60 Pages, Chapter 1-5
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CHAPTER ONE
1.1 WHAT ARE HONEY BEES
Honey bees are a subset of bees in the genus Apis, primarily distinguished by the production and storage of honey and the construction of perennial, colonial nests from wax. Honey bees are the only extant members of the tribe Apini, all in the genus Apis. Currently, only seven species of honey bee are recognized, with a total of 44 subspecies, though historically, from six to 11 species have been recognised. Honey bees represent only a small fraction of the roughly 20,000 known species of bees. Some other types of related bees produce and store honey, but only members of the genus Apis are true honey bees (Micheal, 1999).
1.2 HONEY BEE VENOM
Honeybee stings are common and frequent threat in tropical and subtropical regions of the globe, where fatal envenoming due to their massive attacks has been documented. Majority of bee toxins are cytotoxins and primarily target to liver. Further, liver plays very important role in mammalian metabolism, so that any change in liver systematic will definitely affect complete metabolism of an animal. The present investigation has been emphasized on dynamics of some vital liver enzymes in circulation. The sub-lethal venom doses (1/4 and 1/2 LD50) has induced unenviable increase in level of serum alanine amino transferase (ALT), aspartate amino transferase (AST), alkaline phosphatase (ALP) and gamma-glutamyl transpeptidase (GGT). These enzymes provide functional support to liver in maintaining metabolic equilibrium. However, presence of liver functioning enzymes in circulation is the signal of massive damage of hepatic cells resulting in certain systemic reactions (Ahmad et al., 2013).
Honey bee venom investigations started almost a hundred years ago by Langer (1897) who found out that it consists of active and hemolytic basic components. The venom of the honey bee is a complex mixture of enzymes, polypeptides and low molecular weight components. A number of enzymes have been reported, such as phospholipase A2 and hyaluronidase (Habermann and Neumann 1957), acid phosphomonoesterase and esterase uenton L’-glucoslaase, Iysopflospflolipase.(Ivanova and Shkenderov 1982), ocga1actosidase and oc—acetylaminodeoxyglucosidase (Hsiang and Elliott 1975) arylamidases (Bousquet et al., 1979).
1.3 EFFECTS OF HONEY BEE VENOM
Bee venom has long been used as one of folk remedies for the arthritis and gout. Bee venom, known to be effective on the inflammatory diseases and pains, is composed of complex mixture of various components. Of them, the peptides have anti-inflammatory (Habermann and Riez, 1965), antibacterial and strong analgesic actions, and contribute to the enhancement of immune responses. Melittin, a major component of the dried bee venom, stimulates the pituitary and adrenal glands to produce catecholamine and cortisone, and stabilize the cell membrane of the lysosome for the anti-inflammatory action (Dunn and Killion, 1988). Bee venom is an alternative approach to the arthritis drugs containing steroids and immunosuppressant. However, its prolonged use causes serious side effects to patients. Further, bee has more potent venom during the summer (Croft, 1988). Venomof Apis dorsata contains the enzyme, phospholipaseA-2. This enzyme hydrolyzes the phospholipids to free fatty acids and lypolipids and thus initiates the biosynthesis of eicosanoids and platelet–activating factor, potent mediators of inflammation, allergy, apoptosis, and tumorigenesis. Melittin is another principal component of bee venom. It is 100 times more potent than hydrocortisone (Vick et al., 1974).
According to O’ Connor and Peck (1978) about fifty percent of the dry venom of bees is melittin, a peptide consisting of twenty-six amino acids, free of sulphur. Melittin is responsible for the pain involved in bee stings. In cell membranes, melittin forms tetrameric pores that facilitate ion diffusion. Melittin also binds to components of skin to form a tight complex. This complex formation appears to be at least somewhat specific, as melittin does not form a complex with albumin. O’Connor and Peck (1978) mentioned that the melittin family exhibits pronounced surfactant properties and potent haemolytic activity. Secapin and tertiapin were also identified in honey bee venom.
Melittin also stabilizes the lysosome cell membrane to protect against inflammation (Rudenko and Nipot, 1996). It is the major component of the dried bee venom, stimulates the pituitary and adrenal glands to produce catecholamine and cortisone. The main lethal factors of bee venoms for mammals were considered to be phospholipase A2 (PLA2), melittin and apamin which are present in the venom in quantities of about 15-20%, 40-60% and 2% respectively (Banks and Shipolini, 1986). Melittin was found to be the main lethal component in honey bee venom which accounts for local and general toxicity (Schmidt, 1995). Moreover, it was reported that melittin and PLA2 interact with lipid membranes and consequently have a haemolytic action (Marsh and Whaler 1980). They are also referred to as neurotoxins as they are toxic to neuromusclar (Tu 1977; Hawgood et al., 1988). The relationship between structure and action was extensively studied by Schroder et al., (1971). Blood glucose level is increased when bee venom is subcutaneously injected into rabbits, the venom may stimulate adrenaline secretion in the animals and thereby increase glyconeogenesis (Artemov et al., 1972). Although it was reported that the primary envenomation is cardiac failure (Tu 1977; Marsh and Whaler 1980).
1.4 AIMS AND OBJECTIVES OF THE STUDY
TABLE OF CONTENT
CHAPTER ONE
1.0 Introduction
1.1 What are honey bees
1.2 Honey bee venom
1.3 Effects of honey bee venom
1.4 Aims and objectives of the study
CHAPTER TWO
2.1 Honey Bee venom
2.2 Types of Honey Bee Venom
2.2.1 Bumble bee venom
2.2.2 Solitary bee venom
2.3 Physical characteristics of bee venom
2.4 The composition of bee venom
2.5 Studies on bee venom and its medical use
2.6 The allergic for honey bee venom
2.7 Cardiac effect of Honey bee venom in rats
2.8 Haematological, Biochemical and Enzymological effects on Albino rats
CHAPTER THREE
3.0 Materials and method
3.1 Study Area
3.2 Experimental procedure
3.3 Study Test
CHAPTER FOUR
4.0 Results
4.1 Results Interpretation
4.2 Table of Results
CHAPTER FIVE
5.0 Discussion and Conclusion
5.1 Discussion
5.2 Conclusion
REFERENCES
