In this article, we share Kambo Research that I have gathered over time. Some of the Kambo Research is based on individual peptides contained in Kambo, not the total secretion.
The Lymphatic System is a drainage network of fluid, organs, and vessels that is responsible for the removal of cellular debris, large proteins, foreign bodies, pathogenic agents, viruses, toxins, etc.; and excess fluid from the extracellular that moves through the Lymphatic system, which acts as active purification centres.
The primary lymphoid organs include the bone marrow. The secondary lymphoid organs include the spleen, appendix, tonsils, adenoids and Peyer’s patches (lymphoid tissue present in the small and large intestines). Their function is to defend the body against aggressive agents entering the body or to destroy accumulated wastes.
There are approximately 6 to 10 litres in the body, compared to 3.5 to 5 litres of blood.; About 1.5 to 2 litres of lymph per day circulate throughout the whole body. Efficient circulation activation can increase this number from 10 to 30 litres per day. Lymph vessels slowly increase in size, moving lymph toward its entry into the circulatory system behind the heart. The lymphatic system is not connected to the heart, so it has to rely upon some other method, usually muscular contraction, to create the necessary pumping action needed to move lymph. The lymphatic system is filled with millions of one-way valves, which allow lymph fluid to flow in one direction only; usually upward and away from gravity.
Lymph passes through processing and collection centres called lymph nodes. These nodes act as filtration and purification stations for lymph circulation, capturing and destroying toxins and Capturing cancer cells.
There are from 400 up to 1,000 nodes in the human body, more than one-half located in the abdomen ( This might explain why Kambo is felt strongly in the gut). Understanding the Lymphatic system helps us understand Kambo Research more.
Read the original and full article HERE
Screening for new bioactive peptides in South
American anurans have been pioneered in frogs of the genus
Phyllomedusa. All frogs of this genus have venomous skin
secretions, i.e., a complex mixture of bioactive peptides
against potential predators and pathogens that presumably
evolved in a scenario of predator-prey interaction and
defence against microbial invasion. For every new anuran
species studied, new peptides are found with homologies to
hormones, neurotransmitters, antimicrobials, and several
other peptides with unknown biological activity. From
Vittorio Erspamer findings, this genus has been reported as
a ‘‘treasure store’’ of bioactive peptides, and several groups
focus their research on these species.
Read the full paper here. 593_antimicrobial_peptides_from_phyllomedusa_frogscalderon_et_al._2010-1 (1)
Recently, we have found that the skin secretions of the Amazonian tree frog Phyllomedusa bicolor contain molecules with
antitumor and angiostatic activities and identified one of them as the antimicrobial peptide dermaseptin (Drs) B2. In the
present study we further explored the in vitro and in vivo antitumor activity of this molecule and investigated its mechanism
of action. We showed that Drs B2 inhibits the proliferation and colony formation of various human tumor cell types, and the
proliferation and capillary formation of endothelial cells in vitro. Furthermore, Drs B2 inhibited tumor growth of the human
prostate adenocarcinoma cell line PC3 in a xenograft model in vivo. Research on the mechanism of action of Drs B2 on
tumor PC3 cells demonstrated a rapid increasing amount of cytosolic lactate dehydrogenase, no activation of caspase-3,
and no changes in mitochondrial membrane potential. Confocal microscopy analysis revealed that Drs B2 can interact with
the tumor cell surface, aggregate and penetrate the cells. These data together indicate that Drs B2 does not act by
apoptosis but possibly by necrosis. In conclusion, Drs B2 could be considered as an interesting and promising
pharmacological and therapeutic leader molecule for the treatment of cancer.
Read the full paper here.
French-Cancer-Research
Three naturally occurring dermorphin-like
peptides from the skin of the frog PhyUomedusa bicolor, the
related carboxyl-terminal amides, and some substituted analogs
were synthesized, their binding profiles to opioid receptors were
determined, and their biological activities were studied in isolated organ preparations and intact animals. The opioid binding
profile revealed a very high selectivity of these peptides for IA
sites and suggested the existence of two receptor subtypes, of
high and low affinity. The peptides tested acted as potent IA
opioid agonists on isolated organ preparations. They were
several times more active in inhibiting electrically evoked contractions in guinea pig ileum than in mouse vas deferens. When
injected into the lateral brain ventricle or peritoneum of rats, the
high-affinity-site-preferring ligand, [Lys7-NH21dermorphin, behaved as a potent analgesic agent. By contrast, the low-affinitysite-preferring ligand, [Trp4,Asn7-NH2]dermorphin, produced
a weak antinociception but an intense catalepsy.
Read the full paper here.
Dermorphin-related-peptides
Deltorphins are endogenous linear heptapeptides, isolated from skin extracts of frogs belonging to the genus
PhyUomedusa, that have a higher affinity and selectivity for 6
opioid binding sites than any other natural compound known.
Two deltorphins with the sequence Tyr-Ala-Phe-Asp(or Glu)-
Val-Val-Gly-NH2 have been isolated from skin extracts of
PhyUomedusa bicolor. The alanine in position 2 is in the D
configuration. These peptides, [D-Ala2]deltorphins I and II,
show an even higher affinity for 6 receptors than the previously
characterized deltorphin, which contains D-methionine as the
second amino acid. These peptides show some similarity to
another constituent of Phylomedusa skin, dermorphin, which
is highly selective for ,u-opioid receptors. These peptides all
have the N-terminal sequence Tyr-D-Xaa-Phe, where D-Xaa is
either D-alanine or D-methionine. While this structure seems to
be capable of activating both pA and 6 opioid receptors,
differences in the C-terminal regions of these peptides are
probably responsible for the observed high receptor selectivity
of dermorphin and deltorphin.
