BEE VENOM THERAPY FOR CERVICAL CANCER
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The other names for cervical cancer are collum cancer and cancer cervicus. After breast cancer, it is the second most common type of cancer among women. Cancer, if diagnosed at an early stage, can be controlled through a proper regime. Those women, who go for regular screening programs avoid the chances of becoming a victim of cancer to a great extent. And that is the reason that the ratio of cancer in women belonging to developed countries to those, who are from undeveloped countries is quite low.
Regular screening programs help in detecting the disease at an early stage. This leads to an on-time treatment. A screening program is also important because symptoms related to cancer can take a lot of time to surface so; it helps in making an early prediction. And if it is diagnosed late then till that time the disease might wreak havoc inside the body system. Sampling is done in a screening test to analyze any sort of cell changes. |
These samples are tested thoroughly to determine the chances of any impending deadly disease. In the same manner, screening helps in detecting cervical cancer too. When done at an early stage the chances of recovery become quite satisfactory. On the other hand, if the growing cancer is not diagnosed at the right time, it can get very difficult for a woman to fight the growth of cervical cancer.
The weight of the uterus is around 40 to 70 grams and is nearly the size of a pear. Outer walls of the uterus are composed of muscles that are nearly one centimeter thick, while the inner wall is made of a mucous membrane. During mensuration, the inner wall (mucous membrane) is responsible for the excretion made. Once the transitional stage is over, the uterus gets a little smaller in size due to shrinkage.
The cervix plays an important role inside the vagina. It is also another form of glandular mucosa that helps prevent dangerous infectious bacteria from getting inside the uterus. The border between the cervix and mucosa is known as the TZ (transformation zone). It is a very small area and any sort of human papillomavirus (HPV infections) can lead to cell changes and ultimately cancers. During the process of screening, cell samples are obtained from the TZ zone for colposcopy.
In a few cases, cervical cancer can be detected with the help of visible symptoms, but one must not solely rely on those symptoms. Sometimes these symptoms arise very late and the treatment gets complicated and challenging. So, regular screening is always recommended.
If you notice blood in your vomit or abnormal bleeding from the vagina during sexual intercourse consult a doctor right away. If left unattended you might experience bloody discharge from the vagina constantly.
Cervical cancer is most commonly transmitted through sexual contact and the virus responsible for its manifestation is known as human papillomavirus. Cervical cancer doesn’t initiate right away, as it requires certain conditions and changes. Any prolonged infection with a carcinogenic type of human papillomavirus is an essential prerequisite for developing into cervical cancer.
According to various experts, it has been determined that there is a strong connection between sexual habits and the chances of cervical cancer in women. The obvious reasons are several partners, who can make a woman prone to this cancer during first pregnancy or first intercourse, excessive alcohol intake and tobacco consumption can also increase the chances of becoming a victim of cervical cancer.
Today cervical cancer has become quite common in women due to multiple sexual partners, an early sexual debut, unsafe pregnancy, and substandard oral contraceptives and even smoking.
Apoptotic Effect of Melittin Purified from Iranian Honey Bee Venom on Human Cervical Cancer HeLa Cell Line
One of the main components of honey bee venom is melittin, which is a peptide. Several clinical studies have revealed that melittin holds an inhibitory effect when it comes to controlling the division of cancer cells. Though this effect is understood and further clinical research is required to scrutinize the molecular mechanism of this inhibitory effect.
For this clinical research, melittin was obtained from Iranian honey BV. It was found that pure melittin delivers anti-cancer effects on the subjects of cervical cancer. Bee venom was obtained from the Iranian honey bee and in the second stage, melittin was isolated through reversed-phase HPLC. The biological mechanism of melittin was evaluated through a hemolytic test done on the human RBCs (red blood cells).
Further investigation was carried out to determine if melittin could inhibit the propagation of those cells that are responsible for cervical cancer. The viability of the melittin cured HeLa cell line was examined through MTT assay. In the end, a cell death study was carried out using Annexin V-FITC and Propidium iodide dual staining. The data obtained presented that HD50 (half hemolytic concentration) induced melittin stood at 0.5 µg/ml in a free BS solution. The IC50 attained after 12 hours at 1.8 µg/ml by the MTT assay.
