Search

Copyright of Progress in Plant Protection is the property of Institute of Plant Protection and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Panallergens are proteins commonly found in nature. Although they are present in unrelated organisms, they perform a similar function in them. Panallergens have highly conserved amino acid sequence regions and a similar three-dimensional structure, and thus meet the requirements for cross-recognition by IgE. Some of them are pathogenesis- releted proteins produced in plant tissues as a result of biotic and abiotic environmental stress. The article describes the most important panallergen families described so far. [ABSTRACT FROM AUTHOR]

The work presents the results of a computer analysis (in silico) applied for the hydrolysis of the selected sequences of the chicken (Gallus gallus) meat proteins to obtain the biologically active peptides. The protein sequences were derived from UniProt database, whereas bioactive peptide sequences -- from the database of protein and bioactive peptides sequences BIOPEP. The combination of enzymes applied to start the proteolysis was: pepsin (EC 3.4.23.1), trypsin (EC 3.4.21.4), and chymotrypsin (EC 3.4.21.1). It was found, that due to the combination of the enzymes applied, the analysed chicken meat proteins potentially released peptides with the activities such as antioxidant, enzyme inhibitors, stimulating different body functions, and antithrombotic. Among the peptides functioning as enzyme inhibitors, ACE inhibitors (i.e. peptides involved in blood pressure reduction) were enzymatically released from all chicken meat protein sequences. Our results prove the suitability of bioinformatic analysis of food components in the design of functional food. [ABSTRACT FROM AUTHOR]

Copyright of Pediatric Endocrinology, Diabetes & Metabolism is the property of Termedia Publishing House and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Phosphorylation and dephosphorylation play a fundamental role in most signaling pathways, as these processes can directly regulate various aspects of protein function. It is estimated that there are about 100,000 potential phosphorylation sites in proteins encoded by the human genome and about 30-50% of all proteins in the cell can be phosphorylated, which is directly related to the functions they perform. To determine whether a given protein is phosphorylated, any changes in its mobility caused by this modification are examined during PAGE electrophoresis. Concurrently, tandem mass spectrometry (MS/MS) allows to identify specific phosphorylation sites. The next step involves the prediction (using in silico analysis) which kinases can phosphorylate a specific site in the given protein. Then, in order to verify the information obtained from databases, in vitro and/or in vivo experiments are carried out.

Adenylate kinase (AK, EC 2.7.4.3) is a ubiquitous phosphotransferase which catalyzes the reversible transfer of high-energy β - and γ-phosphate groups between nucleotides. All classified AKs show a similar structure: they contain a large central CORE region, nucleoside monophosphate and triphosphate binding domains (NMPbd and NTPbd) and the LID domain. Analysis of amino acid sequence similarity revealed the presence of as many as nine human AK isoenzymes, which demonstrate different organ-tissue and intercellular localization. Among these kinases, only two, AK1 and AK2, fulfill the structural and functional criterion by the highest affinity for adenine nucleotides and the utilization of only AMP or dAMP as phosphate acceptors. Human AK isoenzymes are involved in nucleotide homeostasis and monitor disturbances of cell energy charge. Participating in large regulatory protein complexes, AK supplies high energy substrates for controlling the functions of channels and transporters as well as ligands for extracellular P2 nucleotide receptors. In pathological conditions AK can take over the function of other kinases, such as creatine kinase in oxygen-depleted myocardium. Directed mutagenesis and genetic studies of diseases (such as aleukocytosis, hemolytic anemia, primary ciliary dyskinesia (PCD)) link the presence and activity of AK with etiology of these disturbances. Moreover, AK participates in regulation of differentiation and maturation of cells as well as in apoptosis and oncogenesis. Involvement of AK in a wide range of processes and the correlation between AK and etiology of diseases support the medical potential for the use of adenylate kinases in the diagnosis and treatment of certain diseases. This paper summarizes the current knowledge on the structure, properties and functions of human adenylate kinase.

Within the last decade, several antimicrobial peptides (AMPs) have been discovered. Cathelicidins are one family of AMPs characterized by a conserved cathelin domain and a variable C-terminal cationic antimicrobial domain. These peptides are produced by different cells, including leukocytes, epithelial cells and keratinocytes. Besides their direct antimicrobial function, cathelicidins can also regulate the course of inflammation and influence the mechanisms of innate immunity. In this review we discuss the biology of animal cathelicidins, their structure, expression and function.

