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PubMed1977

The binding and cleavage characteristics of human Hageman factor during contact activation. A comparison of normal plasma with plasmas deficient in factor XI, prekallikrein, or high molecular weight kininogen.

The ability of human Hageman factor (coagulation factor XII) to bind to a glass surface and its susceptibility to limited proteolytic cleavage during the contact activation of plasma have been studied using normal human plasma and plasmas genetically deficient in factor XI, prekallikrein, or high molecular weight kininogen (HMWK). When diluted normal plasma containing (125)I-Hageman factor was exposed to a glass surface for varying times, the Hageman factor was found to bind to the surface, and within 5 min became maximally cleaved from its native 80,000 mol wt to yield fragments of 52,000 and 28,000 mol wt. Hageman factor in factor XI-deficient plasma behaved similarly. In prekallikrein-deficient plasma, the binding of Hageman factor to the glass surface occurred at the same rate as in normal plasma but the cleavage was significantly slower, and did not reach maximum until 60 min of incubation. Cleavage of Hageman factor in HMWK-deficient plasma occurred at an even slower rate, with greater than 110 min of incubation required for maximal cleavage, although the rate of binding to the glass was again the same as in normal plasma. Normal rates of cleavage of Hageman factor were observed for the deficient plasmas after reconstitution with purified human prekallikrein or HMWK, respectively. These observations suggest that normal contact activation in plasma is associated with proteolytic activation of surfacebound Hageman factor. The cleavage of the surface-bound Hageman factor molecule responsible for the formation of the 52,000-and 28,000-mol wt fragments occurred at two closely situated sites, one of which was within a disulfide loop. Cleavage at the site external to the disulfide bond resulted in the release from the surface of the 28,000-mol wt fragment. Cleavage at the site within the disulfide loop resulted in the formation of a 28,000-mol wt fragment which remained surface bound, presumably by virtue of the disulfide linkage to the larger fragment.

Blood Coagulation Disorders↗

PubMed1994

Diabetic GK rat plasma but not normal Wistar rat plasma induces insulin-stimulated DNA synthesis in primary cultured smooth muscle cells in GK rat aorta.

We investigated the effect of diabetic plasma on insulin-stimulated DNA synthesis in primary cultured aortic smooth muscle cells (SMC) of the GK rat, a model of non-insulin-dependent diabetes mellitus, and compared it with that of Wistar normal rat plasma. We measured the incorporation of 3H-thymidine into cultured SMC. The diabetic plasma (3%) of GK rat, but neither the plasma (3%) of Wistar normal rat nor the plasma (3%) (not containing both insulin-like growth factor-I (IGF-I) and corticosterone) of Wistar hypophysectomized rat induced insulin-stimulated DNA synthesis in GK rat SMC. The responsiveness of SMC to insulin, not to IGF-I, was decreased remarkably by the diabetic state. The diabetic plasma of GK rat remarkably enhanced and the plasma of Wistar hypophysectomized rat weakly enhanced insulin-stimulated DNA synthesis in Wistar normal rat SMC. Corticosterone (20 nM) increased insulin-stimulated DNA synthesis in GK rat SMC but decreased it in Wistar normal rat SMC, using the plasma of Wistar hypophysectomized rat. Corticosterone levels were lower in GK rat plasma than in normal Wistar rat plasma. These results demonstrate that the enhancement of insulin-stimulated DNA synthesis in diabetic SMC by the diabetic plasma of GK rat may be due to neither IGF-I nor corticosterone but due to other factors.

Animals↗

PubMed2006

Changes of fructose concentrations in seminal plasma and glucose and testosterone concentrations in blood plasma in rams over the course of a year.

