دورية أكاديمية

Structural heterogeneity and multifunctionality of lactoferrin.

التفاصيل البيبلوغرافية
العنوان: Structural heterogeneity and multifunctionality of lactoferrin.
المؤلفون: Albar AH, Almehdar HA, Uversky VN, Redwan EM; Department of Biological Science, Faculty of Science, King Abdulaziz University, Jeddah, PO Box 80203, Jeddah 21589, Saudi Arabia. redwan1961@yahoo.com.
المصدر: Current protein & peptide science [Curr Protein Pept Sci] 2014; Vol. 15 (8), pp. 778-97.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Review
اللغة: English
بيانات الدورية: Publisher: Bentham Science Publishers Country of Publication: United Arab Emirates NLM ID: 100960529 Publication Model: Print Cited Medium: Internet ISSN: 1875-5550 (Electronic) Linking ISSN: 13892037 NLM ISO Abbreviation: Curr Protein Pept Sci Subsets: MEDLINE
أسماء مطبوعة: Publication: Saif Zone, Sharjah, U.A.E. : Bentham Science Publishers
Original Publication: Hilversum, Netherlands ; Boca Raton, FL : Bentham Science Publishers, c2000-
مواضيع طبية MeSH: Lactoferrin/*chemistry , Lactoferrin/*metabolism, Alternative Splicing/genetics ; Amino Acid Sequence ; Animals ; Anti-Bacterial Agents/pharmacology ; Antiviral Agents/pharmacology ; Glycosylation ; Humans ; Lactoferrin/genetics ; Lactoferrin/pharmacology ; Molecular Sequence Data
مستخلص: Lactoferrin or lactotransferrin is a multifunctional glycoprotein found in blood circulation, mucosal surfaces, neutrophils, and in various secretory fluids, such as milk, bile, tears, nasal secretion, pancreatic juice, and saliva. The lactoferrin content in milk varies between different mammalian species and, within one species, between lactation periods. Although lactoferrin is known to be involved with immunoprotection, its functions are not limited to the regulation of innate immunity, but extend to iron transfer to cells, control of the level of free iron in blood and external secretions, interaction with DNA, RNA, heparin, and polysaccharides, and pronounced antimicrobial and antiviral activities. This multifunctionality is determined by the fact that lactoferrin belongs to the class of hybrid proteins possessing both ordered domains and functionally important intrinsically disordered regions. Structurally, lactoferrin is a globular glycoprotein with a molecular mass of about 80 kDa consisting of two homologous domains known as N-terminal and C-terminal lobes. These lobes are unevenly glycosylated (with the C-lobe typically containing more N-linked glycosylation sites). Each lobe can bind a single ferric ion concomitantly with one bicarbonate anion. Lactoferrin and its lobes have a wide spectrum of antimicrobial and antiviral activities, with the antimicrobial and antiviral potentials dependent on the type of microbes and viruses. Often, the N-lobe possesses the majority of antimicrobial activities. In addition, lactoferrin and its lobes possess clear anti-cancer, wound healing, anti-inflammatory, and immunomodulation activities.
المشرفين على المادة: 0 (Anti-Bacterial Agents)
0 (Antiviral Agents)
EC 3.4.21.- (Lactoferrin)
تواريخ الأحداث: Date Created: 20140924 Date Completed: 20150721 Latest Revision: 20191027
رمز التحديث: 20231215
DOI: 10.2174/1389203715666140919124530
PMID: 25245670
قاعدة البيانات: MEDLINE
الوصف
تدمد:1875-5550
DOI:10.2174/1389203715666140919124530