Recent bioinformatic and genetic analyses of several model plant genomes have revealed the existence of a highly abundant group of signaling peptides that are defined as cysteine-rich peptides (CRPs). CRPs are usually in size between 50 and 90 amino acid residues, they are positively charged, and they contain 4-16 cysteine residues that are important for the correct conformational folding. Despite the structural differences among CRP classes, members from each class have striking similarities in their molecular properties and function. The present review presents the recent progress in research on signaling peptides from several families including: EPF/EPFL, SP11/SCR, PrsS, RALF, LURE, and some other peptides belonging to CRP group. There is convincing evidence indicating multiple roles for these CRPs as signaling molecules during the plant life cycle, ranging from stomata development and patterning, self-incompatibility, pollen tube growth and guidance, reproductive processes, and nodule formation.

Acyltransferases'participate in many metabolic pathways in plants, especially in secondary metabolism pathways. These enzymes catalyse transfer of an acyl group from energy-rich donor molecule to nucleophilic group of an acceptor molecule resulting in ester bond formation. Plant acyltransferases can be divided into two families: serine carboxypeptidase-like acyltransferases (SCPL) and BAHD acyltransferases (named after its first four characterized enzymes). Based on differences in substrate specificity and aminoacid sequence, BAHD acyltransferas-es have been classified into five clades. SCPL acyltransferases utilise energy-rich 1-O-β-D-glucose esters as donors of an acyl group, instead of coenzyme A thioesters, which are substrates for acyltransferases from more abundant BAHD family. SCPL acyliransferases are homologous to hydrolases from serine carboxypeptidases family. They share some structural elements, such as conserved catalitic triad or αβ hydrolase fold.

Heat shock proteins (Hsps) are a class of proteins with highly conserved amino acid sequences. They are widespread in nature; they are found in archeons, true bacteria and eukaryotic organisms. Hsps from various families, commonly interact to execute essential cellular tasks, such as molecular regulation of newly synthesized protein-folding or restoration of the appropriate conformation of denatured and aggregated proteins. In this review we discuss mechanisms of spatial organization of protein structure mediated by Hsp10, Hsp40, Hsp60, Hsp70, Hsp104 (Hsp100) and Hsp110. Interactions between Hsps of different molecular weights are described.

Chemical modifications of proteins are crucial for studying their functions, biophysical properties and cellular localization. The most important is the protein fluorescent modification utilized in biochemistry, molecular biology and medicinal diagnostics. Precision of fluorophore attachment in certain part of the protein or amino acid sequence is very important for the labeling and subsequent characterization or protein applications. One of the most important type of probes used for fluorescent protein labeling are biarsenical probes. They are not only to localize proteins in cell but based on their chemical properties they are widely applied for studying protein folding, degradation, control of the activity, protein inactivation with singlet oxygen, oligomerization and protein purification. Here, author presents principles of protein labeling with biarsenical probes with special attention to factors affecting proper protein modification. Review includes the most interesting applications of biarsenical probes in molecular biology, molecular diagnostics and analytical biochemistry.

Newly identified metabotropic GPR17 receptors are structurally related to purinergic P2Y receptors and cysteinyl leukotriene receptors. Re- cent studies showed that they play an important role in maturation of oligodendrocyte precursor cells. This review describes structure and pharmacological characterization of GPR17 receptors. It also summarizes knowledge about role of GPR17 receptors in physiology and patho- logy of nervous system, with special attention to remyelination processes.

The actin family consists of highly conservative proteins, abundant in all eukaryotic cells. Actin plays different roles in cell functioning including cell motility, maintenance of cell shape, signal transduction and transcription. The beta and y cytoplasmic actins are ubiquitously present in all cell types and are essential for cell survival. They differ only by four amino acids located at the N-terminus of the polypeptide chain. The proportion of cytoplasmic actins varies and depends on the cell type. In addition, it changes in pathological conditions. There is also some evidence that beta and gamma actins are located in different cytoplasmic areas, what suggests functional differences between them. Studies conducted in recent years, demonstrating the increase or reduction of cytoplasmic actin isoforms expression allow for better understanding of the role of these proteins in cell functioning. In this article, we present contemporary view on this subject.