Flow cytometric analysis showed that melittin instigated apoptosis at a general concentration of more than 1 µg/ml. It is suggested that melittin causes apoptotic cell death of those cells presents inside the cervical that can lead to cancer at any stage. It can be concluded that melittin can serve as a potential therapeutic agent for future clinical studies meant for discovering anticancer treatments.
Bee Venom Inhibits Growth of Human Cervical Tumors in Mice
Bee venom contains a variety of peptides and enzymes, including serine proteases. While the presence of serine proteases in bee venom has been demonstrated, the role of these proteins in bee venom has not been elucidated. Furthermore, there is currently no information available regarding the melanization response or the fibrin (ogen) olytic activity of bee venom serine protease, and the molecular mechanism of its action remains unknown. Here we show that bee venom serine protease (Bi-VSP) is a multifunctional enzyme.
In insects, Bi-VSP acts as an arthropod prophenoloxidase (proPO)-activating factor (PPAF), thereby triggering the phenoloxidase (PO) cascade. Bi-VSP injected through the stinger induces a lethal melanization response in target insects by modulating the innate immune response.
In mammals, Bi-VSP acts similarly to snake venom serine protease, which exhibits fibrin(ogen)olytic activity. Bi-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, defining roles for Bi-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease.
These findings provide a novel view of the mechanism of bee venom in which the bee venom serine protease kills target insects via a melanization strategy and exhibits fibrin(ogen)olytic activity. Bee venom contains a variety of peptides and enzymes, including serine proteases. While the presence of serine proteases in bee venom has been demonstrated, the role of these proteins in bee venom has not been elucidated. Furthermore, there is currently no information available regarding the melanization response or the fibrin(ogen)olytic activity of bee venom serine protease, and the molecular mechanism of its action remains unknown.
Here we show that bee venom serine protease (Bi-VSP) is a multifunctional enzyme. In insects, Bi-VSP acts as an arthropod prophenoloxidase (proPO)-activating factor (PPAF), thereby triggering the phenoloxidase (PO) cascade. Bi-VSP injected through the stinger induces a lethal melanization response in target insects by modulating the innate immune response. In mammals, Bi-VSP acts similarly to snake venom serine protease, which exhibits fibrin(ogen)olytic activity. Bi-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, defining roles for Bi-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease.
These findings provide a novel view of the mechanism of bee venom in which the bee venom serine protease kills target insects via a melanization strategy and exhibits fibrin(ogen)olytic activity.Bee venom contains a variety of peptides and enzymes, including serine proteases. While the presence of serine proteases in bee venom has been demonstrated, the role of these proteins in bee venom has not been elucidated. Furthermore, there is currently no information available regarding the melanization response or the fibrin(ogen)olytic activity of bee venom serine protease, and the molecular mechanism of its action remains unknown.
Here we show that bee venom serine protease (Bi-VSP) is a multifunctional enzyme. In insects, Bi-VSP acts as an arthropod prophenoloxidase (proPO)-activating factor (PPAF), thereby triggering the phenoloxidase (PO) cascade. Bi-VSP injected through the stinger induces a lethal melanization response in target insects by modulating the innate immune response. In mammals, Bi-VSP acts similarly to snake venom serine protease, which exhibits fibrin(ogen)olytic activity. Bi-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, defining roles for Bi-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease.
