The role of whey acidic protein four-disulfide-core proteins in respiratory health and disease.

Members of the whey acidic protein (WAP) or WAP four-disulfide-core (WFDC) family of proteins are a relatively under-explored family of low molecular weight proteins. The two most prominent WFDC proteins, secretory leukocyte protease inhibitor (SLPI) and elafin (or the precursor, trappin-2), have been shown to possess multiple functions including anti-protease, anti-bacterial, anti-viral and anti-inflammatory properties. It is therefore of no surprise that both SLPI and elafin/trappin-2 have been developed as potential therapeutics. Given the abundance of SLPI and elafin/trappin-2 in the human lung, most work in the area of WFDC research has focused on the role of WFDC proteins in protecting the lung from proteolytic attack. In this review, we will outline the current evidence regarding the expanding role of WFDC protein function with a focus on WFDC activity in lung disease as well as emerging data regarding the function of some of the more recently described WFDC proteins.

Through the eye of an electrospray needle: mass spectrometric identification of the major peptides and proteins in the milk of the one-humped camel (Camelus dromedarius).

The milk of the one-humped camel (Camelus dromedarius) reportedly offers medicinal benefits, perhaps because of its unique bioactive components. Milk proteins were determined by (1) two-dimensional gel electrophoresis and peptide mass mapping and (2) liquid chromatography-tandem mass spectrometry (LC-MS/MS) following one-dimensional polyacrylamide gel electrophoresis. Over 200 proteins were identified: some known camel proteins including heavy-chain immunoglobulins and others exhibiting regions of exact homology with proteins from other species. Indigenous peptides were also identified following isolation and concentration by two strategies: (1) gel-eluted liquid fraction entrapment electrophoresis and (2) small-scale electrophoretic separation. Extracts were analyzed by LC-MS/MS and peptides identified by matching strategies, by de novo sequencing and by applying a sequence tag tool requiring similarity to the proposed sequence, but not an exact match. A plethora of protein cleavage products including some novel peptides were characterized. These studies demonstrate that camel milk is a rich source of peptides, some of which may serve as nutraceuticals.

Alergia alimentaria / Food allergies

Las reacciones alérgicas incluyen un amplio espectro de reacciones clínicas. Con una incidencia del 15–30% de las enfermedades alérgicas y afecta a un 8% de los niños y específicamente a la proteína de la leche de vaca entre un 5–15% de los niños. Pueden manifestarse como intolerancia o alergia dando manifestaciones respiratorias, cutáneas o gastrointestinales que pueden ser inducidos por cantidades minimas de la ingesta deproteína y cuyo tratamiento básico es la exclusión de la proteína de leche sobre todo en los primeros años de vida.

Allergic reactions include a wide spectrum of clinical reactions. With a 15-30% incidence of llergicdiseases, affecting 8% of children and specifically to the protein in cow's milk 5-15% of children hey can manifest as intolerance or allergy giving respiratory manifestations, gastrointestinal or skin can be induced by minimal amounts of protein intake and whose basic treatment is the exclusión of milk protein specially inthe early years of life.

The bovine lactation genome: insights into the evolution of mammalian milk.

BACKGROUND: The newly assembled Bos taurus genome sequence enables the linkage of bovine milk and lactation data with other mammalian genomes. RESULTS: Using publicly available milk proteome data and mammary expressed sequence tags, 197 milk protein genes and over 6,000 mammary genes were identified in the bovine genome. Intersection of these genes with 238 milk production quantitative trait loci curated from the literature decreased the search space for milk trait effectors by more than an order of magnitude. Genome location analysis revealed a tendency for milk protein genes to be clustered with other mammary genes. Using the genomes of a monotreme (platypus), a marsupial (opossum), and five placental mammals (bovine, human, dog, mice, rat), gene loss and duplication, phylogeny, sequence conservation, and evolution were examined. Compared with other genes in the bovine genome, milk and mammary genes are: more likely to be present in all mammals; more likely to be duplicated in therians; more highly conserved across Mammalia; and evolving more slowly along the bovine lineage. The most divergent proteins in milk were associated with nutritional and immunological components of milk, whereas highly conserved proteins were associated with secretory processes. CONCLUSIONS: Although both copy number and sequence variation contribute to the diversity of milk protein composition across species, our results suggest that this diversity is primarily due to other mechanisms. Our findings support the essentiality of milk to the survival of mammalian neonates and the establishment of milk secretory mechanisms more than 160 million years ago.

Safety evaluation of a milk basic protein fraction.

Milk products are widely consumed by individuals in the US population in the form of fluid milk and milk-derived products and ingredients. Milk is a good source of calcium, which plays a role in maintaining bone health. In addition to calcium, the whey protein fraction of milk contains basic proteins that have been demonstrated to increase bone metabolism and inhibit bone resorption. A specific basic protein fraction in milk (Milk Basic Protein; MBP) was tested in an acute oral toxicity study, teratology study, subchronic oral toxicity study, and reverse mutation assay and no treatment related adverse effects were found. MBP has been evaluated for its use as an ingredient in food and concluded to be safe for its intended use.

Nomenclature of the proteins of cows' milk--sixth revision.

This report of the American Dairy Science Association Committee on the Nomenclature, Classification, and Methodology of Milk Proteins reviews changes in the nomenclature of milk proteins necessitated by recent advances of our knowledge of milk proteins. Identification of major caseins and whey proteins continues to be based upon their primary structures. Nomenclature of the immunoglobulins consistent with new international standards has been developed, and all bovine immunoglobulins have been characterized at the molecular level. Other significant findings related to nomenclature and protein methodology are elucidation of several new genetic variants of the major milk proteins, establishment by sequencing techniques and sequence alignment of the bovine caseins and whey proteins as the reference point for the nomenclature of all homologous milk proteins, completion of crystallographic studies for major whey proteins, and advances in the study of lactoferrin, allowing it to be added to the list of fully characterized milk proteins.

[Problem of the rational classification of dietary proteins]. / K voprosu o ratsional'noi klassifikatsii pishchevykh belkov.

A classification of food proteins has been proposed based on two new qualitative parameters: potential biological value (BVp) and compensation coefficient (C). BVp determines the balance degree and agreement with the body requirement of food protein amino acids. The C coefficient estimates the value of the food protein aminogram improvement at the expense of the endogenous essential amino acid reserve. According to these parameters food proteins can be divided into 4 classes. Class I includes proper alimentary specific food proteins (milk and egg proteins) possessing mean values of BVp and high C coefficients. Class II proteins are characterized by rather high BVp values, i.e. by a good balance of essential amino acids and C coefficient reaching 0, they are represented by animal proteins (those of meat and fish), and vegetable proteins (those of soybean, rape and cotton). Class III contains proteins of food grains characterized by low BVp values and C coefficients. Class IV contains proteins with zero values of BVp, containing no essential amino acids (for example, gelatin, hemoglobin, zein), but showing high C coefficients. In such cases the nature of compensation differs from that of class I proteins, it is paradoxic and temporary.