Thanks, but I have seen this already. I still do not really understand what Need 2 Slin does exactly. Why would I want to take it before meals? What is difference between eating, say, a steak with broccoli and taking 1 capsule of Need 2 Slin 30 minutes before meal and then eating a steak with broccoli?
Is it that you don't understand the MOA for the ingredients as they were laid out, or the concepts of nutrient partitioners and insulin in general? I'll try to address what I think you're questioning, but honestly it feels a bit like you're smarter than you're letting on and trying to "stump the chump" for some odd reason.
Here's something from StrategicMove on Na-R-ALA:
I suppose your interest is pre-meal timing is to use Na-R-ALA to enhance insulin synthesis. Due to Na-R-ALA's superior stability, bioavailability, and longer-acting properties versus other forms of ALA, recommendations range from 15 minutes before a meal to right after the meal. Considering, that it has multiple benefits reclycling of vitamins C, E, glutathione, and coenzyme-Q10; as well as chelation of metals and general free-radical quenching, it may be useful to take it closer to meals (about 10 minutes before), so it can also support the detoxification of mutagenic agents found in food, in addition to its impact on insulin levels. For perspective, a recent study (Carlson DA, Smith AR, Fischer SJ, Young KL, Packer L. Altern Med Rev. 2007 Dec;12(4):343-51.) showed that Na-R-ALA reached peak plasma concentrations within 10-20 minutes of oral supplementation.
One on Gymnema:
Gymnema sylvestre stimulates insulin release in vitro by increased membrane permeability.
Persaud SJ, Al-Majed H, Raman A, Jones PM.
SourcePhysiology Division, School of Biomedical Sciences, King's College, London, UK.
Abstract
To determine whether extracts of Gymnema sylvestre may have therapeutic potential for the treatment of non-insulin-dependent diabetes mellitus (NIDDM), we examined the effects of an alcoholic extract of G. sylvestre (GS4) on insulin secretion from rat islets of Langerhans and several pancreatic beta-cell lines. GS4 stimulated insulin release from HIT-T15, MIN6 and RINm5F beta-cells and from islets in the absence of any other stimulus, and GS4-stimulated insulin secretion was inhibited in the presence of 1 mM EGTA. Blockade of voltage-operated Ca(2+) channels with 10 microM isradipine did not significantly affect GS4-induced secretion, and insulin release in response to GS4 was independent of incubation temperature. Examination of islet and beta-cell integrity after exposure to GS4, by trypan blue exclusion, indicated that concentrations of GS4 that stimulated insulin secretion also caused increased uptake of dye. Two gymnemic acid-enriched fractions of GS4, obtained by size exclusion and silica gel chromatography, also caused increases in insulin secretion concomitant with increased trypan blue uptake. These results confirm the stimulatory effects of G. sylvestre on insulin release, but indicate that GS4 acts by increasing cell permeability, rather than by stimulating exocytosis by regulated pathways. Thus the suitability of GS4 as a potential novel treatment for NIDDM can not be assessed by direct measurements of beta-cell function in vitro.
PMID: 10556769 [PubMed - indexed for MEDLINE]
A little on Corosolic Acid (banaba leaf):
Corosolic acid stimulates glucose uptake via enhancing insulin receptor phosphorylation.
Shi L, Zhang W, Zhou YY, Zhang YN, Li JY, Hu LH, Li J.
SourceNational Center for Drug Screening, People's Republic of China.
Abstract
Corosolic acid, a triterpenoid compound widely existing in many traditional Chinese medicinal herbs, has been proved to have antidiabetic effects on animal experiments and clinical trials. However, the underlying mechanisms remain unknown. Here, we investigate its cellular effects and related signaling pathway. We demonstrate that it enhances glucose uptake in L6 myotubes and facilitates glucose transporter isoform 4 translocation in CHO/hIR cells. These actions are mediated by insulin pathway activation and can be blocked by phosphatidylinositol 3-kinase (PI(3) Kinase) inhibitor wortmannin. Furthermore, Corosolic acid inhibits the enzymatic activities of several diabetes-related non-receptor protein tyrosine phosphatases (PTPs) in vitro, such as PTP1B, T-cell-PTP, src homology phosphatase-1 and src homology phosphatase-2
And on cAMP:
cAMP enhances insulin secretion by an action on the ATP-sensitive K+ channel-independent pathway of glucose signaling in rat pancreatic islets.
H Yajima, M Komatsu, T Schermerhorn, T Aizawa, T Kaneko, M Nagai, G W Sharp and K Hashizume
+ Author Affiliations
Department of Aging Medicine and Geriatrics, Shinshu University School of Medicine, Matsumoto, Japan.
Abstract
Cyclic AMP potentiates glucose-stimulated insulin release by actions predominantly at a site, or sites, distal to the elevation of the cytosolic free Ca2+ concentration ([Ca2+]i). Glucose also acts at a site, or sites, distal to the elevation of [Ca2+]i via the ATP-sensitive K+ channel (K+ATP channel)-independent signaling pathway. Accordingly, using rat pancreatic islets, we studied the location of the action of cAMP and its interaction with the glucose pathway. Forskolin, an activator of adenylyl cyclase, raised intracellular cAMP levels and enhanced KCl-induced (Ca2+ -stimulated) insulin release in the presence, but not in the absence, of glucose. Thus, cAMP has no direct effect on Ca2+ -stimulated insulin release. The interaction between cAMP and glucose occurs at a step distal to the elevation of [Ca2+]i because forskolin enhancement of KCl-induced insulin release, in the presence of glucose, was demonstrated in the islets treated with diazoxide, a K+ATP channel opener. The enhancement of insulin release was not associated with any increase in [Ca2+]i. Furthermore, the interaction between cAMP and glucose was unequivocally observed even under stringent Ca2+ -free conditions, indicating the Ca2+ -independent action of cAMP. This action of cAMP is physiologically relevant, because not only forskolin but also glucagon-like peptide 1, glucose-dependent insulinotropic polypeptide, and pituitary adenylyl cyclase activating polypeptide exerted similar actions. In conclusion, the cAMP/protein kinase A pathway has no direct effect on Ca2+ -stimulated insulin exocytosis. Rather, it strongly potentiates insulin release by increasing the effectiveness of the K+ATP channel-independent action of glucose
and that matters because of the relationship of forskolin and cAMP:
Mechanism(s) of Action
Forskolin acts primarily by activating the enzyme adenylate cyclase, which results in increased cyclic adenosine monophosphate (cAMP) in cells. Cyclic AMP belongs to a class of substances known as “second messengers,” and is one of the most important cell-regulating compounds. Among its many roles, cAMP activates numerous other enzymes involved in diverse cellular functions. Hormones and neurotransmitters also activate adenylate cyclase—but forskolin appears to be able to activate adenylate cyclase by itself. Thus, forskolin can increase cyclic AMP without the assistance of hormones or neurotransmitters.
So, if you read all these, they all relate to insulin. If you understand insulin, and how bodybuilders use insulin to gain mass, it makes sense to take these types of supplements before meals to make the most use of insulin for anabolic purposes. Even with broccoli and steak (one of my favorites, though chicken and broccoli are more synergistic), insulin usage and GLUT-4 translocation can help anabolism.
I hope that helps clarify why you would take it pre-meal, and enough detail on MOAs.