Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02774 (Gc-globulin)
 196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The development of new analytic and preparative techniques in the field of protein chemistry has essentially extended our knowledge about the variety of human plasma proteins in the last 15 years. In many cases plasma proteins have been particularly determined by immunologic techniques, partially highly purified and physicochemically well characterized, before knowing the biological function. To these proteins belong among others the alpha 1-antitrypsin, Cl-inactivator, alpha 2-macroglobulin, Gc-globulin and the cold-insoluble globulin. Today we know more than 100 proteins being isolated from human plasma and among these are nearly 20, of which the biological function is not yet known. To this group are belonging proteins, which are known since many years, like the alpha 1-acid glycoprotein and the C-reactive proteins as well as proteins, which have only been described in the last years and which partially have an interesting chemical structure, e.g. the histidinerich 3,8S-alpha 2-glycoprotein and the leucine-rich 3,1S-alpha 2-glycoprotein, of which every fifth amino acid is formed by leucine. It is to be hoped that the special chemical structure of some of these human plasma proteins as well as the quantitative immunologic determination in different patient sera will give hints to their biological function.
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PMID:Purified human plasma proteins of unknown function. 617 5

Gc-globulin has been found in bronchoalveolar lavage fluid in patients with chronic obstructive pulmonary disease (COPD) and adult respiratory distress syndrome (ARDS) and has been shown to enhance neutrophil chemotaxis to C5-derived peptides in vitro. We proposed that Gc-globulin may enhance the inflammatory response in lungs by influencing monocyte chemotaxis to C5-derived peptides as it does with neutrophils. Monocyte chemotaxis was measured in blind well chambers by a leading-front technique. Purified human Gc-globulin had no intrinsic chemotactic activity for monocytes at concentrations ranging from 1 fM to 1 microM. However, Gc-globulin, at concentrations as low as 10 pM, increased monocyte chemotaxis over 10-fold in a concentration-dependent fashion when added to non-chemotactic doses of C5a (0.1 nM) and C5a des Arg (0.5 nM). The chemotaxis-enhancing effect of Gc-globulin was specific for C5-derived peptides, as Gc-globulin did not enhance monocyte chemotaxis to other chemoattractants such as leukotriene B4 or formyl-Met-Leu-Phe. The enhancement of monocyte chemotaxis to C5-derived peptides by Gc-globulin was not a nonspecific effect of anionic proteins, as other serum proteins of similar size and charge did not enhance monocyte chemotaxis to C5a des Arg. These results indicate that Gc-globulin enhances the monocyte response to C5-derived peptides and, together with previous work, indicates that its presence in the airways of patients with COPD and ARDS may up-regulate the monocyte inflammatory response in the lungs.
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PMID:Human monocyte chemotaxis to complement-derived chemotaxins is enhanced by Gc-globulin. 812 Apr 52