Read the full paper here.
Deltorphins
A frog used for “hunting magic” by several
groups of Panoan-speaking Indians in the borderline between
Brazil and Peru is identified as PhyUomedusa bicolor. This
frog’s skin secretion, which the Indians introduce into the body
through fresh burns, is rich in peptides. These include vasoactive peptides, opioid peptides, and a peptide that we have
named adenoregulin, with the sequence GLWSKIKEVGKEAAKAAAKAAGKAALGAVSEAV as determined from
mass spectrometry and Edman degradation. The natural peptide may contain a D amino acid residue, since it is not identical
in chromatographic properties to the synthetic peptide. Adenoregulin enhances binding of agonists to Al adenosine receptors; it is accompanied in the skin secretion by peptides that
inhibit binding. The vasoactive peptide sauvagine, the opioid
peptides, and adenoregulin and related peptides affect behavior in mice and presumably contribute to the behavioral
sequelae observed in humans.
Read the full paper here.
kambo-and-pepides.more_
The dermaseptins belong to a superfamily of host defense peptides that are made in the skin of Hylidae frogs. These peptides are genetically related, with a remarkable identity in signal sequences and intervening sequences of their preproforms, but they have markedly diverged to yield several families of peptides that are structurally and functionally distinct. These include the dermaseptins (stricto sensu), the phylloseptins, the plasticins, the dermatoxins, the phylloxins, the raniseptins, the caerin-related peptides, the caerins, the fallaxidins, the frenatins, and the aureins. Most of these peptides are cidal against wall-less bacteria, Gram-negative and Gram-positive bacteria, fungi, protozoa, yeast, and enveloped viruses but are weakly toxic against mammalian cells. Their antimicrobial activity results from their capacity to bind to the bacterial plasma membrane, thereby triggering transient wormhole formation or membrane disruption.
Read the full study here
https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/dermaseptin?fbclid=IwAR3IaR6lVIYh0GKTwQGSLCfI0dJL6Sip4KVXf9QWlnlp7jd25YOjn-4GgOc
Phyllomedusa rohdei, a small Brazilian amphibian, contains in its skin, in addition to a number of inactive polypeptides, at least three peptides active on plain muscle. The first one (polypeptide a) is characterized by a stimulant action on the rat uterus and the
rat colon combined with a moderate hypotensive action in the dog; the second (polypeptide b) by a typical bradykinin-like activity; the third (polypeptide c) by a physalaemin-like activity (cf. Bertaccini, Cei & Erspamer, 1965a, 1965b).
The three polypeptides may be separated from each other by chromatography on alkaline alumina column followed by elution with descending concentrations of ethanol.
Polypeptide a emerges from the column in the 95% ethanol eluates, polypeptide b in the 70% ethanol eluates, and polypeptide c in the 60% and 50% ethanol eluates.
Polypeptide a is possibly a tryptophan-containing pentapeptide, the synthesis of which is in progress; polypeptide c has not yet been obtained in a pure state; polypeptide b has been isolated and identified as bradykinyl-isoleucyl-tyrosine 0-sulphate (Anastasi,
Erspamer, Bertaccini & Cei, unpublished). The proposed structure has been confirmed by synthesis (Bernardi, Bosisio, De Castiglione & Goffredo, 1966). For the new naturally occurring bradykinin-like endecapeptide the name of phyllokinin has been suggested.
This paper describes some of the pharmacological actions of natural and synthetic phyllokinin in comparison with synthetic bradykinyl-isoleucyl-tyrosine and with synthetic bradykinin.
Read the full paper here.
PHARMACOLOGICAL-DATA-ON-PHYLLOKININ-2
“Kambô circulates in the heart. Our shaman said that when we take Kambô, it makes the heart move accurately so that things flow, bringing good things to the person. It is as if there was a cloud on the person, preventing the good things to come, then, when it takes the Kambô; it comes a ‘green light’, which opens its
ways, making things easier”
Read the full paper here.
Kambo-Spirit-of-the-Shaman
Kambo is the name of a secretion of a tropical
frog, the Phyllomedusa bicolor or giant leaf frog from the
Amazonian forest, which has been used for centuries by
local tribes to enhance their hunter skills. Its first tribal use
was described in 1925, and included the first effects after
administration of the secretion: nausea and vomiting. Since
the end of last century Kambo is introduced in Europe and
the USA as a ‘healing’ intervention to cleanse the bodily
systems, it is regarded as a ‘detox’ intervention.
Method: We reviewed all available literature related to
adverse events and pharmacological effects of the active
peptides in Kambo.
Result: The secretion of the frog consists several
bioactive peptides and within few minutes after intake,
nausea, vomiting, facial edema, palpitations and hypotension
can occur. In the pharmacological and medical literature,
these are reported as transient adverse events, although in
essence the reactions are purely pharmacological.
We will present and discuss its adverse events, the
pharmacological basis of these events and present contraindications and recommendations for safe use.
Read the full paper here.
Kambo_and_its_Multitude_of_Biological_Effects_Adve
We talk a lot about the peptides in Kambo, but what are they? In this paper, Hans gives an in-depth explanation of Peptides and proteins.
Read the full paper here. ( This is a scientific paper and can be challenging to understand. I have included a second article that is easier for the layman to understand.
Peptidevorlesung
Kambo is not safe for everyone to use and should be carefully considered. Always seek advice from a healthcare provider or Kambo Practitioner.
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