These findings provide a novel view of the mechanism of bee venom in which the bee venom serine protease kills target insects via a melanization strategy and exhibits fibrin(ogen)olytic activity.In this study, it was determined if bee venom can prohibit the growth of the cervical tumor by inactivating nuclear factor kappa B and enhancing death receptor expressions in mice. According to the Vivo study, it was observed that bee venom, 1mg per kg inhibited the growth of the tumor. In the same manner, the inhibitory effects of bee venom on the growth of cancer cells in the cervix were also observed. Bee venom 1 to 5 µg per ml also inhibited the growth of the cancer responsible cells, C33A and Ca-Ski by induction of the apoptotic cell death but in a dose-dependent regime. Expression of the death receptors DR6, DR3, FAS and DR downstream pro-apoptotic proteins that included Bax and caspase-3 were concurrently increased. But it was also noticed that expression of the Bcl-2 and NF-κB activity were inhibited with the help of bee venom treatment on cultured cancer cells, human cancer cells, human tumor, and tumor mice.
Bee venom therapy has been used in the treatment of various diseases and illnesses. It has also been used to treat chronic inflammatory diseases like rheumatoid arthritis. Different clinical studies have shown that bee venom hinders mammary carcinoma cell production in vivo and growth of tumor in vivo, like leukemia cells, cancer cells, renal, bladder, and liver, ovarian and prostate. Related to the effect of bee venom on the human cervical cancer cells, not a lot of information is available.
According to the lab studies done earlier, it has been established that bee venom led to repression of cancer cells and angiogenesis in the culture of cervical cancer cells. This study is focused on the xenograft model that makes use of clinical data based on human samples and inhibition of human cancer cell growth. Cervical cancer is the second most common type of cancer that affects women. HPV infection is the major reason for the development of cervical cancer.
To examine the anti-tumor effect of bee venom in vivo, growth of a tumor on the cervical cancer cell xenograft, having nude mice following a bee venom therapy 1mg/kg, was adopted. In light of previous studies, the administration of bee venom was altered. It was found that 3mg/kg was ineffective in the previous studies so, the amount of bee venom was altered to 1mg/kg to get the desired results.
Bee venom was given intraperitoneally, for twice a week till 4 weeks to those mice that had tumors ranging in-between 100 to 300 mm. Right after 7 days the tumor was measured and at the end of the period of the clinical trial all mice were exterminated and their tumors dissected and weighed. It was found that the inhibitory effect of the bee venom on the development of cervical tumor was quite significant in xenograft based model mice.
To evaluate the relationship between the DR expression and human tumor growth and NF-κB activity, expression of p21,p53, and expression of FAS, DR3, DR6, cleavaged 9, 8 and 3 and NF-κB activity between the human tumor tissues and normal human cervical tissues. It was found that expression of p53, p21, DR6, DR3, and FAS were elevated significantly and the cleavaged caspase 9, 8 and 3 in the cervical tumor tissues when compared to those in the normal tissues investigated by immunohistochemistry and Western blotting. Results of the study also revealed that nucleus expression of p65 and p50, plκB expression and NF-κB activity was much higher in the human tumor tissues when compared to those present in normal cervical tissues.
Dual Function of a Bee Venom Serine Protease: Prophenoloxidase-Activating Factor in Arthropods and Fibrin(ogen)olytic...
Bee venom is an effective therapeutic agent, as it consists of biogenic amines, peptides, and enzymes. It has been observed that a bee sting can lead to a serious allergic reaction that is caused due to hypersensitive response and if not treated immediately it can lead to anaphylaxis. Apis mellifera is also known as a honey bee and Bombus spp is also known as a bumblebee, these are the most common species of bees. Honeybee, as we all know, is a beneficial bee for humans while, the bumblebee is used to pollinate crops so, indirectly it is also beneficial.
There is one major difference between the honeybee and the bumblebee and that is the amount of bee venom that they produce. A honeybee sting is nearly 5 times more powerful than that of a bumblebee and that means that the venom of the honeybee is also very strong. But right after stinging, honey bees lose their stinger but that is not the case with bumblebees, as they can make repeated attacks. The reason being, they do not lose their stinger.
It has been observed that bumblebee venom is highly cross-reactive with the honeybee venom. Honey bee venom has been used for long to deal with symptoms related to skin diseases, tumors, cancer cells, general pain, rheumatism, and arthritis. Components of bee venom still need to be studied carefully to get the most out of it.
