Abstract
Lactoferrin (Lf), an iron-binding protein from the transferrin family has been reported to have numerous functions. Even though Lf was first isolated from milk, it is also found in most exocrine secretions and in the secondary granules of neutrophils. Antimicrobial and anti-inflammatory activity reports on lactoferrin identified its significance in host defense against infection and extreme inflammation. Anticarcinogenic reports on lactoferrin make this protein even more valuable. This review is focused on the structural configuration of iron-containing and iron-free forms of lactoferrin obtained from different sources such as goat, camel and bovine. Apart for emphasizing on the specific beneficial properties of lactoferrin from each of these sources, the general antimicrobial, immunomodulatory and anticancer activities of lactoferrin are discussed here. Implementation of nanomedicinial strategies that enhance the bioactive function of lactoferrin are also discussed, along with information on lactoferrin in clinical trials.
Highlights
Milk proteins are considered to be the most important source of bioactive peptides, as an increasing number of bioactive peptides have been identified in milk protein hydrolysates
Lf activated the natural killer (NK) cells, enhanced antibody dependent cell cytotoxicity and increased the production of macrophages [32]. Human Lf (hLf) has been found to play a role in the nutritional activity by increasing the thymidine content in damaged crypt cells helping in their recovery and development [33]. hLf is used as a diagnostic marker as its immunochemical detection in the feces indicates the presence of gastrointestinal disorders and risk of colon cancer [34]
It was revealed that these NCs showed highly promising anti-inflammatory properties and induced reversal of OA by dissoluting the calcium pyrophosphate crystals found in mice joints [38]
Summary
Milk proteins are considered to be the most important source of bioactive peptides, as an increasing number of bioactive peptides have been identified in milk protein hydrolysates. This natural protein is proving to be a highly promising biodrug in anticancer research due to its potential use as a natural agent for combating cancer. The use of chemotherapeutic agents has posed a major risk of failure due to the development of drug-resistant cancers. This limitation demands the need of a natural molecule that has patient compliance and can possibly completely eradicate the primary tumor, eliminating the risk of recurrence. Lactoferrin (Figure 1) is considered to be an important host defense molecule and has a diverse range of physiological functions such as antimicrobial/antiviral activities, immunomodulatory activity, and antioxidant activity [11,12]. All the three forms are known to inhibit the activity of Akt (protein kinase B), survivin and to activate p21, p27, p38, and JNK (c-Jun N-terminal kinase) and to induce the release of caspase-8, caspase-3, and cytochrome c to induce apoptosis [14,23]
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