Astaxanthin (AXT)
is one of the most important fat-soluble carotenoids
that have abundant and diverse therapeutic applications namely in
liver disease, cardiovascular disease, cancer treatment, protection
of the nervous system, protection of the skin and eyes against UV
radiation, and boosting the immune system. However, due to its intrinsic
reactivity, it is chemically unstable, and therefore, the design and
production processes for this compound need to be precisely formulated.
Nanoencapsulation is widely applied to protect AXT against degradation
during digestion and storage, thus improving its physicochemical properties
and therapeutic effects. Nanocarriers are delivery systems with many
advantages—ease of surface modification, biocompatibility,
and targeted drug delivery and release. This review discusses the
technological advancement in nanocarriers for the delivery of AXT
through the brain, eyes, and skin, with emphasis on the benefits,
limitations, and efficiency in practice.
1-aminocyclopropane-1-carboxylic acid oxidase (ACO) enzyme is a member of the Fe II-dependent family of oxidases/oxygenases which require Fe(2+) as a cofactor, ascorbate as a cosubstrate and CO(2) as an activator. This enzyme catalyses the terminal step in the plant signaling of ethylene biosynthetic pathway. A 948 bp fragment of the ACO1 gene cDNA sequence was cloned from tomato (Lycopersicon esculentum) fruit tissues by using reverse transcriptase-polymerase chain reaction (RT-PCR) with two PCR primers designed according to the sequence of a tomato cDNA clone (X58273). The BLAST search showed a high level of similarity (77-98 %) between ACO1 and ACO genes of other plants. The calculated molecular mass and predicted isoelectric point of LeACO1 were 35.8 kDa and 5.13, respectively. The three-dimensional structure studies illustrated that the LeACO1 protein folds into a compact jelly-roll motif comprised of 8 α-helices, 12 β-strands and several long loops. The cosubstrate was located in a cofactor-binding pocket referred to as a 2-His-1-carboxylate facial triad. Semi-quantitative RT-PCR analysis of gene expression revealed that the LeACO1 was expressed in fruit tissues at different ripening stages.
Urtica dioica L. is an Iranian native pharmacological plant for which little attention has been paid to the anatomical structure. Medical applications of this plant include diabetes therapy, digestive improvement, anemia and kidney disease therapy. Because climatic conditions can affect the anatomical structure which in turn affects pharmacological compositions, research on the anatomy of this plant is needed. In this research, plant samples were collected from populations near the cities of Brojerd, Mashad, Ghazvin, and Ramsar. Cross sections, were made from stem, leaf, and petiole at the second internodes, and stained using double staining methods. Differences between stem, leaf, and petiole tissues confirmed that climatic factors produced differences among the populations in anatomical structure of aerial organs. Noted differences included: 1-Number and diameter of vascular bundles with five vascular bundles in Ghazvin population, five to seven vascular bundles in the Brojerd population, and four vascular bundles in populations in Mashad and Ramsar. The Mashad and Ramsar populations differed in diameter. 2-Protective tissue and thickness of the cuticle of plants from Ghazvin had more tissues because of lower thermal mean and mountain region. 3-Differences in petiole diameter with the largest petiole diameter in the Mashad population and the smallest petiole diameter in the Ramsar population. These observed differences in anatomy confirmed the effect of climate on differentiation in anatomical structure in Urtica dioica L.
: Ecarin is a metalloproteinase found in snake venom (SVMP) with an important role in coagulation and control of hemostasis. It can specifically produce active-thrombin from prethrombin-2 and does not differentiate between normal and abnormal prothrombin. It is used in diagnostic tests and to evaluate the treatment process of many diseases. There are many drawbacks associated with separating these compounds from snake venom. Therefore, in this study, full-length recombinant Ecarin (r-Ecarin) was cloned, expressed, and purified in eukaryotic host cells. To determine the most effective form of the enzyme, r-Ecarin was compared with the recombinant truncated form, which has only the metalloprotease domain of the protein (r-Ecamet) in terms of function and expression. Briefly, A DNA construct composed of sequence-encoding Ecarin was designed and cloned into pCAGGS expression vector and, subsequently, expressed in Chinese Hamster Ovary (CHO) cells. To identify the enzymatic activity of expressed protein, a bioactivity assay was performed. Blood coagulation time and expression levels of r-Ecarin and r-Ecamet proteins were compared. Also, a histopathological assessment was carried out on the liver of mice treated with these proteins. Comparison of r-Ecarin and r-Ecamet expression pattern demonstrated that full-length Ecarin expression has at least 2-fold higher expression in eukaryotic cells. Determination of r-Ecarin function proved that this protein is capable of prothrombin cleavage and producing thrombin. Comparison of PT test results between the r-Ecarin and r-Ecamet showed that there is a significant difference in the activity of the two enzymes and the full-length protein coagulates the blood in less time.
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