The neurotrophins play an important role in the development of the nervous system. These trophic factors affect the cells through the neurotrophin receptors Trk and p75NTR. Trk (tyrosine kinase receptor) mediated signaling promotes survival and growth, while p75NTR-mediated signaling promotes cell death. The structure of p75NTR and its role in the regulation of survival, growth and induction of apoptosis are discussed. p75NTR can interact with the aggregated form of Aβ peptides and by influencing protein tau hyperphosphorylation plays an important role in etiopathogenesis of Alzheimer's disease.

Of the plant allergens listed in the Official Allergen Database of the International Union of Immunological Societies, approximately 25% belong to the group of pathogenesis-related proteins (PRs). They have been classified into 17 PR families based on similarities in their amino acid sequence, enzymatic activities, or other functional properties. Plant-derived allergens have been identified with sequence similarities to PR families 2, 3, 4, 5, 8, 10, and 14. The main birch allergen in northern Europe is a class 10 (PR-10) protein from the European white birch (Betula pendula) termed Bet v 1. Pollen of other Fagales species contains PR-10 homologues that share epitopes with Bet v 1, as do several fruits, nuts and vegetables. Among the plant food fruits of the Rosaceae family are the most frequently responsible for allergenic reactions. It is documented, that approximately 2% of European population is allergic to apples. The article presents molecular characterization of PR-10 proteins with regard to their structure and function as well as apple Mal d 1 gene-determined allergenicity.

The HIT superfamily consists of proteins that share the histidine triad motif, His-X-His-X-His-X-X (where X is a hydrophobic amino acid), which constitutes enzymatic catalytic center. These enzymes act as nucleotidylyl hydrolase or transferase, and the mutation of the second histidine in the triad abolishes their activity. HIT proteins were found ubiquitous in all organisms and they were classified into 5 branches, which are represented by human proteins: HINT1, FHIT, Aprataxin, GALT and DCPS. Because HINT1 orthologs, which belong to the evolutionally oldest family branch, were found from prokaryotes to eukaryotes, it is clear that HIT motif was conserved during the evolution what means that the enzymatic activity is necessary for functions of these proteins. However, in few cases, e.g. HINT1 and FHIT, the connection between the biological function and the enzymatic activity is still obscure. In this review, the relations between biology and activity for 7 HIT proteins, which were found in human, are highlighted.

Peptides from the pyrokinin (PK) family are a large, structurally and functionally diverse group of the insect neuropeptides produced by neurosecretory cells of the insect nervous system. This family contains short and long peptides which share C-terminal -FXPRLa amino acid sequence. Pyrokinins regulate the visceral muscle contractions, pheromone biosynthesis, pupariation and diapause duration in insects. They are encoded by two genes PBAN and capa, which are mainly expressed in the suboesophageal ganglion. Peptides are then transported to the retrocerebral complex and released into haemolymph. Recent studies are focused on application of pyrokinins as biopesticides in the regulation of insect pests growth and development.

In our study we analyzed the nucleotide sequence of the C- terminal 256 bp fragment of the myfA gene encoding MyfA protein, the major subunit of Yersinia enterocolitica Myf fimbriae. We examined ten representative strains of major Y. enterocolitica pathogenic bioserotypes belonging to European (4/O3; 2/O9; 3/O5,27) and American (1B/O8) phylogenetic lineages. DNA sequencing revealed that consensus nucleotide sequences of the tested myfA fragment were indistinguishable in all the tested strains. The resulting common consensus sequence found in our study was identical to the corresponding fragment of reference sequences Z21953 and NC008800 deposited in GenBank database for pathogenic Y. enterocolitica strains. In contrast, 18 point mutations leading to 13 amino acid substitutions were found when the common consensus sequence was aligned to sequence AY966879 determined for the myfA homologue detected by PCR in Y. enterocolitica 1A strain. The strong conservation of the nucleotide and amino acid sequence of myfA gene among virulent bioserotypes of Y. enterocolitica indicate that fimbriae MyF could play important role in pathogenesis, even before the divergence of European and American lineages.

