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PubMed1992

Expression, purification, and characterization of the recombinant kringle 1 domain from tissue-type plasminogen activator.

A novel fusion protein expression plasmid that allows ready purification and subsequent facile release of the target molecule has been constructed and employed to express in Escherichia coli and purify the tissue plasminogen activator kringle 1 domain ([K1tPA] residues C92-C173). The resulting plasmid encodes the tight lysine-binding kringle (K)1 domain of human plasminogen ([K1HPg]) followed by a peptide (PfXa) containing a factor Xa-sensitive bond, downstream of which [K1tPA] was inserted. The recombinant (r) [K1HPg]PfXa[K1tPA] fusion polypeptide was purified from various cell fractions in one step by Sepharose-lysine affinity chromatography. After cleavage with fXa, the mixture was repassaged over Sepharose-lysine, whereupon the r-[K1tPA]-containing polypeptide passed unretarded through the column. A homogeneous preparation of this material was then obtained after a simple step employing fast protein liquid chromatography. The purified r-[K1tPA], which contained the amino acid sequence SNAS[K1tPA]S, provided an amino-terminal amino acid sequence, through at least 20 amino acid residues, that was identical to that predicted from the cDNA sequence. The molecular mass of r-SNAS[K1tPA]S, determined by electrospray mass spectrometry, was 9621.9 +/- 4.0 (expected molecular mass, 9623.65). 1H-NMR spectroscopy and thermal stability studies of r-SNAS[K1tPA]S revealed that the purified material was properly folded and similar to other isolated kringle domains. Additionally, employment of this methodology revealed that only a very weak interaction between epsilon-aminocaproic acid and the isolated r-[K1tPA] domain occurred.

Amino Acid Sequence↗
PubMed2001

Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a.

The plasminogen receptors responsible for enhancing cell surface-dependent plasminogen activation expose COOH-terminal lysines on the cell surface and are sensitive to proteolysis by carboxypeptidase B (CpB). We treated U937 cells with CpB, then subjected membrane fractions to two-dimensional gel electrophoresis followed by ligand blotting with (125)I-plasminogen. A 54-kDa protein lost the ability to bind (125)I-plasminogen after treatment of intact cells and was purified by two-dimensional gel electrophoresis and then sequenced by mass spectrometry. Two separate amino acid sequences were obtained and were identical to sequences contained within human and rat TIP49a. The cDNA for the 54-kDa protein matched the human TIP49a sequence, and encoded a COOH-terminal lysine, consistent with susceptibility to CpB. Antibodies against rat TIP49a recognized the plasminogen-binding protein on two-dimensional Western blots of U937 cell membranes. Human (125)I-Glu-plasminogen bound specifically to TIP49a protein, and binding was inhibited by epsilon-aminocaproic acid. A single class of binding sites was detected, and a K(d) of 0.57 +/- 0.14 microm was determined. TIP49a enhanced plasminogen activation 8-fold compared with the BSA control, and this was equivalent to the enhancement mediated by plasmin-treated fibrinogen. These results suggest that TIP49a is a previously unrecognized plasminogen-binding protein on the U937 cell surface.

ATPases Associated with Diverse Cellular Activitie↗
PubMedDate not supplied

Light from Maillard reaction: photon counting, emission spectrum, photography and visual perception.