To carry out this experiment the P.rapae, S.exigua, B.mori, and B.ignitus were used in this clinical study that was supplied by the Department Of Agricultural Biology, Republic Of Korea. Instead of fact that Bi-VSP holds Ser, Asp and His reside in the positions that correspond to catalytic triad that is also identified in the snake venom. It was determined if Bi-VSP also functions in the same manner as that of snake venom serine that exhibits fibrinolytic activity.
The B.ignitus bees went through dissection on a special piece of ice with a stereo microscope obtained from Zeiss, Germany. The tissue samples included venom sac, venom gland, and fat body, they were gathered and treated with PBS 1.5 mM KH2PO4, 8 mM Na2HPO4, 27 mM KCl, 140 mM NaCl, pH 7.4. The Hemolymph was collected in the cold test tubes by perforating the main body of B.ignitus bees and by cutting the legs of P.rapae larvae, S.exigua and B.mori. Later, the hemolymph went under centrifugation at 10,000×g for nearly 10 minutes to get rid of the cell debris. Tissue samples that were obtained were made use of without any further processing.
To tackle this issue, the time course of the human prothrombin cleavage was by the Bi-VSP and it was found that the thrombin was a major cleavage product. Now this shows that Bi-VSP leads to activation of prothrombin that indicates a role for the Bi-VSP as an effective thrombin activator. According to the cleavage pattern that was observed during the process of prothrombin, activation it was noted down that Bi-VSP actively converts prothrombin into simple thrombin in a way that is quite familiar to mammalian blood coagulation factor Xa.
This study is one of its first types of research that carries evidence in favor of bee venom serine protease functions analogously meant for both: snake venom serine protease and an arthropod PPAF. Findings made in this clinical research also highlight and justify the presence of serine protease in BV. It is to be noted that Bi-VSP genuinely acts as a PPAF that helps induce lethal melanization reaction in the arthropod and as fibrin (ogen) olytic enzyme to facilitate infiltration of BV components in the bloodstream of mammals. The essential finding is that BV serine protease acts with a unique mechanism in mammals and arthropods and that gives importance to a two-pronged strategy that is only possible with BV serine protease.
The weight of the uterus is around 40 to 70 grams and is nearly the size of a pear. Outer walls of the uterus are composed of muscles that are nearly one centimeter thick, while the inner wall is made of a mucous membrane. During mensuration, the inner wall (mucous membrane) is responsible for the excretion made. Once the transitional stage is over, the uterus gets a little smaller in size due to shrinkage.
The cervix plays an important role inside the vagina. It is also another form of glandular mucosa that helps prevent dangerous infectious bacteria from getting inside the uterus. The border between the cervix and mucosa is known as the TZ (transformation zone). It is a very small area and any sort of human papillomavirus (HPV infections) can lead to cell changes and ultimately cancers. During the process of screening, cell samples are obtained from the TZ zone for colposcopy.
In a few cases, cervical cancer can be detected with the help of visible symptoms, but one must not solely rely on those symptoms. Sometimes these symptoms arise very late and the treatment gets complicated and challenging. So, regular screening is always recommended.
If you notice blood in your vomit or abnormal bleeding from the vagina during sexual intercourse consult a doctor right away. If left unattended you might experience bloody discharge from the vagina constantly.
Cervical cancer is most commonly transmitted through sexual contact and the virus responsible for its manifestation is known as human papillomavirus. Cervical cancer doesn’t initiate right away, as it requires certain conditions and changes. Any prolonged infection with a carcinogenic type of human papillomavirus is an essential prerequisite for developing into cervical cancer.
According to various experts, it has been determined that there is a strong connection between sexual habits and the chances of cervical cancer in women. The obvious reasons are several partners, who can make a woman prone to this cancer during first pregnancy or first intercourse, excessive alcohol intake and tobacco consumption can also increase the chances of becoming a victim of cervical cancer.
Today cervical cancer has become quite common in women due to multiple sexual partners, an early sexual debut, unsafe pregnancy, and substandard oral contraceptives and even smoking.