The ABO human blood group system consists of A antigens, B antigens, and antibodies against these antigens. The antigenic determinants are synthesized in the Golgi apparatus by specific glycosyltransferases which transfer proper sugars to an oligosaccharide acceptor, called H antigen. N-acetylgalactosaminotransferase (transferase A) uses a UDP-GalNac donor to convert the H antigen to A antigen, whereas galactosyltransferase (transferase B) uses a UDP-galactose donor to convert the H antigen to B antigen. The amino-acid sequences of transferases A and B differ by four residues, of which only two cause a change in enzyme specificity. These residues are Leu/Met266 and Gly/Ala268 in transferases A and B, respectively. Structural studies revealed that the presence of amino acids with bulky side chains (methionine and alanine) in transferase B cause its inability to bind N-acetylgalactosamine. The recessive trait O, in which antigens A and B are not present, is caused by the expression of an incomplete enzyme as a result of a base deletion and a subsequent reading frame change. In addition to the basic ABO gene variants, several alleles are rarely found that may lead to the expression of enzymes with different specificities. In this article the mechanism of the synthesis of A and B antigens, the molecular background of ABO gene variablity, their allelic variants, and possible mechanisms by which they emerge are described.

The aim of the present investigation was personal identification of an unknown man whose remains were exhumed four years after burial. The femur of the deceased was secured for the genetic analysis. The comparative material included buccal swabs collected from the putative relatives of the deceased, i.e. the wife, son and brother. Genomic DNA was extracted from the bone using two methods: traditional isolation with phenol/chloroform and as a alternative technique, a simple and rapid method described by T. Kalmár et al. The results were then compared. The specimens underwent DNA amplification using the AmpFISTRSEfiler PCR Amplification Kit. The authors obtained a full STR profile of the unknown man from each isolate, yet the DNA extraction method proposed by T. Kalmár et al. allowed for simpler and faster isolation of genetic material. The statistical analysis of the obtained results confirmed the paternity of the deceased and established his son as his rightful child (P = 99.999999%), also confirming the consanguinity between the investigated individual and his putative brother (P = 99.9999%).

Bacteria require iron for growth. To acquire environmental iron and transport it into the bacterial cell, they evolved sophisticated mechanisms. However, an excess of iron may be toxic for the cell, mostly by its involvement in the generation of reactive species. To date, no mechanisms of excretion of iron outside the bacterial cell were found, thus cellular iron level regulation is performed by control of its transport and appropriate synthesis of iron-coordinating and iron-storage proteins. The majority of genes engaged in iron homeostasis in the bacterial cell are under a global regulator, repressor Fur. In this work, structure and function of proteins comprising Fur family and their involvement in iron level regulation is presented.

Proinsulin connecting peptide (C-peptide) has been initially regarded as deprived of biological functions other than correct scaffolding of insulin. This was caused by the lack of evident effect of C-peptide administration to healthy subjects or animals. At present, in view of numerous studies concerning its structure, membrane binding and biological functions, C-peptide seems to constitute a crucial role in the pathogenesis of complications in diabetes mellitus type 1 (DM1). Patients who maintain high remnant insulin secretion (and therefore also of C-peptide) develop complications such as nephropathy, neuropathy and later microangiopathy with a milder clinical course. In this article we have covered molecular and cellular aspects of C-peptide functioning, such as: activation of protein kinase C, Na+,K+- ATP-ase, nitric oxide synthase, MAP and ERK 1/2 kinases, improvement of nerve conduction velocity and interactions with exogenous and endogenous insulin. We also outline the clinical consequences of deficiency of this underestimated peptide along with its potential therapeutical possibilities in the primary and secondary prevention of DM1 complications.

Tuftsin, a natural tetrapeptide of sequence TKPR, occuring in the blood of humans and other mammals, capable of stimulating certain white blood cells (monocytes, macrophages, and neutrophils), was isolated at Tufts University in 1970 by Najjar and Nishioka. Tuftsin is a compound with a wide spectrum of biological activities, notable enhances phagocytosis, immune response, bactericidal, tumoricidal and antifungal activities. This article concerns new analogues and properties of tuftsin.

