PubMed · 4626529
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J Grossman, G N Abraham, J P Leddy, J L Condemi. 1972. Crystalglobulinemia.. https://doi.org/10.7326/0003-4819-77-3-395
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We report a case of pseudothrombocytopenia due to platelet cold agglutinins. Platelet counts were decreased in blood drawn in a tube without anti-coagulant just after withdrawal as well as in blood drawn in a tube with anti-coagulant, such as EDTA-2K, MgSO4, citrate or heparin. In our case, platelet aggregates were noted on blood-smear made from blood samples obtained with and without anti-coagulant. RBC and WBC counts were within the normal range. Platelet aggregates mainly consisted of 2-5 platelets. Patient plasma agglutinated normal platelets at a temperature below 10 degrees C. Immunoglobulin class was determined as IgM by flow cytometry.
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Mechanisms of the cryoprecipitation of cryoglobulins have long been studied but not fully understood. In the present study, we characterize a monoclonal immunoglobulin G1 (IgG1) cryoglobulin that forms sharp needle crystals upon cooling and therefore might be an ideal example for the elucidation of a mechanism of cryoprecipitation of cryoglobulins. Limited proteolysis by papain of this cryoglobulin resulted in disappearance of cryocrystallization. Interactions of the proteolytic fragments were examined by surface plasmon resonance measurements. A temperature-dependent isologous Fab-Fab interaction was observed for this cryoglobulin. Glycosylation profiling by use of the HPLC mapping technique revealed that cryoglobulin expresses homogeneous N-glycans in its Fc portion. These results suggest that (1) the temperature-dependent crystallization of the cryoglobulin was ascribed to its specific Fab-Fab interaction and (2) the unusual homogeneity of the Fc glycosylation promote the crystallization of this cryoglobulin.