Apoptotic Effect of Melittin Purified from Iranian Honey Bee Venom on Human Cervical Cancer HeLa Cell Line
One of the main components of honey bee venom is melittin, which is a peptide. Several clinical studies have revealed that melittin holds an inhibitory effect when it comes to controlling the division of cancer cells. Though this effect is understood and further clinical research is required to scrutinize the molecular mechanism of this inhibitory effect.
For this clinical research, melittin was obtained from Iranian honey BV. It was found that pure melittin delivers anti-cancer effects on the subjects of cervical cancer. Bee venom was obtained from the Iranian honey bee and in the second stage, melittin was isolated through reversed-phase HPLC. The biological mechanism of melittin was evaluated through a hemolytic test done on the human RBCs (red blood cells).
Further investigation was carried out to determine if melittin could inhibit the propagation of those cells that are responsible for cervical cancer. The viability of the melittin cured HeLa cell line was examined through MTT assay. In the end, a cell death study was carried out using Annexin V-FITC and Propidium iodide dual staining. The data obtained presented that HD50 (half hemolytic concentration) induced melittin stood at 0.5 µg/ml in a free BS solution. The IC50 attained after 12 hours at 1.8 µg/ml by the MTT assay.
Flow cytometric analysis showed that melittin instigated apoptosis at a general concentration of more than 1 µg/ml. It is suggested that melittin causes apoptotic cell death of those cells presents inside the cervical that can lead to cancer at any stage. It can be concluded that melittin can serve as a potential therapeutic agent for future clinical studies meant for discovering anticancer treatments.
Bee Venom Inhibits Growth of Human Cervical Tumors in Mice
Bee venom contains a variety of peptides and enzymes, including serine proteases. While the presence of serine proteases in bee venom has been demonstrated, the role of these proteins in bee venom has not been elucidated. Furthermore, there is currently no information available regarding the melanization response or the fibrin (ogen) olytic activity of bee venom serine protease, and the molecular mechanism of its action remains unknown. Here we show that bee venom serine protease (Bi-VSP) is a multifunctional enzyme.
In insects, Bi-VSP acts as an arthropod prophenoloxidase (proPO)-activating factor (PPAF), thereby triggering the phenoloxidase (PO) cascade. Bi-VSP injected through the stinger induces a lethal melanization response in target insects by modulating the innate immune response.
In mammals, Bi-VSP acts similarly to snake venom serine protease, which exhibits fibrin(ogen)olytic activity. Bi-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, defining roles for Bi-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease.
These findings provide a novel view of the mechanism of bee venom in which the bee venom serine protease kills target insects via a melanization strategy and exhibits fibrin(ogen)olytic activity. Bee venom contains a variety of peptides and enzymes, including serine proteases. While the presence of serine proteases in bee venom has been demonstrated, the role of these proteins in bee venom has not been elucidated. Furthermore, there is currently no information available regarding the melanization response or the fibrin(ogen)olytic activity of bee venom serine protease, and the molecular mechanism of its action remains unknown.
Here we show that bee venom serine protease (Bi-VSP) is a multifunctional enzyme. In insects, Bi-VSP acts as an arthropod prophenoloxidase (proPO)-activating factor (PPAF), thereby triggering the phenoloxidase (PO) cascade. Bi-VSP injected through the stinger induces a lethal melanization response in target insects by modulating the innate immune response. In mammals, Bi-VSP acts similarly to snake venom serine protease, which exhibits fibrin(ogen)olytic activity. Bi-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, defining roles for Bi-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease.
These findings provide a novel view of the mechanism of bee venom in which the bee venom serine protease kills target insects via a melanization strategy and exhibits fibrin(ogen)olytic activity.Bee venom contains a variety of peptides and enzymes, including serine proteases. While the presence of serine proteases in bee venom has been demonstrated, the role of these proteins in bee venom has not been elucidated. Furthermore, there is currently no information available regarding the melanization response or the fibrin(ogen)olytic activity of bee venom serine protease, and the molecular mechanism of its action remains unknown.
