Overseen ByDavid Putrino, PhD, PT
Age: 18+
Sex: Any
Travel: May be covered
Time Reimbursement: Varies
Trial Phase: Phase 1 & 2
Recruiting
Sponsor: Icahn School of Medicine at Mount Sinai
No Placebo Group
Approved in 3 jurisdictions
Trial Summary
What is the purpose of this trial?This will be a pilot multi-arm clinical trial investigating the feasibility of Lumbrokinase (LK) as an intervention in three clinical cohorts:
* Long Covid (LC)
* Post-treatment Lyme disease syndrome (PTLDS)
* Myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS)
What safety data is available for lumbrokinase as a treatment?The provided research does not directly address the safety data of lumbrokinase in humans. The studies focus on the fibrinolytic and antithrombotic effects of lumbrokinase in animal models and its expression and characterization in recombinant forms. While these studies suggest potential therapeutic benefits, they do not provide specific safety data for human use.23457
Do I need to stop taking my current medications for this trial?The trial does not specify if you need to stop taking your current medications, but you cannot participate if you are currently using antiplatelet or anticoagulation medications.
Is Lumbrokinase a promising drug for Long COVID?Lumbrokinase, a drug derived from earthworms, shows promise because it can dissolve blood clots and is absorbed into the bloodstream when taken orally. This suggests it could help with conditions related to blood clots, which might be beneficial for Long COVID.23567
What data supports the idea that Lumbrokinase for Long COVID is an effective treatment?The available research shows that Lumbrokinase, a fibrinolytic enzyme from earthworms, has been studied for its ability to break down blood clots in various conditions. However, there is no specific data provided here about its effectiveness for Long COVID. The studies focus on its potential for treating blood clot-related issues, like in animal models with thrombosis, but do not directly address Long COVID. Therefore, while Lumbrokinase may have potential due to its clot-dissolving properties, more research is needed to confirm its effectiveness specifically for Long COVID.12357
Eligibility Criteria
This trial is for individuals with Long Covid, Post-treatment Lyme disease syndrome (PTLDS), or Myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS). Specific eligibility criteria are not provided.Inclusion Criteria
I have been diagnosed with Long Covid, Post-treatment Lyme disease syndrome, or ME/CFS by a doctor.
I meet the criteria for ME/CFS with active symptoms.
I have been diagnosed with Long Covid, Post-treatment Lyme disease syndrome, or ME/CFS.
Exclusion Criteria
I have been diagnosed with an autoimmune condition.
I am currently taking medication to prevent blood clots.
I have surgery planned during or right after the study.
I have a history of bleeding or clotting issues.
Participant Groups
The trial is testing Lumbrokinase (LK) as a potential treatment in three separate groups: those with Long Covid, PTLDS, and ME/CFS. It's a pilot study to see if the treatment is feasible.
3Treatment groups
Experimental Treatment
Group I: Post-treatment Lyme Disease SyndromeExperimental Treatment1 Intervention
Boluoke® brand lumbrokinase capsules, 300,000 functional units (FUs) twice per day, daily for 6 weeks.
Group II: ME/CFSExperimental Treatment1 Intervention
Boluoke® brand lumbrokinase capsules, 300,000 functional units (FUs) twice per day, daily for 6 weeks.
Group III: Long CovidExperimental Treatment1 Intervention
Boluoke® brand lumbrokinase capsules, 300,000 functional units (FUs) twice per day, daily for 6 weeks.
Lumbrokinase is already approved in China, United States, Japan for the following indications:
🇨🇳 Approved in China as Lumbrokinase for:
- Cardiovascular diseases
- Stroke prevention
- Myocardial infarction prevention
🇺🇸 Approved in United States as Boluoke for:
- Supplement for cardiovascular health
- Blood clot prevention
🇯🇵 Approved in Japan as Lumbrokinase for:
- Cardiovascular diseases
- Stroke prevention
Find A Clinic Near You
Research locations nearbySelect from list below to view details:
The Cohen Center for Recovery from Complex Chronic Illnesses (CoRE)New York, NY
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Who is running the clinical trial?
Icahn School of Medicine at Mount SinaiLead Sponsor
Columbia UniversityCollaborator
PolyBio Research FoundationCollaborator
References
A novel fibrinolytic enzyme extracted from the earthworm, Lumbricus rubellus. [2019]A strong fibrinolytic enzyme was readily obtained in saline extracts of the earthworm, Lumbricus rubellus. It hydrolyzed not only plasminogen-rich fibrin plates, but also plasminogen-free fibrin plates. The average fibrinolytic activity was about 100 CU (plasmin units) or 250 IU (urokinase units)/g wet weight. The molecular weight and isoelectric point were about 20,000 and 3.4, respectively. The enzyme was heat-stable and displayed a very broad optimal pH range. DFP and SBTI strongly inhibited the enzyme, but the anti-plasmin agent, t-AMCHA, exerted little effect under the same conditions. Purification of the enzyme was performed and three partially purified fractions were obtained. These three fractions were further subdivided. The first fraction (F-I) was divided into three fractions (F-I-0, F-I-1, and F-I-2), which exhibited similar biochemical characteristics. The second fraction (F-II) could not be subdivided. The third fraction (F-III) was divided into two fractions (F-III-1 and F-III-2). Based on results for their enzymatic activities against various substrates, the fraction I enzymes are thought to represent a chymotrypsin-like enzyme and the fraction III enzymes to represent a trypsin-like enzyme. The fraction II enzyme appears to be neither a trypsin- or chymotrypsin-like enzyme nor an elastase. The amino acid compositions of the six enzymes were estimated. Compared with other serine enzymes, these enzymes contained very abundant asparagine or aspartic acid, and there was very little proline or lysine. From the above data, these enzymes are regarded as novel fibrinolytic enzymes, and we name them collectively as Lumbrokinase from the generic name of the earthworm.