Several authors have reported on high-sensitivity measurement of oxygen-dependent low-level chemiluminescence (CL) from Maillard reactions (MR), i.e. nonenzymatic amino-carbonyl reactions between reducing sugars and amino acids (also referred to as nonenzymatic browning). Here we report for the first time, that light from Maillard reactions can be seen by the human eye and also can be photographed. In parallel with visual perception and photography CL was monitored by means of a CL-detection programme of a liquid scintillation counter (LSC, single photon rate counting). CL emission spectrum was recorded by a monochromator-microchannel plate photomultiplier arrangement. CL intensity from reaction of 6-aminocaproic acid with D-ribose (200 mg each) in 5 mL H2O at pH 11 at 95 degrees C was high enough for visual perception after adaptation to absolute darkness. Reaction in dimethylsulphoxide (DMSO) exhibited strongly enhanced CL (10 mg each in 5 mL were sufficient for visual detection) and could be photographed (15 minutes' exposure, ASA 6400); all characteristics of Maillard specific CL (O2-dependence, no CL from nonreducing sugars, inhibition by sulphur compounds) remained. Visual detection of CL and measurement by LSC were in full concordance. The CL emission spectrum showed two broad peaks at around 500 nm and 695 nm. Fluorescence emission of the brown reaction mixture matched the blue-green part of the CL emission spectrum. Emission of visible light during Maillard reactions may partly originate from oxygen-dependent generation of excited states and energy transfer to simultaneously formed fluorescent products of the browning reaction.

Amino Acids↗
PubMed2004

Surgical and clinical management of a patient with Glanzmann thrombasthenia: a case report.

A 6-year-old girl with Glanzmann thrombasthenia presented with caries and periapical lesions in the primary mandibular second molars and moderate gingivitis of the maxillary and mandibular anterior teeth. Dental extraction was recommended, and before every surgical intervention, the patient underwent platelet-concentrate transfusion to prevent hemorrhage. Epsilon aminocaproic acid was administered 6 hours before, and 48 hours after every dental procedure to prevent bleeding. In this case, treatment was effective in the prevention of hemorrhagic complications, during the required dental procedures.

Aminocaproates↗
PubMed1995

Role of conserved amino acid residues in the complementarity determining regions on hapten-antibody interaction of anti-(4-hydroxy-3-nitrophenyl) acetyl antibodies.

Monoclonal antibodies (mAbs) specific to (4-hydroxy-3-nitrophenyl)acetyl (NP) were prepared at various times after immunization and the amino acid sequences of VH and V lambda 1 in these mAbs were deduced from cDNA nucleotide sequences. Replacements due to somatic mutation were not found in day 7 mAbs but were found in those of days 14, 84 and 294. The affinity of day 7 mAbs to NP-glycine(NP-Gly) was in the order of 10(4) M-1 and it increased about 8000-fold with time after immunization. The extrinsic circular dichroism (CD) spectrum of the NP-epsilon-aminocaproic acid (NP-Cap)/Ab complex was unique for each mAb, although the spectra were grouped into two types, which tended to shift from one type to another with time, suggesting a variation in the micro-environments around NP-Cap in the combining sites. All these data indicate that the structure of the combining site was altered by somatic mutation; however, the fine-specificity measured by cross-reactivity with hapten analogues did not change significantly with time. We examined the amino acid residues in CDRs responsible for recognition of NP-haptens by comparing the amino acid sequences of anti-NP mAbs. Analyses revealed the presence of several conserved amino acid residues in CDRs of VH and V lambda 1, such as Tyr-32H, and Tyr-60H, in addition to a core segment involving Arg-50H.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1981

Excess alpha chains are lost from beta-thalassemic reticulocytes by proteolysis.

During incubation of reticulocytes from patients with beta-thalassemia, after labeling of the hemoglobin with radioactive amino acids, the excess alpha chains are gradually lost from the cells. The aim of this study was to investigate the mechanism of this phenomenon. A system was developed in which reticulocytes from beta-thalassemia patients are labeled with [3H]leucine, washed several times in nonradioactive medium, and then incubated in the same medium containing puromycin added in order to stop further protein synthesis. The results have clearly shown that excess alpha chains are gradually degraded by proteolysis. N-ethylmaleimide or epsilon-aminocaproic acid inhibited the proteolysis of free alpha chains. The addition of either ATP or hemin did not change the rate of alpha chain degradation. The time required to degrade 50% of the pool of free alpha chains was directly dependent on the initial value of this pool. This finding suggests the absence of a significant individual variation in the ability to proteolyse free alpha chains.