The present study was performed to examine seasonal changes in the fructose concentrations of seminal plasma and glucose and testosterone concentrations of blood plasma over the course of a year (from November 2004 to November 2005) using 5 Suffolk rams. Osmolality of the seminal plasma was also measured. The fructose concentrations in the seminal plasma increased as the breeding season approached, with the maximum in October (179.8 mg/dl) and the minimum in May (6.9 mg/dl), although there were no significant differences during the year. Osmolality of the seminal plasma in February (304 mOsm) was significantly (P<0.05) lower than in January (325 mOsm), July (327 mOsm), and August (325 mOsm). It was also significantly (P<0.05) lower in November (308 mOsm) than in January and August. The blood plasma glucose concentration in October (79.3 mg/dl) was significantly (P<0.05) higher than in January and February (43.2 and 43.7 mg/dl, respectively). The blood plasma testosterone (T) concentrations were significantly (P<0.05) higher in September (8.5 ng/ml) and October (10.2 ng/ml) than in other months. The fructose concentrations in the seminal plasma appeared to be related to the glucose and T concentrations in the blood plasma. These results show that fructose concentrations in the seminal plasma and blood plasma glucose and T concentrations tended to increase during the breeding season, with the highest concentrations in October.

Animals↗

PubMed1992

Changes in plasma vasopressin concentration and plasma osmolality in relation to age and time of day in the male Wistar rat.

The influence of age on several parameters related to water balance was studied in Wistar rats. Plasma AVP concentration and plasma osmolality were increased at midday in 21-month-old rats as compared with 3- and 4-month-old rats. Daily water intake per 100 g body weight was reduced in 14- and 21-month-old rats as compared with 3- and 4-month-old rats, but total water intake was unaltered. These results suggest that there is a change in water balance in Wistar rats with age. In order to obtain information about the influence of age on daily fluctuations in plasma AVP concentration and osmolality these parameters were determined in 4-month-old Wistar rats sacrificed at 2 h intervals during the day and in 20- and 31-month-old rats sacrificed at 8 h intervals. Plasma AVP concentrations were low during the light period and high during the dark period in 4-month-old rats. The relationship between plasma osmolality and plasma AVP concentration was dependent on the time of day in 4-month-old-rats. Plasma AVP concentrations were higher at 16.00 than at 08.00 and 24.00 in 20-month-old rats, and higher at 24.00 than at 08.00 and 16.00 in 31-month-old rats. In contrast to the plasma AVP concentration during the light period, the average daily AVP concentration (average of plasma AVP concentrations at 08.00, 16.00 and 24.00) was increased in 31-month-old rats only. The relationship between plasma osmolality and plasma AVP concentration was not age-related.(ABSTRACT TRUNCATED AT 250 WORDS)

Aging↗

PubMed1994

The relationship between plasma osmolality and plasma vasopressin concentration is altered in old male Lewis rats.

Kidney dysfunction has been observed in aged humans and rats, the primary cause of which may reside in the kidney itself or in the hypothalamus. The latter possibility is suggested by the increased release of AVP in response to salt infusion in humans. The effect of age on the relationship between plasma osmolality and plasma AVP concentration has never been verified in an animal model. Therefore, in the present study, 9% salt solution was infused into adult and aged Lewis rats, and plasma AVP concentration and osmolality were measured. Basal plasma AVP concentration, osmolality and total water intake were not altered in aged Lewis rats as compared with adult animals, indicating the absence of overt disturbances in water homeostasis. Infusion of 9% salt solution resulted in a linear increase in plasma osmolality in both adult and aged rats. Plasma osmolality increased more with time in aged animals than in adult animals, suggesting an age-related difference in kidney function during salt infusion. Plasma AVP concentration increased 50% less with osmolality at relatively low osmolalities, but not at relatively high osmolalities. The altered relationship between plasma osmolality and plasma AVP concentration in rats with age may be related to changes in neurons monitoring osmolality or to changes in baroreflex regulation. The data suggest that reduced kidney function with age does not result from an altered relationship between plasma osmolality and plasma AVP concentration.

Aging↗

PubMed1992

Changes in plasma catecholamine, free fatty acid, and glucose concentrations, and plasma monoamine oxidase activity before and after feeding in laying hens.

