Increased Plasma Proteolytic Activity Due to Arginine Amidase in Patients with Pancreatitis

Gullick, Herbert D.

doi:10.1056/nejm196304182681601

Cited by 25 publications

(7 citation statements)

References 35 publications

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“…griseus (Awad and Wilcox, 1963;Hashizume and Imahori, 1964). Our observations indicate that thrombin also can be included.…”

Section: Discussionmentioning

confidence: 57%

Activation of Chymotrypsinogen-A by Thrombin Preparations^*

Engel¹,

Alexander²

1966

Biochemistry

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Earlier demonstration that thrombin resembles trypsin in the ability to convert trypsinogen and plasminogen to their respective proteases prompted investigation of its effect on chymotrypsinogen A. Purified thrombin added to the zymogen induced rapid and progressive appearance of esterolytic activity toward acetyltyrosyl ethyl ester. The addition of indole to the zymogen-thrombin mixture after interaction had proceeded obviated esterolysis, indicating that the evolved activity was due to chymotrypsin. Elaboration of the active enzyme from its precursor appeared to take place in accord with enzyme kinetics, the thrombin functioning enzymatically on the zymogen. That this was not due to a possible trypsin contaminant of the thrombin was demonstrated with appropriate inhibitors, by procedures known to block thrombic action, and by separation of certain known contaminants, which T hrombin resembles trypsin in many enzymatic properties (Sherry and Troll, 1954; MiUer and Van Vunakis, 1956;Gladner and Laki, 1956; Laki et al., 1958;Martin et al., 1959;Ronwin, 1960;Laki and Gladner, 1964;Sherry et al., 1965; KCzdy et al., 1965), including the ability to activate trypsinogen and plasminogen (Engel et al., 1966). Since cleavage of the ester and peptide bonds of many synthetic substrates (Ehrenpreis et al., 1957;Lorand et al., 1962;Elmore and Curragh, 1963; Baird ef al., 1965) and proteins1 are catalyzed by both enzymes, and since trypsin activates chymotrypsinogen, the question whether thrombin can similarly activate this zymogen was explored.

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“…griseus (Awad and Wilcox, 1963;Hashizume and Imahori, 1964). Our observations indicate that thrombin also can be included.…”

Section: Discussionmentioning

confidence: 57%

Activation of Chymotrypsinogen-A by Thrombin Preparations^*

Engel¹,

Alexander²

1966

Biochemistry

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“…Subsequently, activation of complement cascade leads to the formation of C5a-induced leukocyte, platelet, and fibrin aggregation. This ultimately causes retinal and renal cortical embolization and ischemia, leading to life- and organ-threatening complications, as in our patient [21–23, 30–32]. Endothelin released from damaged vessels also contributes to this process by producing vasospasm, which further aggravates ischemia.…”

Section: Discussionmentioning

confidence: 69%

Purtscher’s retinopathy and renal cortical necrosis: two rare vaso-occlusive complications in a patient with acute pancreatitis: a case report

et al. 2016

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BackgroundPurtscher’s retinopathy and renal cortical necrosis are two rare vaso-occlusive complications of acute pancreatitis. Purtscher’s retinopathy causes sudden impairment of vision, which was first reported in a patient with head trauma. Subsequently, it was also reported as a complication of acute pancreatitis and few other clinical conditions. Acute pancreatitis also rarely causes renal cortical necrosis leading to acute kidney injury. However, the simultaneous presence of both complications is rarely reported.Case presentationA 20-year-old Bengali man presented to our hospital with a history of acute upper abdominal pain, vomiting, anuria, and disorientation. He was ultimately found to have bilateral complete blindness due to Purtscher’s retinopathy and acute kidney injury due to renal cortical necrosis, as sequelae of acute pancreatitis. He became dialysis-dependent, his vision did not recover, and he died 16 months after diagnosis.ConclusionsThis case highlights Purtscher’s retinopathy and renal cortical necrosis might be considered as a recognized pair complication of acute pancreatitis.

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“…Although the nature of these enzymatic factors is as yet unknown, it has been shown that they possess an arginine-amydase activity resembling that of bradykinin and trypsin (Gullick, 1963). It has also become apparent that lecithinase A increases during the course of acute pancreatitis (Zieve and Vogel, 1961).…”

Section: Discussionmentioning

confidence: 99%

“…Recent investigations have clearly shown that the enzymes released during an attack of acute pancreatitis are responsible for producing most of the clinical manifestations of this disease (Nardi, 1959; Thal et al, 1963). Although the nature of these enzymatic factors is as yet unknown, it has been shown that they possess an arginine-amydase activity resembling that of bradykinin and trypsin (Gullick, 1963). It has also become apparent that lecithinase A increases during the course of acute pancreatitis (Zieve and Vogel, 1961).…”

Section: Discussionmentioning

confidence: 99%

Respiratory failure in acute pancreatitis. I. The biophysical characteristics of lungs in experimental pancreatitis

Bolooki

Minkowitz

Giammona

et al. 1971

Journal of Surgical Oncology

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Four percent of patients with acute pancreatitis develop an acute form of respiratory overwork and die within 24 hr. To elucidate the basic physiology of this respiratory failure in a group of dogs after production of acute pancreatitis, the respiratory functions and mechanics were studied and were compared with dogs undergoing sham operation. The results showed diminished pulmonary tissue recoil accompanied by deficiency in gas exchange after acute pancreatitis. The minute respiratory volume and oxygen uptake were increased in the presence of a large pulmonary venoarterial shunt. This was associated with hypoxemia and carbon dioxide retention which could be corrected with respiratory assistance by using a volume-controlled respirator. I n clinical states any evidence of respiratory overwork and decreased Po2 should be considered as a warning sign of this malignant complication of acute pancreatitis.

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Increased Plasma Proteolytic Activity Due to Arginine Amidase in Patients with Pancreatitis

Cited by 25 publications

References 35 publications

Activation of Chymotrypsinogen-A by Thrombin Preparations^*

Activation of Chymotrypsinogen-A by Thrombin Preparations^*

Purtscher’s retinopathy and renal cortical necrosis: two rare vaso-occlusive complications in a patient with acute pancreatitis: a case report

Respiratory failure in acute pancreatitis. I. The biophysical characteristics of lungs in experimental pancreatitis

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Increased Plasma Proteolytic Activity Due to Arginine Amidase in Patients with Pancreatitis

Cited by 25 publications

References 35 publications

Activation of Chymotrypsinogen-A by Thrombin Preparations*

Activation of Chymotrypsinogen-A by Thrombin Preparations*

Purtscher’s retinopathy and renal cortical necrosis: two rare vaso-occlusive complications in a patient with acute pancreatitis: a case report

Respiratory failure in acute pancreatitis. I. The biophysical characteristics of lungs in experimental pancreatitis

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Product

Resources

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Activation of Chymotrypsinogen-A by Thrombin Preparations^*

Activation of Chymotrypsinogen-A by Thrombin Preparations^*