In the last decade the abnormalities in male infertility became the main problem of more than 50% couples. The main reasons of male infertility are abnormal gonadotropin releasing hormone (GnRH) secretion, pituitary gland diseases and presence of testicular genetic defects. The male infertility also may result from chemotherapy, radiotherapy and viral infections. The main genetic factors responsible for male infertility encompass the mutations of genes, which encode important factors of spermatogenesis. Recently mRNAs of numerous genes have been identified in spermatozoa. The first transcripts found in spermatozoa included protamine 1 and 2 (PRM1 and PRM2). Protamines are basic polypeptides, which form complex with DNA in spermatids and spermatozoa. Structure of PRM1 and PRM2 genes and function of these proteins suggest the possible relationship between of protamines expression disorders and male infertility. The PRM1, PRM2 and transition proteins 1 and 2 (TP1 and TP2) play important role in DNA condensation. We attempted to present current knowledge regarding structure and expression regulation of PRM1 and PRM2 genes. We also discussed the effect of disorders of PRM1 and PRM2 expression on male infertility.

The immunoglobulins of the Camelidae family belonging to subclasses IgG2 and IgG3 consist of heavy chains only. The lack of light chains is caused by a point mutation in the heavy-chain gene, resulting in the loss of the splice consensus signal and the removal of the entire CH1 domain together with introns. The heavy-chains antibodies also contain longer hinge regions and conservative amino-acid substitutions in the framework regions. Despite the lack of light chains, the heavy-chain antibodies reveal normal antigen binding ability and effector functions. The heavy-chain antibodies are relatively easy to clone and possess good stability, high specificity, low molecular weight, and the ability to recognize unique epitopes. Possible areas of application of heavy-chain antibodies include their use as in vivo imaging reagents and sources of peptide-based drugs.

Lysosomal carboxypeptidase A (cathepsin A) is synthetized in the form of preproenzyme, which undergoes to active enzyme as a result of post-translational modification. It splits off C-terminal amino acid residues from peptides and proteins and synergizes with other proteases in degradation of cellular proteins in lysosomes. Lysosomal carboxypeptidase A has an effect on peptide hormones and peptides of biological activity of tissues and body fluids as well. It forms complexes with some glycosidases that protects them against proteolytic degradation. Deficiency of this enzyme induces storage diseases. Lysosomal carboxypeptidase A as multifunctional enzyme plays an important regulatory role in organismal metabolism.

The article presents the current knowledge on the proteines under question. The first analysed E-S products released by G. duodenalis was a polydisperse hydrophobic complex (16.5-225 kDa), protease VI sensitive, chloroform-methanol insoluble. Based on inhibition studies cysteine protease and metalloprotease were detected in the complex. The further analysis revealed that a 58 kDa heat stable as wall as protease sensitive glycoprotein secreted by G. duodenalis trophozoites is highly immunogenic for the hosts. Before encystation, G. duodenalis trophozoites secrete leucine-rich cyst wall proteins: CWP1, CWP2 and CWP3. Steady-state levels of CWPs gene transcripts are low in non-encysting trophozoites but increase more than 100-fold during encystation. Another protein, which expression also increases during encystation is gGSP (Giardia Granule-Specific Protein). The protein possesses typical strucutre of calcium-binding proteins. Inhibition of gGSP expression abolishes cyst wall formation, suggesting that this protein regulates Ca(2+)-dependent degranulation of encystation-specific secretory vesicles (ESVs) during cyst wall formation.

Leukaemia inhibitory factor (LIF) is a multifunctional cytokine, which plays a role in growth-promotion and differentiation, regulates calcium and bone metabolism, induces acute phase proteins and causes cachexia in organisms with neoplastic disorders. Moreover, LIF participates in the induction of inflammation, and therefore represents an important pathogenic factor of many disorders. The multifunctional properties of LIF have become of special interest to investigators from different disciplines of medicine.

Peptide histidine-isoleucine (PHI) and its human analogue peptide histidine-methionine (PHM) are members of a superfamily of structurally related peptides embracing, among others, pituitary adenylate cyclase-activating polypeptide (PACAP), vasoactive intestinal peptide (VIP), peptide histidine-valine (PHV), and helodermin. All the peptides display a pleiotropic biological activity. PHI, PHM, PHV and VIP are co-synthesized from the same precursor and share high levels of structural and functional similarity. These peptides may act through common receptors and are widely distributed throughout the body tissues (the central nervous system, gastrointestinal tract, respiratory system, and reproductive system); however, their role remains largely unknown. Changes in the levels of the peptides in the course of different diseases suggest their possible importance and usefulness in diagnostics. Moreover, the neurotrophic and neuroprotective properties of PHI suggest, by analogy to VIP or PACAP, its therapeutic potential in many neurodegenerative diseases, such as Alzheimer's and Parkinson's disease.