In order to better understand the relationship of free fatty acid (FFA) concentrations to feed intake in laying hens, plasma levels of catecholamine, glucose, and FFA and plasma monoamine oxidase activity were measured. Blood samples were taken in the morning before and after the start of feeding via chronic brachial vein catheters. Plasma concentrations of epinephrine and norepinephrine were analyzed by modified HPLC with an electrochemical detection method. Plasma concentrations of FFA and glucose were not significantly different before and after the start of feeding, however a negative correlation (r = -.763, r2 = .582, P less than .01) between these parameters was observed. No significant correlations between the plasma concentration of FFA and plasma concentrations of epinephrine or norepinephrine before and after the start of feeding were observed. However these were significantly correlated (r = .444, r2 = .197, P less than .05 for FFA and epinephrine; r = .787, r2 = .619, P less than .01 for FFA and norepinephrine) when the behavioral activity of hens was low, such as in resting or feeding. Plasma activity of monoamine oxidase was not different before and after the start of feeding, and no relationship was observed between plasma monoamine oxidase activity and plasma epinephrine or norepinephrine concentration. It is suggested that the increase in plasma FFA concentration before feeding would be elicited by the increase in the circulating epinephrine and norepinephrine concentrations. Plasma FFA concentration was not affected by the increase in circulating epinephrine and norepinephrine concentrations during active behavior such as pacing and egg call before and after oviposition.

Animals↗

PubMed1975

[Plasma renin activity, plasma aldosterone and electrolyte balance in the postoperative period (author's transl)].

Plasma renin-activity and plasma aldosterone were measured by radioimmunoassay in 15 female patients before and 16 hours after intraabdominal surgery. Plasma renin was increased in all patients and plasma aldosterone in 12 patients after operation. Plasma renin and plasma aldosterone were correlated significantly (r=0.66, p less than 0.01) in the whole group. The increase of renin and plasma aldosterone was correlated inversely to urinary sodium-potassium-ratio. In 5 patients the increase of plasma renin and plasma aldosterone could not be prevented by the intra- and postoperative administration of 360 mEq of sodium, which was consequently retained. It is proposed that postoperative hyperaldosteronism is at least partly mediated through the renin-angiotensin-system. An absolute or relative sodium deficit appears to be an unlikely explanation for the stimulation of the renin-angiotensin-system in the postoperative period. The postoperative increase of plasma renin and consequently plasma aldosterone is possibly a consequence of anaesthetic induced impaired kidney perfusion and/or catecholamine mediated stimulation of renin release.

Adrenal Glands↗

PubMedDate not supplied

In vitro metabolic degradation of a bovine growth hormone-releasing factor analog Leu27-bGRF(1-29)NH2 in bovine and porcine plasma. Correlation with plasma dipeptidylpeptidase activity.

A bovine growth hormone-releasing factor analog, Leu27-bGRF(1-29)NH2, was rapidly hydrolyzed to Leu27-bGRF(3-29)NH2 when incubated at 0.03 mM with porcine and bovine plasma at 37 degrees C in vitro (t1/2 = 8.4 min and 22.1 min, respectively). The site of cleavage was the same as that reported by Frohman et al. (J. Clin. Invest. 78, 906-913, 1986) for the GRF/human plasma system and was suggested by the authors to be due to the presence of dipeptidylpeptidase IV (DPP-IV) in human plasma. The DPP-IV-like activity of porcine plasma, determined with Gly-Pro-p-nitroanilide as substrate at pH 7.6 was about 2- to 3-fold higher than that of bovine plasma and seems to correlate well with the more rapid degradation of the GRF analog in porcine plasma. The hormone half-life was extended to 83.3 min when Leu27-bGRF(1-29)NH2 was incubated in vitro with bovine plasma in the presence of an equimolar amount of diprotin A (a competitive DPP-IV inhibitor). Dipeptidylpeptidase II-like activity of porcine and bovine plasma (which may overlap with substrate specificity of DPP-IV) was measured with Lys-Ala-beta-naphthylamide and at pH 7.6 was found to be relatively low (3% and 21% of the corresponding plasma DPP-IV activities). Tyr-beta-naphthylamide was hydrolyzed slowly by porcine plasma and not degraded at all by bovine plasma, which suggests that the sequential cleavage from the GRF N-terminus starting with Tyr at position 1 is not dominant.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗

PubMed1985

Plasma decay of chylomicron remnants is not affected by heparin-stimulated plasma lipolytic activity in normal fasting man.