Adenine↗
PubMed2006

A novel type of lysine oxidase: L-lysine-epsilon-oxidase.

The melanogenic marine bacterium M. mediterranea synthesizes marinocine, a protein with antibacterial activity. We cloned the gene coding for this protein and named it lodA [P. Lucas-Elío, P. Hernández, A. Sanchez-Amat, F. Solano, Purification and partial characterization of marinocine, a new broad-spectrum antibacterial protein produced by Marinomonas mediterranea. Biochim. Biophys. Acta 1721 (2005) 193-203; P. Lucas-Elío, D. Gómez, F. Solano, A. Sanchez-Amat, The antimicrobial activity of marinocine, synthesized by M. mediterranea, is due to the hydrogen peroxide generated by its lysine oxidase activity. J. Bacteriol. 188 (2006) 2493-2501]. Now, we show that this protein is a new type of lysine oxidase which catalyzes the oxidative deamination of free L-lysine into 6-semialdehyde 2-aminoadipic acid, ammonia and hydrogen peroxide. This new enzyme is compared to other enzymes related to lysine transformation. Two different groups have been used for comparison. Enzymes in the first group lead to 2-aminoadipic acid as a final product. The second one would be enzymes catalyzing the oxidative deamination of lysine releasing H2O2, namely lysine-alpha-oxidase (LalphaO) and lysyl oxidase (Lox). Kinetic properties, substrate specificity and inhibition pattern show clear differences with all above mentioned lysine-related enzymes. Thus, we propose to rename this enzyme lysine-epsilon-oxidase (lod for the gene) instead of marinocine. Lod shows high stereospecificity for free L-lysine, it is inhibited by substrate analogues, such as cadaverine and 6-aminocaproic acid, and also by beta-aminopropionitrile, suggesting the existence of a tyrosine-derived quinone cofactor at its active site.

2-Aminoadipic Acid↗
PubMed1993

Functional independence of the kringle 4 and kringle 5 regions of human plasminogen.

As part of continuing studies to evaluate whether the kringle domain regions of human plasminogen (HPg) exhibit independent conformational properties, simple model systems are required. Toward this end, we have constructed cDNA regions of HPg encoding its kringle 4 ([K4HPg]) and kringle 4-5 ([K4HPgK5HPg]) regions, expressed these gene fragments in bacterial cells, and purified the recombinant (r) products. The resulting r-[K4HPgK5HPg] was also employed to obtain the r-[K5HPg] domain of HPg by limited elastolytic digestion of this double-kringle polypeptide. The omega-amino acid ligand binding properties and thermal denaturation characteristics of r-[K4HPg], r-[K5HPg], and r-[K4HPgK5HPg] were determined, along with those for the [K5HPg] domain linked to the protease (P) region of HPg ([K5HPg]P). This allowed us to evaluate whether the conformational properties of the [K5HPg] module were influenced by the presence of its neighboring domains in HPg. The temperature midpoint of maximum heat capacity, Tm (and calorimetric enthalpy, delta H), for thermal denaturation of r-[K4HPg] was 57.8 degrees C (79.8 kcal/mol) in the absence of epsilon-aminocaproic acid (EACA) and 70.8 degrees C (93.7 kcal/mol) in the presence of that ligand. The corresponding values for isolated r-[K5HPg] were 50.4 degrees C (78.4 kcal/mol) and 61.0 degrees C (89.8 kcal/mol), respectively. These parameters for the isolated kringles were essentially unchanged when these same kringle domains were present in the r-[K4HPgK5HPg] and [K5HPg]P covalently linked pairs. Similarly, the thermodynamic characteristics (delta G, delta H, and delta S) that describe the binding energy of EACA to r-[K4HPg] at 25 degrees C were -6.3 kcal/mol, -4.5 kcal/mol, and 6.0 eu, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMedDate not supplied

Intracranial aneurysms and subarachnoid hemorrhage. A cooperative study. Antifibrinolytic therapy in recent onset subarachnoid hemorrhage.