Proteases (peptide hydrolases) aside from known catabolic functions and protein processing play numerous roles in many tasks imposed by a parasitic life cycle; this includes parasite immunoevasion, excystment/encystment, tissue penetration and digestion of host tissue for nutrition. They have been identified in biological systems from viruses to vertebrates. Proteases are divided into four major groups on the basis of the catalytic mechanism used during the hydrolytic process - serine, aspartic, cysteine and metalloproteinases; other 'undefined' or cryptic proteases may also exist. There are a number of excellent reviews covering general parasite proteinases but by far the largest number of papers in the literature report on enzymes belonging to the papain superfamily of cysteine proteinases. It turns out, however, that although many different proteases have been characterized in parasitic helminths many of them have yet to be discovered.

The human beta 2-adrenoceptor is a member of the seven-transmembrane family of receptors. It is expressed in many cell types such as airway smooth muscle cells, neutrophils, eosinophiles, alveolar macrophages and airway epithelial cells. The beta 2-adrenoceptor agonists are the most important group of bronchodilator drugs used in the treatment of asthma. They are classified by their selectivity, affinity for the receptor, potency and pharmacological efficacy. The gene encoding the beta 2-adrenergic receptor is highly polymorphic in the human population. Polymorphism affecting amino acids 16, 27 and 164 are the most common and they have been shown to correlate with some clinical features of asthma, including airways reactivity. They can modulate the behaviour of the beta 2-receptor, altering ligand binding and the characteristics of down-regulation following agonist exposure. The homozygous glycine-16 (Arg-->Gly) variant of the beta 2-adrenoceptor is known to predispose to agonist-induced down-regulation and desensitization, and may play a role in the pathogenesis of asthma severity. The polymorphism at position 27 (Gln-->Glu) is associated with decreased airway responsiveness. The polymorphic variant 164 (Thr-->Ile) shows impaired agonist binding and decreased adenylyl cyclase activity. No convincing evidence has been presented demonstrating a linking of asthma per se with this receptor polymorphism.

Unlabelled: The principles of ionic selectivity of the two crystallised bacterial ion channels are described. These channels are: the potassium channel KcsA, whose amino-acid sequence is homologous to the eukaryotic voltage--dependent potassium channels and the chloride channel EcClC that is a prokaryotic member of the ClC family of chloride channels., In Conclusion: although the overall molecular architecture of KcsA is different from that of EcClC, the selectivity filters in both cases show similarities. They both utilise helix dipoles organised within the channel molecule in such a fashion to produce electrostatically favourable environment for anions (in the case of EcClC) or cations (in the case of KcsA).

Prometalloproteinases are activated by serine proteases, MMP-3, leucocytic elastase, furin, furin-like proteases and by membrane-type metalloproteinases as well. They form complexes with some proMMPs and thus they modify their activation.

Biochemical part of the paper presents the structure, biosynthesis and degradation of the endothelins. Physiological chapter deals with endothelin-1 endocrine and mitogenic action as well as its impact on diuresis, natriuresis and cardiovascular system. In the clinical part of the article the role of endothelin-1 in essential hypertension, congestive heart failure and chronic renal failure is described.

Matrix metalloproteases (MMPs) are synthesized in the form proenzymes. They are activated in the process of limited proteolysis and non-enzymatically by active forms of oxygen. Activity of these enzymes is controlled by tissue inhibitors of metalloproteases (TIMPs).

Tissue factor pathway inhibitor (TFPI) is an important regulator of blood coagulation. It was described as antyconwertin (AC), extrinsic pathway inhibitor (EPI) and lipoprotein-associated coagulation inhibitor (LACI). TFPI is a glycoprotein, which is mainly synthesized by vascular endothelial cells. The concentration of this enzyme in plasma is low (100 ng/ml). TFPI inhibits activity of factor Xa and complex FVIIa/TF. Changes TFPI activity play an important role in coagulation disorders and presently the function of TFPI in various kinds of diseases is discussed.