In an earlier study it was shown that retinyl palmitate appeared to be a satisfactory label for the core of chylomicrons and their remnants. When chylomicrons were endogenously labeled with retinyl palmitate and pulse-injected into healthy donors, retinyl palmitate was cleared from plasma by a first order process. Its fractional decay constant was very similar to the fractional catabolic rate of VLDL triglycerides, a lipoprotein lipase-dependent process, and 2-3 times slower than hepatic chylomicron remnant uptake in experimental animals. We, therefore, investigated whether plasma clearance of retinyl palmitate-labeled chylomicrons is accelerated by enhanced plasma triglyceride hydrolysis produced by heparin administration. Five healthy subjects took retinyl palmitate by mouth and 5-6 hr later two units of plasma were obtained by plasma-pheresis. After storage for 42 hr, the units were pooled and separated into two equal volumes. The first half was injected into the donor and plasma retinyl palmitate and chylomicron triglyceride were measured for 3.5 hr (control study). Heparin was then given intravenously as a bolus followed by an infusion for 7 hr. A second retinyl palmitate clearance (postheparin study) was performed during the heparin infusion. Plasma lipolytic activity and retinyl palmitate and chylomicron triglyceride concentrations were measured serially. Total plasma lipolytic activity and hepatic triglyceride lipase activity were increased approximately 500-fold during postheparin studies, enhancing triglyceride decay 2.5- to 3-fold. Retinyl palmitate plasma decay, however, was unaffected. Retinyl palmitate plasma decay was a biexponential concentration-dependent function in eighty of ten pre- and postheparin studies with the first, rapid exponential accounting for 90 +/- 4% of total plasma retinyl palmitate decay.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1982

Effects of chemical sympathectomy on the increases in plasma catecholamines and dopamine-beta-hydroxylase induced by forced immobilization and insulin-induced hypoglycemia: origin and fate of plasma dopamine-beta-hydroxylase.

The effect of acute stresses on plasma norepinephrine, epinephrine and dopamine-beta-hydroxylase (DBH) were evaluated in control and 6-hydroxydopamine-treated, awake cannulated guinea pigs. Forced immobolization for 1 hr caused a 3- and 5-fold increase in plasma DBH and norepinephrine, respectively. Pretreatment with 6-hydroxydopamine (23 mg/kg b.wt.i.a., 72 and 48 hr before stress) reduced by 70% the increase in plasma DBH and totally prevented the rise in plasma catecholamines evoked by the restraining stress. Injection of insulin (5 U/kg b.wt.i.a.) induced a 60% decrease in blood glucose, a 1-fold increase in plasma DBH and a selective 4-fold increase in plasma epinephrine; these effects were not modified by chemical sympathectomy. Our results indicate that forced immobilization and hypoglycemia produce a preferential activation of the sympathetic postganglionic nerves and of the adrenal medulla, respectively, and that in guinea pigs both stresses increase plasma DBH. The kinetics of disappearance of plasma DBH were studied after subjecting the guinea pigs for 1 hr to forced immobilization. Although 7 of 12 animals showed a biphasic rate of fall of plasma DBH, in each case there was a rapid initial fall possibly due to the "distribution" of the enzyme with a T1/2 of 1.65 hr. Similar findings were observed in 6-hydroxydopamine-treated guinea pigs. These results suggest that the distribution of DBH is the most important process in reducing the augmented plasma DBH levels elicited by a short-term stress and that this process is not dependent on the integrity of the sympathetic nerves nor on the adrenal or sympathetic origin of the enzyme. This study supports the view that the ratio, content of releasable DBH present in sympathetic nerves and adrenal glands/total circulating pool of DBH, is the factor that determines whether an increase in plasma DBH would occur in animals exposed to an acute stress.

