Proteolytic Cleavage of Chromogranin A (CgA) by Plasmin
نویسندگان
چکیده
منابع مشابه
Chromogranin A (CgA) References
"There appears to be a direct correlation between tumor burden and serum CgA levels. Rising serum levels of CgA can predeed radiographic evidence of recurrence. . . . .Using serum CgA level above 30 U/ml, one is able to discriminate between disease free patients and those with recurrent metastatic disease with a sensitivity of 92% and specificity of 96%. This is superior to measuring urinary 5-...
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Introduction: Adrenal tumours can produce specific hormones and cause characteristic symptoms. The majority of adrenal incidentalomas are clinically silent, but some may be malignant or pose other potential threats to life. Chromogranin A (CgA) is the main, nonspecific marker of neuroendocrine tumours (NET). In the adrenals, CgA is produced by chromaffin cells localised in the adrenal medulla. ...
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The plasminogen/plasmin system is involved in a variety of normal physiological and pathological processes, including tissue remodelling, angiogenesis and tumour metastasis. Plasminogen activators and receptors for plasminogen/plasminogen activators are essential for the processing of plasminogen to form the active serine protease plasmin. Plasmin can in turn positively or negatively regulate f...
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C1r was unable to cleave and activate proenzyme C1s unless first incubated at 37 degrees C in the absence of calcium before the addition of C1s. The acquisition of ability to activate C1s was associated with, and paralleled by, cleavage of each of the two noncovalently bonded 95,000 dalton chains of the molecule into disulfide linked subunits of 60,000 and 35,000 daltons, respectively. Thus, C1...
متن کاملProcessing of chromogranin A by plasmin provides a novel mechanism for regulating catecholamine secretion.
Chromogranin A (CgA) is the major soluble protein in the core of catecholamine-storage vesicles and is also distributed widely in secretory vesicles throughout the neuroendocrine system. CgA contains the sequences for peptides that modulate catecholamine release, but the proteases responsible for the release of these bioactive peptides from CgA have not been established. We show here that the m...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m101545200