Here we show that bee venom serine protease (Bi-VSP) is a multifunctional enzyme. In insects, Bi-VSP acts as an arthropod prophenoloxidase (proPO)-activating factor (PPAF), thereby triggering the phenoloxidase (PO) cascade. Bi-VSP injected through the stinger induces a lethal melanization response in target insects by modulating the innate immune response. In mammals, Bi-VSP acts similarly to snake venom serine protease, which exhibits fibrin(ogen)olytic activity. Bi-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, defining roles for Bi-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease.
These findings provide a novel view of the mechanism of bee venom in which the bee venom serine protease kills target insects via a melanization strategy and exhibits fibrin(ogen)olytic activity.In this study, it was determined if bee venom can prohibit the growth of the cervical tumor by inactivating nuclear factor kappa B and enhancing death receptor expressions in mice. According to the Vivo study, it was observed that bee venom, 1mg per kg inhibited the growth of the tumor. In the same manner, the inhibitory effects of bee venom on the growth of cancer cells in the cervix were also observed. Bee venom 1 to 5 µg per ml also inhibited the growth of the cancer responsible cells, C33A and Ca-Ski by induction of the apoptotic cell death but in a dose-dependent regime. Expression of the death receptors DR6, DR3, FAS and DR downstream pro-apoptotic proteins that included Bax and caspase-3 were concurrently increased. But it was also noticed that expression of the Bcl-2 and NF-κB activity were inhibited with the help of bee venom treatment on cultured cancer cells, human cancer cells, human tumor, and tumor mice.
Bee venom therapy has been used in the treatment of various diseases and illnesses. It has also been used to treat chronic inflammatory diseases like rheumatoid arthritis. Different clinical studies have shown that bee venom hinders mammary carcinoma cell production in vivo and growth of tumor in vivo, like leukemia cells, cancer cells, renal, bladder, and liver, ovarian and prostate. Related to the effect of bee venom on the human cervical cancer cells, not a lot of information is available.
According to the lab studies done earlier, it has been established that bee venom led to repression of cancer cells and angiogenesis in the culture of cervical cancer cells. This study is focused on the xenograft model that makes use of clinical data based on human samples and inhibition of human cancer cell growth. Cervical cancer is the second most common type of cancer that affects women. HPV infection is the major reason for the development of cervical cancer.
To examine the anti-tumor effect of bee venom in vivo, growth of a tumor on the cervical cancer cell xenograft, having nude mice following a bee venom therapy 1mg/kg, was adopted. In light of previous studies, the administration of bee venom was altered. It was found that 3mg/kg was ineffective in the previous studies so, the amount of bee venom was altered to 1mg/kg to get the desired results.
Bee venom was given intraperitoneally, for twice a week till 4 weeks to those mice that had tumors ranging in-between 100 to 300 mm. Right after 7 days the tumor was measured and at the end of the period of the clinical trial all mice were exterminated and their tumors dissected and weighed. It was found that the inhibitory effect of the bee venom on the development of cervical tumor was quite significant in xenograft based model mice.
To evaluate the relationship between the DR expression and human tumor growth and NF-κB activity, expression of p21,p53, and expression of FAS, DR3, DR6, cleavaged 9, 8 and 3 and NF-κB activity between the human tumor tissues and normal human cervical tissues. It was found that expression of p53, p21, DR6, DR3, and FAS were elevated significantly and the cleavaged caspase 9, 8 and 3 in the cervical tumor tissues when compared to those in the normal tissues investigated by immunohistochemistry and Western blotting. Results of the study also revealed that nucleus expression of p65 and p50, plκB expression and NF-κB activity was much higher in the human tumor tissues when compared to those present in normal cervical tissues.
Dual Function of a Bee Venom Serine Protease: Prophenoloxidase-Activating Factor in Arthropods and Fibrin(ogen)olytic...