Animals↗

PubMed1998

Thrombomodulin in human plasma contributes to inhibit fibrinolysis through acceleration of thrombin-dependent activation of plasma procarboxypeptidase B.

Thrombomodulin (TM) expressed on endothelial cells binds thrombin and initiates anticoagulant pathways. Soluble functional proteolytic fragments of TM are also present in circulating plasma. Recently, it was reported that TM accelerated thrombin-dependent plasma procarboxypeptidase B (pro-pCPB) activation in a purified system and suggested that TM may inhibit fibrinolysis in crude plasma. The aim of present study was to evaluate any functional role of soluble TM fragments in plasma or purified TM added into plasma to the regulation of coagulation and fibrinolysis. Addition of rabbit TM (1-200 ng/ml) to plasma resulted in a concentration-dependent prolongation of urokinase (UK)- or tissue plasminogen activator (t-PA)-induced clot lysis time. The concentration of TM required for the inhibition of fibrinolysis was lower than that required for the inhibition of coagulation. Addition of anti-rabbit TM IgG or anti-human TM IgG into plasma reduced UK- or t-PA-induced clot lysis time without affecting clotting times, indicating that exogenous TM or soluble TM fragments in normal human plasma participated in regulation of fibrinolysis. Moreover, the TM-dependent inhibition of fibrinolysis was observed only in the presence of thrombin and blocked by addition of carboxypeptidase B inhibitors, but not mediated by protein C activation or direct inhibition of UK, t-PA or plasmin. Analysis of various substrates and inhibitors indicated that TM accelerated thrombin-dependent pro-pCPB activation in plasma. The present results indicate that TM, including soluble TM fragments in plasma, inhibit fibrinolysis via activation of pro-pCPB in plasma.

Animals↗

PubMed1984

Efficacy of several plasma components in a young boy with chronic thrombocytopenia and hemolytic anemia who responds repeatedly to normal plasma infusions.

This report describes a patient with thrombocytopenia, microangiopathic hemolytic anemia, proteinuria, and microscopic hematuria that could be transiently improved by the infusion of plasma or various plasma components. An increase in platelet count following the transfusion of normal plasma was predictable and reproducible. In therapeutic trials with commercially available plasma components, factor VIII preparations were effective for inducing an increase in the platelet count and improving hemolytic anemia, but albumin, gamma-globulin, factor IX, and fibronectin preparations were ineffective. Serum from normal donors also relieved the symptoms of this condition in our patient. Partial plasma exchange (1,000 ml/m2 of body surface area) was performed with albumin instead of normal plasma, but there was no significant effect on platelet count or anemia. Large, multimeric von Willebrand factor components of the factor VIII complex (VIII/vWF) were found in the patient's plasma when his platelet count was normal, but their levels were reduced when the platelet count was decreased. The multimers of the patient's plasma were larger than those in normal plasma, but smaller than those in normal platelet lysate. Although the pathogenesis of this disease remains unknown, we conclude that transfusions of normal plasma, serum or factor VIII concentrate provide a factor that causes significant improvement in the thrombocytopenia and hemolytic anemia. Furthermore, large VIII/vWF multimers are possibly directly involved in pathogenesis of this disease.

Anemia, Hemolytic, Congenital↗

PubMed1990

Alpha- and gamma-tocopherol in plasma, red blood cells, and platelets during plasma exchange.