In this cooperative study among 13 institutions, 502 patients were treated with antifibrinolytic medication (epsilon-aminocaproic acid or tranexamic acid) within a 14-day period following rupture of an intracranial aneurysm. Mortality at the end of 14 days was 11.6%; proved rebleed rate was 12.7%. Patients with an internal carotid or anterior cerebral aneurysm had the highest mortality and rebleed rate. Most rebleeds occurred between the sixth and eleventh days following the initial bleed. Significantly higher mortality was reported among patients with cerebral vasospasm, yet rebleed rate was no different among those patients with or without vasospasm. The same pattern was observed among patients with a mean blood pressure value above and below 110 mm Hg. We conclude that antifibrinolytic therapy provides beneficial treatment to patients with recent onset subarachnoid hemorrhage (SAH) following rupture of an intracranial aneurysm.

Age Factors↗
PubMed1987

Binding of tissue plasminogen activator to human umbilical vein endothelial cells.

Binding of purified recombinant human tissue plasminogen activator to cultures of human umbilical vein endothelial cells (HUVEC) was studied in vitro. 125I-tPA was shown to bind to HUVEC in a specific, saturable, and dissociable manner. Scatchard analysis revealed a low affinity binding site with Keq = 4.2 X 10(6) M-1 and 1.2 X 10(7) sites per cell. Binding of tPA was inhibited by L-lysine, e-aminocaproic acid, and D-phenylalanyl-L-prolyl-L-arginine chloromethyl ketone but not by carbohydrates including mannose, galactose, N-acetyl glucosamine and N-acetyl galactosamine. Neat human plasma abrogates but does not totally inhibit binding of tPA to HUVEC. These results may indicate a role for endothelial cells in the removal of tPA from the circulation in vivo.

Aminocaproates↗
PubMed2002

Renal complications of sickle cell disease: managing for optimal outcomes.

A broad spectrum of renal changes is observed in patients with sickle cell anemia, and ideal therapeutic measures for the management of these alterations are still being studied. Affected patients have deficient urinary concentration and potassium excretion. Perhaps owing to a compensatory mechanism, the proximal tubules are in a condition of "hyperfunction", with increased sodium and phosphorus reabsorption and greater creatinine and uric acid secretion. Mild tubular acidosis may be present. No treatment has been reported for these tubular changes, except for care in the maintenance of hydration. The use of anti-inflammatory drugs is being studied in order to inhibit the prostaglandins involved in the process. Increased renal blood flow, glomerular filtration rate, and filtration fraction are frequent findings. Hematuria commonly occurs as a consequence of red blood cell sickling in the renal medulla, papillary necrosis, or even renal medullary carcinoma. Measures such as increased fluid ingestion, urine alkalinization and, if necessary, administration of epsilon-aminocaproic acid and certain invasive procedures have been proposed to treat hematuria. Nephropathy in patients with sickle cell anemia can be manifested by proteinuria and, more rarely, nephrotic syndrome. Drugs such as prednisone and cyclophosphamide are ineffective for the treatment of patients with nephrotic syndrome. Angiotensin converting enzyme inhibitors decrease proteinuria, but their long-term effect in preventing the progression of glomerular disease has not been established. Chronic renal failure, although infrequent, may be one of the manifestations of this disease. Hemodialysis and transplantation are satisfactory therapeutic options for patients with end-stage renal disease.

Anemia, Sickle Cell↗
PubMed2006

Perioperative management of a patient with Bernard-Soulier syndrome for third molar surgery.