Bee venom is an effective therapeutic agent, as it consists of biogenic amines, peptides, and enzymes. It has been observed that a bee sting can lead to a serious allergic reaction that is caused due to hypersensitive response and if not treated immediately it can lead to anaphylaxis. Apis mellifera is also known as a honey bee and Bombus spp is also known as a bumblebee, these are the most common species of bees. Honeybee, as we all know, is a beneficial bee for humans while, the bumblebee is used to pollinate crops so, indirectly it is also beneficial.
There is one major difference between the honeybee and the bumblebee and that is the amount of bee venom that they produce. A honeybee sting is nearly 5 times more powerful than that of a bumblebee and that means that the venom of the honeybee is also very strong. But right after stinging, honey bees lose their stinger but that is not the case with bumblebees, as they can make repeated attacks. The reason being, they do not lose their stinger.
It has been observed that bumblebee venom is highly cross-reactive with the honeybee venom. Honey bee venom has been used for long to deal with symptoms related to skin diseases, tumors, cancer cells, general pain, rheumatism, and arthritis. Components of bee venom still need to be studied carefully to get the most out of it.
To carry out this experiment the P.rapae, S.exigua, B.mori, and B.ignitus were used in this clinical study that was supplied by the Department Of Agricultural Biology, Republic Of Korea. Instead of fact that Bi-VSP holds Ser, Asp and His reside in the positions that correspond to catalytic triad that is also identified in the snake venom. It was determined if Bi-VSP also functions in the same manner as that of snake venom serine that exhibits fibrinolytic activity.
The B.ignitus bees went through dissection on a special piece of ice with a stereo microscope obtained from Zeiss, Germany. The tissue samples included venom sac, venom gland, and fat body, they were gathered and treated with PBS 1.5 mM KH2PO4, 8 mM Na2HPO4, 27 mM KCl, 140 mM NaCl, pH 7.4. The Hemolymph was collected in the cold test tubes by perforating the main body of B.ignitus bees and by cutting the legs of P.rapae larvae, S.exigua and B.mori. Later, the hemolymph went under centrifugation at 10,000×g for nearly 10 minutes to get rid of the cell debris. Tissue samples that were obtained were made use of without any further processing.
To tackle this issue, the time course of the human prothrombin cleavage was by the Bi-VSP and it was found that the thrombin was a major cleavage product. Now this shows that Bi-VSP leads to activation of prothrombin that indicates a role for the Bi-VSP as an effective thrombin activator. According to the cleavage pattern that was observed during the process of prothrombin, activation it was noted down that Bi-VSP actively converts prothrombin into simple thrombin in a way that is quite familiar to mammalian blood coagulation factor Xa.
This study is one of its first types of research that carries evidence in favor of bee venom serine protease functions analogously meant for both: snake venom serine protease and an arthropod PPAF. Findings made in this clinical research also highlight and justify the presence of serine protease in BV. It is to be noted that Bi-VSP genuinely acts as a PPAF that helps induce lethal melanization reaction in the arthropod and as fibrin (ogen) olytic enzyme to facilitate infiltration of BV components in the bloodstream of mammals. The essential finding is that BV serine protease acts with a unique mechanism in mammals and arthropods and that gives importance to a two-pronged strategy that is only possible with BV serine protease.
Sources:
Apoptotic Effect of Melittin Purified from Iranian Honey Bee Venom on Human Cervical Cancer HeLa Cell Line
Trend of Pharmacopuncture Therapy for Treating Cervical Disease in Korea
Dual Function of a Bee Venom Serine Protease: Prophenoloxidase-Activating Factor in Arthropods and Fibrin(ogen)olytic...
Bee venom inhibits growth of human cervical tumors in mice
Apoptotic Effect of Melittin Purified from Iranian Honey Bee Venom on Human Cervical Cancer HeLa Cell Line
Trend of Pharmacopuncture Therapy for Treating Cervical Disease in Korea
Dual Function of a Bee Venom Serine Protease: Prophenoloxidase-Activating Factor in Arthropods and Fibrin(ogen)olytic...
Bee venom inhibits growth of human cervical tumors in mice