The effect of a rapid reduction of plasma lipoproteins on the alpha- and gamma-tocopherol levels in plasma, erythrocytes, and platelets was studied. Sixteen successive plasma exchange procedures performed weekly in an adult with heterozygous familial hypercholesterolemia were evaluated. Plasma exchange was done by intermittent flow centrifugation, exchanging one plasma volume against a 4% human albumin solution. Plasma exchange reduced in plasma alpha-tocopherol from 41.5 +/- 8.9 to 23.6 +/- 4.8 mumol/L and gamma-tocopherol from 4.9 +/- 4.1 to 2.4 +/- 2.1 mumol/L, without changing their ratios to total lipids. It diminished alpha-tocopherol in platelets from 12.97 +/- 4.37 to 10.03 +/- 1.78 mumol/10(13) cells and gamma-tocopherol from 1.43 +/- 0.55 to 1.06 +/- 0.41 mumol/10(13) cells, but did not affect erythrocyte tocopherols. The total amount removed per procedure was 47.57 +/- 13.65 mumol for alpha-tocopherol and 4.70 +/- 3.59 mumol for gamma-tocopherol. Plasma exchange increased the number of erythrocytes from 3.67 +/- 0.10.10(12) to 4.05 +/- 0.13.10(12) cells/L, without affecting their volume. Platelet count did not change, but mean platelet volume decreased from 7.7 +/- 0.5 to 6.9 +/- 0.5 fl and platelet distribution width from 15.1 +/- 0.4 to 14.9 +/- 0.5. Thus, plasma exchange reduces plasma alpha- and gamma-tocopherol to the same extent as total lipids, and decreases these tocopherols in circulating platelets, along with a reduction in platelet size and, compared to the change in erythrocyte count, a fall of platelet number.(ABSTRACT TRUNCATED AT 250 WORDS)

Blood Platelets↗

PubMed1986

The incidence of phagocytizing plasma cells in malignant plasma cell dyscrasias.

Bone marrow smears from 401 patients with malignant plasma cell disorders (MPCD) were examined to evaluate the incidence of phagocytosis by plasma cells and to elucidate the pathogenesis of this phenomenon. Phagocytizing plasma cells were observed in 6 patients (1.6%), 1 of whom had plasma cell leukaemia, from a pool of 382 patients with multiple myeloma that included 7 with plasma cell leukaemia, but not in those with other types of MPCD. In 1 of the 6 cases, the plasma cells acquired phagocytizing ability in the terminal stage of the illness. The incidence of phagocytizing plasma cells in multiple myeloma was higher than might have been expected, judging from a small number of previous reports concerning phagocytosis by plasma cells. The incidence of phagocytizing plasma cells in plasma cell leukaemia (1:7) was not statistically greater than that in non-leukaemic multiple myeloma (5:375).

Humans↗

PubMed1987

Estimation of plasma volume from hematocrit and plasma oncotic pressure during volume expansion in dogs.

Changes in hematocrit and plasma oncotic pressure were measured continuously during and after isotonic volume expansion in splenectomized dogs in order to test the potential of these types of measurements to predict changes in plasma volume. A volume of Ringer's solution amounting to 15% of the initial blood volume was infused over 10 min. At the end of the infusion, 54% of infused fluid remained within the intravascular space and 9% of the infused volume was retained within the intravascular space at 50 min after the end of the infusion. Hematocrit and plasma oncotic pressure decreased by 2.4% and 2.4 mmHg, respectively, at the end of infusion and then variables returned to their control levels gradually. Changes in plasma volume were estimated indirectly from hematocrit and plasma oncotic pressure based on the dilution of the erythrocytes and the protein. Highly significant correlations were observed between the measured plasma volume (Y) and the plasma volume (X) calculated from hematocrit (Y = 0.95X + 0.22, r = 0.96) and the plasma oncotic pressure (Y = 0.86X + 0.46, r = 0.91). We therefore conclude that either hematocrit and plasma oncotic pressure measured continuously are reliable parameters for predicting the time course of the plasma volume change during an isotonic volume expansion of up to 15% of the initial blood volume.

Animals↗

PubMed1990

Human seminal plasma Zn-alpha 2-glycoprotein: its purification and properties as compared with human plasma Zn-alpha 2-glycoprotein.