Bernard-Soulier Syndrome (BSS) is a disease characterized by prolonged bleeding time, thrombocytopenia, and extremely large platelets and has a prevalence of less than 1 in 1,000,000. Patients with disorders of coagulation and bleeding can be among the most difficult surgical patients to manage. Perioperative hemorrhage can contribute to life-threatening complications in even the most routine surgical procedures. Because of the rarity of BSS, there are no well-defined protocols for the management of perioperative bleeding associated with this condition. Treatment with preoperative and intraoperative systemic aminocaproic acid, HLA-matched platelets, and topical gelfoam and thrombin resulted in sustained hemostasis and a durable healing response. For those rare few afflicted with this disease, we present a combined systemic and topical approach that may be helpful in the control and prevention of perioperative hemorrhage in this and other similar platelet disorders.

Adolescent↗
PubMed1995

Concomitant treatment with factor IX concentrates and antifibrinolytics in hemophilia B.

Concomitant use of the monoclonal antibody-purified factor IX concentrate (Mononine, Armour Pharmaceutical Company, Collegeville, Pa.) and two antifibrinolytic agents, epsilon-aminocaproic acid (EACA; Amicar, Immunex, Seattle, Wash.) or tranexamic acid (AMCA; Cyklokapron, Kabi Pharmacia, Piscataway, N.J.) was examined for safety and efficacy in patients with hemophilia B. In a retrospective review of 19 patients treated with monoclonal antibody-purified factor IX and EACA on 35 occasions, bleeding was successfully controlled and no instances of clinical thrombotic complications were reported; one instance of urticaria resolved without additional treatment. The use of EACA or AMCA in combination with monoclonal antibody-purified factor IX was also examined prospectively in a study of 9 patients. Bleeding was effectively controlled and no thrombotic events were detected clinically with either antifibrinolytic agent. No significant changes in hematocrit or hemoglobin were detected, and there was no evidence of thrombosis as evaluated clinically and by sensitive molecular markers. It was concluded from both the retrospective and prospective data that monoclonal antibody-purified factor IX concentrate in combination with an antifibrinolytic agent does not activate the coagulation cascade and is a safe and effective treatment for prevention and control of oral bleeding in hemophilia B patients.

Aminocaproates↗
PubMed1970

Histological localization of plasminogen activator and proteolytic activity in the human stomach and duodenum.

Plasminogen activator activity has been localized in gastric and duodenal tissue using a histological technique. This activity could be separated from proteolytic activity by incorporating in-aminocaproic acid into the fibrin substrate or by heat treatment. Plasminogen activator activity was found in relation to mucosal and submucosal blood vessels in the tissues studied. Proteolytic activity was identified in the surface epithelium, the gastric antral and fundal glands, and in the antral submucosal fat. Proximal duodenal tissue contained proteolytic activity in relation to Brunner's glands.

Aminocaproates↗
PubMed2000

A role for a helical connector between two receptor binding sites of a long-chain peptide hormone.

The conformational freedom of single-chain peptide hormones, such as the 41-amino acid hormone corticotropin releasing factor (CRF), is a major obstacle to the determination of their biologically relevant conformation, and thus hampers insights into the mechanism of ligand-receptor interaction. Since N- and C-terminal truncations of CRF lead to loss of biological activity, it has been thought that almost the entire peptide is essential for receptor activation. Here we show the existence of two segregated receptor binding sites at the N and C termini of CRF, connection of which is essential for receptor binding and activation. Connection of the two binding sites by highly flexible epsilon-aminocaproic acid residues resulted in CRF analogues that remained full, although weak agonists (EC(50): 100-300 nM) independent of linker length. Connection of the two sites by an appropriate helical peptide led to a very potent analogue, which adopted, in contrast to CRF itself, a stable, monomer conformation in aqueous solution. Analogues in which the two sites were connected by helical linkers of different lengths were potent agonists; their significantly different biopotencies (EC(50): 0.6-50 nM), however, suggest the relative orientation between the two binding sites rather than the maintenance of a distinct distance between them to be essential for a high potency.

Adrenocorticotropic Hormone↗
PubMed1988

Severe hemoptysis associated with pulmonary aspergilloma. Percutaneous intracavitary treatment.

