of coupling). LPS (10 microg/ml, 1 h) reduced coupling (i.e., increased resistance) in MMEC isolated from wild-type, connexin37 (Cx37) null and Cx43(G60S) (nonfunctional mutant) mice, but not in MMEC derived from Cx40 null mice. LPS also activated JNK1/2, p38 and ERK1/2 MAP kinases.
4.Action of phorbol esters, bryostatins, and retinoic acid on cholesterol sulfate synthesis: relation to the multistep process of differentiation in human epidermal keratinocytes.
Jetten AM1, George MA, Pettit GR, Herald CL, Rearick JI. J Invest Dermatol. 1989 Jul;93(1):108-15.
This study examines the action of phorbol 12-myristate 13-acetate (PMA) on the synthesis of cholesterol sulfate in cultured normal and transformed human epidermal keratinocytes and assesses the antagonistic effects by retinoids and bryostatins on PMA action in relation to the multistep program of squamous differentiation. Treatment of normal human epidermal keratinocytes (NHEK) with PMA induces terminal cell division (irreversible growth-arrest) and causes a time- and dose-dependent increase in the incorporation of Na2(35)SO4 into cholesterol sulfate, a marker for squamous cell differentiation. This stimulation in sulfate incorporation appears specific for cholesterol sulfate and is due to increased levels of cholesterol sulfotransferase activity. The increase in cholesterol sulfate accumulation parallels the increase in transglutaminase type I, another marker for squamous differentiation. Several transformed NHEK cell lines do not exhibit increased levels of cholesterol sulfate and transglutaminase type I activity after PMA treatment, indicating that they acquired defects in the regulation of squamous differentiation.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