On the basis of the datum that the level of Zn-alpha 2-glycoprotein (Zn alpha 2gp) in human seminal plasma was about 6-times higher than that in adult serum, Zn alpha 2gp was purified from fresh human seminal plasma approx. 70-fold with 60% yield over seminal plasma by DEAE-Sephacel, Zn-chelate Sepharose 4B and DEAE-5PW column chromatographies. The molecular weight of seminal plasma Zn alpha 2gp was 50,000 on Superose column chromatography, and 40,500 and 41,500 on SDS-polyacrylamide gel electrophoresis in the absence and presence of beta-mercaptoethanol, respectively. Plasma Zn alpha 2gp is a glycoprotein, while the protein from seminal plasma does not contain carbohydrate. The amino acid sequence of the first 17 residues of seminal plasma Zn alpha 2gp was Glu-Asn-Gln-Asp-Gly-Asn-Tyr-Ser-Leu-Thr-Tyr-Ile-Tyr-Thr-Gly-Leu-Ser. This sequence was completely identical with the amino acid residues from Glu-2 to Ser-18 in the N-terminal amino acid sequence of plasma Zn alpha 2gp. These data suggest that both Zn alpha 2gps in plasma and seminal plasma may be expressed from one gene, but their posttranslational modifications are different.

Adult↗

PubMedDate not supplied

Thawed plasma an alternative to fresh frozen plasma.

Thawed plasma contains all of the clotting factors that Fresh Frozen Plasma contains with the exception of lower levels of Factor V and Factor VIII. Thawed plasma still has significant levels of factors to enhance coagulation. The purpose of our review was to decrease wastage and cost of fresh frozen plasma by utilizing thawed plasma and to encourage use of thawed plasma in place of fresh frozen plasma. Sources of information included our Blood Bank wastage data and cost analysis per unit. By educating the Trauma Service and Anesthesia and Emergency Services regarding the availability of thawed plasma versus fresh frozen plasma, the University Medical Center significantly decreased wastage of fresh frozen plasma after the program was initiated.

Blood Coagulation Factors↗

PubMed2005

Increased activity of plasma and tissue kallikreins, plasma kininase II and salivary kallikrein in pemphigus foliaceus (fogo selvagem).

BACKGROUND: Pemphigus foliaceus (PF) is an autoimmune blistering disease of unknown aetiology, which is endemic in Brazil. Although the pathogenesis of PF is still unknown, proteins of the contact system have been implicated. OBJECTIVES: As the components of the kinin system may interact with those of the contact system, in this study we evaluated the plasma levels of high-molecular-weight kininogen (HK) and low-molecular-weight kininogen (LK), and the activity of plasma kallikrein, tissue kallikrein and kininase II in plasma of patients with PF presenting with Nikolsky's sign. As kidneys and salivary glands are relevant sources of tissue kallikrein for plasma, we also evaluated urinary/salivary kallikrein and urinary kininase II activities. METHODS: Fifteen patients and 15 age- and sex-matched controls were studied. Kininogen levels were determined by enzyme-linked immunosorbent assay, and the activities of kallikreins and kininase II were determined using selective chromogenic substrates. RESULTS: Compared with controls, plasma HK levels were decreased (P = 0.031), whereas the activities of plasma kallikrein, tissue kallikrein and kininase II in plasma, and the activity of salivary kallikrein, were increased in patients (P < 0.001 for each comparison). Plasma levels of LK and the activities of urinary kallikrein and urinary kininase II were not significantly different from controls. CONCLUSIONS: Diminished levels of HK associated with increased activities of plasma kallikrein and kininase II indicate that the kinin system is activated at the systemic level in PF. As active plasma kallikreins may act on some proteins of the contact system, it is possible that the enzyme may contribute to blister formation. The further observation of an increased tissue kallikrein activity at the systemic and saliva levels may be interpreted as a systemic reflex of skin inflammation. Whether the activation of the kinin system is a cause or a consequence of blister formation needs further clarification.

Adolescent↗