In vivo evaluation of lumbrokinase, a fibrinolytic enzyme extracted from Lumbricus rubellus, in a prosthetic vascular graft. [2016]Lumbrokinase (LK) is a fibrinolytic enzyme purified from the earthworm Lumbricus rubellus. To investigate the fibrinolytic and antithrombotic effects of lumbrokinase, a series of animal experiments were performed.
Codon optimization, expression, and characterization of recombinant lumbrokinase in goat milk. [2006]Lumbrokinase is an important fibrinolytic enzyme derived from earthworm. Although its cDNA has been isolated and sequenced, there is still no report on expression of the lumbrokinase due to unknown reasons. To determine the elements affecting the expression of lumbrokinase, two copies of a lumbrokinase cDNA(w) obtained by RT-PCR and a synthesized lumbrokinase cDNA(m) with optimized codons were cloned into a mammary-gland-specific expression vector pIbCP. The pIbCP-LK-LK vector preparations were directly injected in the lactating goat mammary glands. Results showed that both LK-w and LK-m were successfully expressed in goat milk. The fibrinolytic activity of the LK-w in milk was 225,000 +/- 13,200 tPA units/L, while that of the LK-m was 550,000 +/- 21,600 tPA units/L, indicating that the codon optimization plays an important role in improving the lumbrokinase expression. The molecular weight of the recombinant lumbrokinase is 31.8 kDa. The main physiochemical features of the recombinant lumbrokinase, including temperature stability, pH resistance, and sensitivity to pepsin, were also clarified. This is the first report on expression and characterization of a genetically engineered lumbrokinase.
Purification and characterization of six fibrinolytic serine-proteases from earthworm Lumbricus rubellus. [2019]The six lumbrokinase fractions (F1 to F6) with fibrinolytic activities were purified from earthworm Lumbricus rubellus lysates using the procedures of autolysis, ammonium sulfate fractionation, and column chromatography. The proteolytic activities on the casein substrate of the six iso-enzymes ranged from 11.3 to 167.5 unit/mg with the rank activity orders of F2 > F1 > F5 > F6 > F3 > F4. The fibrinolytic activities of the six fractions on the fibrin plates ranged from 20.8 to 207.2 unit/mg with rank orders of F6 > F2 > F5 > F3 > F1 > F4. The molecular weights of each iso-enzyme, as estimated by SDS-PAGE, were 24.6 (F1), 26.8 (F2), 28.2 (F3), 25.4 (F4), 33.1 (F5), and 33.0 kDa (F6), respectively. The plasminogen was activated into plasmin by the enzymes. The optimal temperature of the six iso-enzymes was 50 degrees C, and the optimal pH ranged from pH 4-12. The four iso-enzymes (F1-F4) were completely inhibited by PMSF. The two enzymes (F5 and F6) were completely inhibited by aprotinin, TLCK, TPCK, SBTI, LBTI, and leupeptin. The N-terminal amino acid (aa) sequences of the first 20 to 22 residues of each fraction had high homology. All six iso-enzymes had identical aa residues 2-3 and 13-15. The N-terminal 21-22 aa sequences of the F2, F3, and F4 iso-enzymes were almost the same. The N-terminal aa sequences of F5 and F6 were identical.
Expression, purification, and characterization of recombinant lumbrokinase PI239 in Escherichia coli. [2009]Lumbrokinase (LK) is an important fibrinolytic enzyme derived from earthworms. It has been found that LK is composed of a group of isoenzymes. To construct and express the mature peptide of LK PI239 in Escherichia coli, we amplified and optimized the gene of LK which was then cloned into the prokaryotic expression vector pET-22b(-). The recombinant LK (rLK) protein was expressed as inclusion bodies and we have developed a purification process of rLK from these inclusion bodies. A step-down urea concentration strategy was applied to the rLK renaturation process. The purified and renatured rLK apparently ameliorated the conditions of the model thrombosis rats used, and may be developed into a therapeutic agent for thrombotic-associated diseases.
Intestinal Absorption of Fibrinolytic and Proteolytic Lumbrokinase Extracted from Earthworm, Eisenia andrei. [2021]To investigate the intestinal absorption of a fibrinolytic and proteolytic lumbrokinase extracted from Eisenia andrei, we used rat everted gut sacs and an in situ closed-loop recirculation method. We extracted lumbrokinase from Eisenia andrei, and then raised polyclonal antibody against lumbrokinase. Fibrinolytic activity and proteolytic activity in the serosal side of rat everted gut sacs incubated with lumbrokinase showed dose- and time-dependent patterns. Immunological results obtained by western blotting serosal side solution using rat everted gut sacs method showed that lumbrokinase proteins between 33.6 and 54.7 kDa are absorbed mostly by the intestinal epithelium. Furthermore, MALDI-TOF mass spectrometric analysis of plasma fractions obtained by in situ recirculation method confirmed that lumbrokinase F1 is absorbed into blood. These results support the notion that lumbrokinase can be absorbed from mucosal lumen into blood by oral administration.
Purification and proteomic analysis of potent fibrinolytic enzymes extracted from Lumbricus rubellus. [2023]Lumbrokinase derived from earthworms, Lumbricus rubellus is known to have fibrinolytic enzymes that have potential as therapeutic drugs due to its ability to dissolve fibrin. The current study is aimed to purify the Lumbrokinase from L. rubellus and identify its protein component.