Surgical therapy for massive hemoptysis associated with pulmonary aspergilloma carries a high morbidity and mortality in patients with limited pulmonary reserve. Bronchial artery embolization has proven ineffective in treating and in preventing recurrent episodes of hemoptysis in this group of patients. Over a four-and-one-half year period, we have successfully treated six episodes of acute hemoptysis in four patients using a percutaneously placed catheter and intracavitary instillation of amphotericin B, N-acetylcysteine, and aminocaproic acid. Advantages of this method of treatment for patients with severely compromised pulmonary reserve include: (1) no further loss of lung function; (2) ease and rapidity of catheter insertion; (3) prompt response to treatment; (4) relatively short hospitalization; and (5) ability to repeat the procedure in the same or another cavity if necessary.

Acetylcysteine↗
PubMed1991

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form.

A discontinuous electrophoretic system for the isolation of membrane proteins from acrylamide gels has been developed using equipment for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Coomassie dyes were introduced to induce a charge shift on the proteins and aminocaproic acid served to improve solubilization of membrane proteins. Solubilized mitochondria or extracts of heart muscle tissue, lymphoblasts, yeast, and bacteria were applied to the gels. From cells containing mitochondria, all the multiprotein complexes of the oxidative phosphorylation system were separated within one gel. The complexes were resolved into the individual polypeptides by second-dimension Tricine-SDS-PAGE or extracted without SDS for functional studies. The recovery of all respiratory chain complexes was almost quantitative. The percentage recovery of functional activity depended on the respective protein complex studied and was zero for some complexes, but almost quantitative for others. The system is especially useful for small scale purposes, e.g., separation of radioactively labeled membrane proteins, N-terminal protein sequencing, preparation of proteins for immunization, and diagnostic studies of inborn neuromuscular diseases.

Aminocaproates↗
PubMed1993

Gelatinolytic and caseinolytic proteinase activities in human prostatic secretions.

Seminal fluid contains a number of proteinase activities, many of which are secreted by the prostate gland. Our objective was to determine proteinase activities in human prostatic secretions which can degrade gelatin and/or casein. Prostatic secretions were collected by prostate massage from men with benign prostatic hyperplasia prior to surgery to relieve obstruction. Significant proteinase activities towards gelatin of about 81, 86, 94, 111, 115 and 163 Kd as well as less active forms of 23, 36, 38, 132, 137, and 148 Kd were detected using protein substrate-polyacrylamide gel zymography. In addition, Ca2+ stimulated activities of approximately 64, 66, 71 and 76 Kd; however, EDTA and EGTA inhibited all activities but the 23, 36 and 38 Kd forms (these were inhibited by benzamidine and epsilon-amino caproic acid). This suggests that the gelatinolytic activities of 64 Kd and greater were metalloproteinases and those of 23, 36, and 38 Kd were serine proteinases. Significant caseinolytic activities of 22, 25, 35, 37, 57, 90, 96, 102 and 116 Kd were found as well as several less active forms and a 12 Kd activity stimulated by Ca2+. Caseinolytic activities of 12, 14, 16, 96, 102, 116, and 126 Kd were inhibited by EDTA and EGTA indicating they are metalloproteinases. The 35, 37, 57 and 58 Kd caseinolytic activities were inhibited by benzamidine, and the 57 and 58 Kd forms by epsilon-aminocaproic acid suggesting they were serine proteinases. There was considerable variability among individuals in the molecular forms of proteinase activity expressed as well as the level of their activity. A significant decrease in the frequency of expression of the 132 Kd gelatinolytic activity was found in secretions from men with atypia or adenocarcinoma, as compared with men with benign prostatic hyperplasia alone. Our results show that human prostatic secretion contains a variety of proteinase activities. The expression of the 132 Kd gelatinolytic activity could prove useful in further evaluation of neoplastic prostatic disease.

Caseins↗