Melatonin chemically known as N-acetyl-5-methoxytryptamine is a small physiological compound of diversified functions. Melatonin has been found in phylogenetically different taxa of bacteria, unicellular eukaryote, microalgae, plants, fungi, and animals. Identification of melatonin in many of these microorganisms is missing, and its function is rarely known. Although, melatonin in microorganisms is not essentially involved in circadian process, rather, it exhibits antioxidant property also and may protect chlorophyll pigment to damage from stress and free radicals. Mostly, the pathway for melatonin synthesis in microorganisms shows similarity with vertebrates. Investigation on melatonin in some organisms allows more concrete discussion about their possible role. The various functions of melatonin in human including sleep and regulation of circadian rhythm has been well characterized. Here, we have focused on the mechanism of immune regulatory, antioxidant, and scavenging property of melatonin during pathogenesis caused by fungi, bacteria, and virus. This article will provide a view on microbial sources and possible therapeutic aspects of melatonin in future.
In order to advance the assisted reproductive technologies used in animals and human beings, it is important to accumulate basic informations about underlying molecular mechanisms that shape the biological processes of reproduction. From within seminal plasma, proteins perform a wide variety of distinct functions that regulate major reproductive events such as fertilization. The ability of such proteins to bind and interact with different antagonistic ions and biomolecules such as polysaccharides, lipids, and other proteins present in the male and female reproductive tract define these capabilities. Over the last two decades, extensive work has been undertaken in an attempt to define the role of seminal plasma proteins, of which, Gelatin binding proteins (GBPs) represent a large family. GBPs comprise of known group of Bovine seminal plasma (BSP) protein family, matrix metallo proteinases (MMP 2 and MMP 9) and fibronectin, which have been widely studied. The presence of a type II repeat is a characteristic feature of GBPs, which is similar in structure to the fibronectin type II domain (fn2), which has ability to bind multiple ligands including gelatin, glycosaminoglycans, choline phospholipids, and lipoproteins. Two fn2 domains are present within the BSP protein family, while, three fn2 domains are found in gelatinases (MMP-2 and MMP9), and ELSPBP1 (Epididymosomes Transfer Epididymal Sperm Binding Protein 1) contains four long fn2 domains. For the most part BSP proteins are exclusively expressed in seminal vesicles although mBSPH1, mBSPH2 and hBSPH1 are all expressed in the epididymis. The expression of gelatinases has been demonstrated in several organs and tissues such as the prostate, testis, epididymis, ovary, human placenta, cervix and endometrial wall. This review intends to bring current updates on the role of GBPs in reproductive physiology to light, which may act as basis for future studies on GBPs.
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